Compositions and methods for preventing, treating, inhibiting and / or eliminating phytopathogenic infestations and infections

Abstract

The present disclosure provides proteins useful for preventing, treating, inhibiting and / or eliminating infestation and infection of plants caused by various phytopathogenic pests, as well as formulations comprising such proteins, polynucleotides encoding such proteins, organisms expressing such proteins, and methods for preparing such proteins. And methods of using such proteins, formulations, polynucleotides, and organisms in agricultural and other effort areas.

Description

[0001] CROSS-REFERENCE TO RELATED APPLICATIONS

[0002] This application claims priority to International Patent Application No. PCT / US2022 / 073761, filed on July 15, 2022 and published on January 19, 2023 as WO 2023 / 288,294, and U.S. Provisional Application No. 63 / 342,064, filed on May 14, 2022, and U.S. Provisional Application No. 63 / 476,590, filed on December 21, 2022, the disclosures of each of which are incorporated herein by reference in their entirety.

[0003] References to sequence listings

[0004] This application contains a sequence listing in computer readable form. The name of the file containing the sequence listing is SQ.XML, which was created on May 12, 2023, and contains 89,744,839 bytes. This computer readable form is incorporated herein by reference. BRIEF DESCRIPTION OF THE DRAWINGS

[0005] Figure 1 is a table showing significant results of efficacy testing of various enzyme treatments against Blumeria graminis. Results are presented as percent disease control relative to an untreated, uninoculated control (None-Uninoculated Control) and an untreated, inoculated control (None-Inoculated Control) at two time points / disease pressures. 100% control means no disease was detected in the treatment, and 0% control means the disease was at the same level as the untreated inoculated control comparator.

[0006] Figure 2 is a table showing the significant results of the efficacy testing of various enzyme treatments against Botrytis cinerea. The results are presented as the percentage increase in spectral parameters (Fv / Fm, ChIldx and mARI) and the percentage of water-soaked lesions (%WSL) compared to the untreated inoculated control (Non-Inoculated Control).

[0007] Figure 3 Is a table showing significant results of the efficacy testing of various enzyme treatments against Fusarium graminearum. The results are presented as the percent increase in spectral parameters (Fv / Fm, ChIldx and cGFP) compared to the untreated inoculated control (Non-Inoculated Control) after 72 hours.

[0008] Figure 4Table showing the significant results of the efficacy testing of various enzyme treatments on Magnaporthe grisea. Results are presented as half maximal effective concentration (Abs EC) at 612 nm. 50 ; mycelial growth inhibition index) and the half-maximal effective concentration (ex 570nm-em 585nm) of fluorescence after reaction with resazurin (fluorescence EC 50 ; cell viability index).

[0009] Figure 5 is a table showing significant results of efficacy testing of various enzyme treatments against Phakopsora pachyrhizi. Results are presented as the average number of combined Phakopsora pachyrhizi lesions and pustule.

[0010] Fig. 6A , Figure 6B , Figure 6C and Fig.6D is a table showing the significant results of various enzyme treatments tested for efficacy against Phytophthora infestans. The results for the pipette-treated tomato leaf discs are Fig. 6A Results for the spray-treated tomato leaf discs are presented in Figure 6B The results are presented as (-) no disease reduction, (+) mild disease reduction, (++) moderate disease reduction or (+++) extreme disease reduction, and in Figure 6C The results for the spray-treated potato leaf discs are presented as average disease percentages. Fig.6D The average health percentage is presented in .

[0011] Figure 7 is a table showing significant results of efficacy testing of various enzyme treatments against Pseudoperonospora cubensis. Results are presented as (-) no disease reduction, (+) mild disease reduction, (++) moderate disease reduction, or (+++) extreme disease reduction.

[0012] Fig. 8A and Figure 8B Is a table showing significant results of efficacy testing of various enzyme treatments against Zymoseptoria tritici. Results are presented as percent disease control relative to untreated inoculated controls at various time points / disease pressures. 100% control means no disease was detected in the treatment, and 0% control means the disease was at the same level as the untreated inoculated control comparator (Non-Inoculated Control).

[0013] Fig. 9Table showing significant results of various enzyme treatments tested for efficacy against Botrytis cinerea, Fusarium graminearum, Fusarium virguliforme and Pseudomonas aeruginosa. Results are presented as minimum inhibitory concentration (MIC) of mean hyphal branch length and mycelial area. 50 ) (i.e., the minimum enzyme concentration required to inhibit the mean hyphal branch length / total mycelial area to 50% or less of the corresponding untreated control).

[0014] Fig. 10A and Fig. 10B Table showing significant results of efficacy tests of various enzyme treatments against Botrytis cinerea, Fusarium graminearum, Macrocystis cinerea, Penicillium digitatum, Penicillium expansum, Penicillium italicum, Phytophthora infestans and Psoralea corylifolia. Results are presented as (-) no growth inhibition, (+) visible stress response and / or mild growth inhibition, (++) moderate growth inhibition or (+++) extreme growth inhibition.

[0015] Fig.11 is a table showing significant results of testing of the efficacy of various enzyme treatments against leaf-feeding insect larvae. The results are presented as relative growth rates of the larvae after two days of feeding on the treated leaf discs.

[0016] Fig.12 is a table showing significant results of testing of the efficacy of various enzyme treatments against leaf-feeding insect larvae. The results are presented as relative growth rates of the larvae after two days of feeding on the treated leaf discs.

[0017] Fig.13 is a table showing the significant results of the efficacy testing of various enzyme treatments against gray mold (Botrytis cinerea). The results are presented as percent disease.

[0018] Fig.14A and Fig. 14B is a table showing significant results of various enzyme treatments tested for efficacy against Fusarium graminearum. The results are presented as a comparison with the corresponding untreated inoculated controls (Non-inoculated Control; Non-inoculated Silwet TM control; non-inoculated pH 6 buffer control; non-inoculated pH 7 buffer control; non-inoculated pH 8 buffer control).

[0019] Fig.15A and Fig. 15Bis a table showing significant results of various enzyme treatments tested for efficacy against Puccinia striiformis. The results are presented as the area under the disease progression curve.

[0020] Fig.16 Table showing significant results of various enzyme treatments tested for efficacy against Botrytis cinerea, Fusarium graminearum, Penicillium digitatum, Penicillium expansum, Penicillium italicum, Phytophthora infestans, Pyricularia grisea and Psoralea graminearum. Results are presented as the amount of oligosaccharides dissolved after hydrolysis of crude cell wall preparations (mg glucose equivalents per gram of crude cell wall material (mg Glc / g CW)).

[0021] Fig.17 is a table showing significant results of various enzyme treatments tested for efficacy against Botrytis cinerea and Penicillium expansum. The results are presented as the minimum enzyme concentration necessary to prevent spore germination in the presence of enzyme, 24 hours after enzyme wash, or 48 hours after enzyme wash.

[0022] Fig.18 Table showing significant results of various enzyme treatments tested for efficacy against Botrytis cinerea. Results are presented as minimum inhibitory concentration (MIC) of average total mycelial area. 50 ) (i.e., the minimum enzyme concentration required to inhibit the mean total mycelial area to 50% or less of the corresponding untreated control).

[0023] Fig.19 is a table showing significant results of various enzyme treatments tested for efficacy against Botrytis cinerea and Penicillium expansum. The results are presented as percent inhibition of germ tube elongation compared to the corresponding buffer control solution. DETAILED DESCRIPTION

[0024] This specification is not intended to be an exhaustive list of all the different ways in which the inventive concepts disclosed herein can be implemented or all the features that can be added thereto. For example, features shown with respect to one embodiment can be incorporated into other embodiments, and features shown with respect to a particular embodiment can be deleted from that embodiment. In addition, it will be clear to those skilled in the art that various variations and additions to the various embodiments proposed herein that do not depart from the present invention will be apparent from this disclosure. Therefore, the following description is intended to illustrate some embodiments of the present invention, rather than exhaustively specifying all permutations, combinations, and variations thereof.

[0025] The terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the invention.

[0026] Unless otherwise defined, all terms (including technical and scientific terms) used herein have the same meaning as commonly understood by those of ordinary skill in the art to which the present invention belongs. It will be further understood that terms such as those defined in commonly used dictionaries should be interpreted as having a meaning consistent with their meaning in the context of this specification and the relevant art, and should not be interpreted in an idealized or overly formal sense unless explicitly defined herein. For the sake of brevity and / or clarity, well-known functions or structures may not be described in detail.

[0027] As used herein, the singular forms “a”, “an” and “the” are intended to include the plural forms as well, unless the context clearly indicates otherwise.

[0028] As used herein, "additive" when referring to the effect of a combination within a composition means that the effect of the combination as a whole is about the same as the sum of the effects of the individual components combined separately. A combination of components that produces such an effect can be referred to as an additive combination.

[0029] As used herein, the terms "agronomic, floricultural, horticultural and / or forestry equipment / facilities" and "agronomic / floristry / horticultural / forestry equipment / facilities" refer to equipment or facilities used for one or more aspects of plant propagation, cultivation and / or harvesting, including but not limited to breeding, planting, irrigating, fertilizing, growing, monitoring, testing, pruning, harvesting, processing, packaging and / or storing plants and plant parts. Exemplary equipment and facilities include cultivators, seed containers, planters, planters, hydroponic growing systems, growing rooms, greenhouses, seed spreaders, fertilizer drills, fertilizer spreaders, irrigation systems, harvesting equipment, post-harvest storage containers, post-harvest handling rooms, and post-harvest transport containers.

[0030] As used herein, the term "agriculturally acceptable carrier" refers to a substance or composition that can be used to deliver a beneficial agent to a plant, plant part, or plant growth medium (e.g., soil) without causing / having an excessively adverse effect on plant growth, development, and / or yield. As used herein, the term "foliar compatible carrier" refers to a material that can be applied foliarly to a plant or plant part without causing / having an excessively adverse effect on the plant, plant part, plant growth, plant health, etc. As used herein, the term "seed compatible carrier" refers to a material that can be applied to seeds without causing / having an excessively adverse effect on the seeds, plants grown from the seeds, seed germination, etc. As used herein, the term "soil compatible carrier" refers to a material that can be added to the soil without causing / having an excessively adverse effect on plant growth, soil structure, soil drainage, etc.

[0031] As used herein, the term "and / or" is intended to include any and all combinations of one or more of the associated listed items, as well as the lack of a combination when interpreted as an alternative ("or"). Thus, the phrase "A, B, and / or C" should be interpreted as "A, A and B, A and B and C, A and C, B, B and C, or C".

[0032] As used herein, "antagonistic" when referring to the effects of a combination within a composition means that the effect of the combination is overall less than the sum of the effects of the individual components of the combination alone. These compositions may be referred to as antagonistic combinations.

[0033] As used herein, the term "aqueous" refers to compositions that contain more than trace amounts of water (ie, more than 0.5% water by weight based on the total weight of the composition).

[0034] As used herein, the terms "associated with," "in association with," and "associated therewith," when used with respect to the relationship between a composition of the present disclosure and a plant or plant part, refer to at least juxtaposition or close proximity of the composition and the plant or plant part. Such juxtaposition or close proximity can be achieved by directly contacting the composition with the plant or plant part or applying it directly to the plant or plant part and / or by applying the composition to a plant growth medium (e.g., soil) in which the plant or plant part will be growing (or is currently growing). According to some embodiments, the composition is applied to the outer surface of the plant or plant part as a coating. According to some embodiments, the composition is applied to soil at, near, or around the site in which the plant or plant part will be growing (or is currently growing).

[0035] As used herein, the term "beneficial agent" may refer to any agent having at least one agronomically / floristry / horticulturally / forestively beneficial property (e.g., the ability to fix atmospheric nitrogen, the ability to solubilize phosphates, the ability to produce one or more agronomically / floristry / horticulturally / forestively beneficial small molecules such as plant signaling molecules, the ability to stimulate one or more plant defense systems, and the ability to produce one or more plant protectants such as pesticidal toxins).

[0036] As used herein, the term "biostimulant" refers to an agent or combination of agents whose application enhances one or more metabolic and / or physiological processes (e.g., carbohydrate biosynthesis, ion uptake, nucleic acid uptake, nutrient delivery, photosynthesis, and / or respiration) of a plant or plant part.

[0037] As used herein, the term "binding module" refers to the region of an enzyme that mediates the binding of the enzyme to a substrate.

[0038] As used herein, the term "catalytic domain" refers to the region of an enzyme that contains the catalytic machinery of the enzyme.

[0039] As used herein, the term "cDNA" refers to a DNA molecule that can be prepared by reverse transcription from a mature spliced ​​mRNA molecule obtained from a eukaryotic or prokaryotic cell. The cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, and then present as a mature spliced ​​mRNA.

[0040] As used herein, the term "coding sequence" refers to a polynucleotide that directly specifies the amino acid sequence of a polypeptide. The boundaries of a coding sequence are usually determined by an open reading frame that begins with a start codon (such as ATG, GTG or TTG) and ends with a stop codon (such as TAA, TAG or TGA). The coding sequence can be genomic DNA, cDNA, synthetic DNA or a combination thereof.

[0041] As used herein, the terms "colony forming unit" and "cfu" refer to microbial cells / spores that are capable of multiplying on or in a suitable growth medium or substrate (e.g., soil) when conditions (e.g., temperature, moisture, nutrient availability, pH, etc.) are favorable for germination and / or microbial growth.

[0042] As used herein, when used with respect to the compositions and methods of the present disclosure, the term "consisting essentially of" means that the composition / method may contain additional components / steps, as long as the additional components / steps do not substantially change the composition / method. When applied to the compositions / methods of the present disclosure, the term "substantially changes" means that the effectiveness of the composition / method is increased or decreased by at least 20%. For example, if a component added to the composition of the present disclosure increases or decreases the ability of the composition to inhibit the growth of a target plant pathogen by at least 20%, the component can be considered to "substantially change" the composition.

[0043] As used herein, the term "control sequence" refers to a nucleic acid sequence that is related to the expression of a polynucleotide in a particular organism or in vitro. Each control sequence can be natural (i.e., from the same gene) or heterologous (i.e., from different genes) for a polynucleotide encoding a polypeptide, and is natural or heterologous relative to each other. Such control sequences include, but are not limited to, leader sequences, polyadenylation sequences, prepro peptides, propeptides, signal peptides, promoters, terminators, enhancers, and transcription or translation initiators and terminator sequences. At a minimum, the control sequence includes a promoter and transcription and translation termination signals. For the purpose of introducing a specific restriction site that is conducive to connecting the control sequence to the coding region of the polynucleotide encoding a polypeptide, the control sequence can be provided with a joint.

[0044] As used herein, the term "derived from" when used in reference to the relationship between an organism and a protein and / or polynucleotide means that the protein and / or polynucleotide naturally occurs in the organism.

[0045] As used herein, the term "diazotrophic organisms" refers to organisms that are able to convert atmospheric nitrogen (N 2 ) into a form that can be used by the plant or plant part (e.g., ammonia (NH 3 ), ammonium (NH 4 +) etc.) organisms.

[0046] As used herein, the term "dispersant" refers to an agent or combination of agents whose administration reduces the cohesion of like particles, the surface tension of a liquid, the interfacial tension between two liquids, and / or the interfacial tension between a liquid and a solid.

[0047] As used herein, the terms "effective amount", "effective concentration" and "effective amount / concentration" refer to an amount or concentration sufficient to cause a desired effect (e.g., inhibiting plant diseases, increasing plant yield). The absolute value of the amount / concentration sufficient to cause the desired effect may be affected by factors such as: the type and intensity of the desired effect; the type, size and volume of the material to which the composition will be applied; one or more types of enzymes in the composition; one or more amounts of one or more enzymes in the composition; the stability of one or more enzymes in the composition; and storage conditions (e.g., temperature, relative humidity, duration). Those skilled in the art will understand how to select an effective amount / concentration using conventional dose-response experiments. In some instances, the effective amount of a substance when used alone may be different from the effective amount of the same substance when used as part of a combination.

[0048] As used herein, the term "endogenous gene" refers to a gene consisting of an endogenous polynucleotide.

[0049] As used herein, the term "endogenous polynucleotide" refers to a polynucleotide native to the referenced host cell.

[0050] As used herein, the terms "enhanced growth" and "enhanced plant growth" refer to an improvement in one or more plant growth and / or developmental characteristics compared to one or more control plants (e.g., plants germinated from untreated seeds or untreated plants). Exemplary plant growth / developmental characteristics include, but are not limited to, biomass, carbohydrate biosynthesis, chlorophyll content, cold tolerance, drought tolerance, height, leaf length, leaf mass, leaf number, leaf surface area, leaf volume, nutrient uptake (e.g., calcium, magnesium, nitrogen, phosphorus and / or potassium uptake), one or more photosynthetic rates, root area, root diameter, root length, root mass, nodule formation (e.g., nodule mass, nodule number, nodule volume), root number, root surface area, root volume, salt tolerance, seed germination, emergence, shoot diameter, shoot length, shoot mass, shoot number, shoot surface area, shoot volume, spread, stomatal conductance, and survival rate.

[0051] As used herein, the terms "enhanced stability" and "enhanced enzyme stability" refer to an improvement in one or more enzyme stability characteristics compared to one or more controls (e.g., a control composition that is identical to the composition of the present disclosure except for the lack of one or more of the components found in the composition of the present disclosure). Exemplary enzyme stability characteristics include, but are not limited to, maintenance of enzyme activity after application to a plant or plant part and / or storage for a defined period of time and the ability to cause a desired effect (e.g., reducing phytopathogenicity of a target pest) after application to a plant or plant part and / or storage for a defined period of time.

[0052] As used herein, the terms "increased yield" and "increased plant yield" refer to an improvement in one or more plant yield characteristics compared to one or more control plants (e.g., control plants germinated from untreated seeds). Exemplary plant yield characteristics include, but are not limited to, biomass; bushels per acre; grain weight per plot (GWTPP); nutritional content; the percentage of plants that cannot produce grain in a given area (e.g., a plot); yield at standard moisture percentage (YSMP), such as grain yield at standard moisture percentage (GYSMP); yield per plot (YPP), such as grain weight per plot (GWTPP); and yield reduction (YRED).

[0053] As used herein, the term "expression" refers to any step involved in the production of a polypeptide, including but not limited to transcription, post-transcriptional modification, translation, post-translational modification, and secretion. Expression can be measured by techniques known in the art (such as measuring the level of mRNA and / or translated polypeptide), for example to detect increased expression.

[0054] As used herein, the term "expression vector" refers to a linear or circular DNA construct comprising a DNA sequence encoding a polypeptide, which is operably linked to a suitable control sequence capable of achieving expression of the DNA in a suitable host. Such control sequences may include a promoter that achieves transcription, an optional operator sequence that controls transcription, a sequence encoding a suitable ribosome binding site on mRNA, an enhancer, and a sequence that controls the termination of transcription and translation.

[0055] As used herein, the term "extension" refers to the addition of one or more amino acids to the amino and / or carboxyl terminus of a polypeptide.

[0056] As used herein, the term "foliage" refers to those parts of a plant that typically grow above the ground and include, but are not limited to, leaves, stalks, stems, flowers, fruiting bodies, and fruits.

[0057] As used herein, the terms "foliar application" and "foliarly applied" refer to applying one or more active ingredients to the foliage of a plant (e.g., the leaves of a plant). Application can be achieved by any suitable means, including but not limited to spraying / atomizing the plant with a composition comprising one or more active ingredients. In some embodiments, one or more active ingredients are applied to the leaves, stems, and / or stalks of a plant without applying to the flowers, fruiting bodies, or fruits of the plant.

[0058] As used herein, the term "fragment" refers to a polypeptide lacking one or more amino acids at the amino and / or carboxyl terminus of a mature polypeptide.

[0059] As used herein, the term "fusion protein" refers to a polypeptide fused to the N-terminus and / or C-terminus of a polypeptide disclosed herein. Fusion proteins are produced by fusing a polynucleotide encoding another polypeptide with a polynucleotide disclosed herein or by fusing two or more polynucleotides disclosed herein together. The technology for producing fusion proteins is known in the art, and includes connecting the coding sequence of the encoded polypeptide so that they meet the reading frame, and the expression of the fusion protein is under the control of one or more identical promoters and terminators. Fusion proteins can also be constructed using intein technology, wherein fusion proteins are produced after translation (Cooper et al., 1993, EMBO J. [Journal of the European Molecular Biology Association] 12: 2575-2583; Dawson et al., 1994, Science [Science] 266: 776-779). The fusion protein may further include a cleavage site between the two polypeptides. After the fusion protein is secreted, the site is cut to release the two polypeptides. Examples of cleavage sites include, but are not limited to, those disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3:568-576; Svetina et al., 2000, J. Biotechnol. 76:245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63:3488-3493; Ward et al., 1998, J. Biotechnol. 76:245-251; 95, Biotechnology 13:498-503; and Contreras et al., 1991, Biotechnology 9:378-381; Eaton et al., 1986, Biochemistry 25:505-512; Collins-Racie et al., 1995, Biotechnology 13:982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6:240-248; and Stevens, 2003, Drug Discovery World 4:35-48.

[0060] As used herein, the term "heterologous" when used to describe the relationship between a polynucleotide or polypeptide and a host cell refers to a polynucleotide or polypeptide that does not naturally occur in the host cell. For the purposes of this disclosure, a foreign copy of a polynucleotide that is native to the reference host cell is considered a heterologous polynucleotide.

[0061] As used herein, the term "heterologous," when used to describe the relationship between a polynucleotide or polypeptide and a control sequence (e.g., a promoter sequence), means that the polynucleotide or polypeptide is not naturally associated with the control sequence (i.e., the control sequence is from a gene other than the gene encoding the mature polypeptide).

[0062] As used herein, the terms "host strain" and "host cell" refer to an organism into which an expression vector, bacteriophage, virus or other DNA construct (including a polynucleotide encoding a polypeptide of interest (e.g., amylase)) has been introduced. Exemplary host strains are microbial cells (e.g., bacteria, filamentous fungi and yeast) and plant cells capable of expressing the protein of interest. The term "host cell" includes protoplasts produced by a cell.

[0063] As used herein, the terms "inoculum composition" and "inoculum" refer to a composition comprising microbial cells and / or spores that are capable of multiplying / germinating on or in a suitable growth medium or substrate (e.g., soil) when conditions (e.g., temperature, moisture, nutrient availability, pH, etc.) are favorable for germination and / or microbial growth.

[0064] As used herein, the term "introduced" when used to describe the insertion of a nucleic acid sequence into a cell encompasses "transfection," "transformation," or "transduction" as known in the art.

[0065] As used herein, the term "isolated" refers to a polypeptide, nucleic acid, cell or other specified material or component that has been separated from at least one other material or component (including but not limited to other proteins, nucleic acids, cells, etc.). Thus, the isolated polypeptide, nucleic acid, cell or other material is in a form that does not exist in nature. An isolated polypeptide includes but is not limited to a culture medium containing a secretory polypeptide expressed in a host cell.

[0066] As used herein, the term "isomer" includes all stereoisomers of the compounds and / or molecules to which it refers, including enantiomers and diastereomers, as well as all conformers, rotational isomers and tautomers, unless otherwise indicated. The compounds and / or molecules disclosed herein include all enantiomers in substantially pure left-handed or right-handed form or in a racemic mixture or in any ratio of enantiomers. Where the embodiments disclose (D)-enantiomers, the embodiments also include (L)-enantiomers; where the embodiments disclose (L)-enantiomers, the embodiments also include (D)-enantiomers. Where the embodiments disclose (+)-enantiomers, the embodiments also include (-)-enantiomers; where the embodiments disclose (-)-enantiomers, the embodiments also include (+)-enantiomers. Where an embodiment discloses an (S)-enantiomer, the embodiment also includes the (R)-enantiomer; where an embodiment discloses an (R)-enantiomer, the embodiment also includes the (S)-enantiomer. The embodiments are intended to include any diastereomer of the compounds and / or molecules mentioned herein in diastereomerically pure form and in the form of mixtures of all ratios. Unless stereochemistry is clearly indicated in a chemical structure or chemical name, a chemical structure or chemical name is intended to include all possible stereoisomers, conformers, rotational isomers, and tautomers of the depicted compounds and / or molecules.

[0067] As used herein, the term "mature polypeptide" refers to a polypeptide in its mature form after N-terminal and / or C-terminal processing (eg, removal of a signal peptide).

[0068] As used herein, the term "mature polypeptide coding sequence" refers to a polynucleotide that encodes a mature polypeptide.

[0069] As used herein, the term "modified microbial strain" refers to a microbial strain that has been improved from a strain isolated from nature. The modified microbial strain can be produced by any one or more suitable methods, including but not limited to chemical or other forms of induced mutations in polynucleotides in any genome within the strain; inserting or deleting one or more nucleotides in any genome within the strain, or a combination thereof; inverting at least one DNA segment in any genome within the strain; rearranging any genome within the strain; widely or specifically transducing homozygous or heterozygous polynucleotide segments into any genome within the strain; introducing one or more bacteriophages into any genome of the strain; transforming any strain, resulting in the introduction of stably replicated autonomous extrachromosomal DNA into the strain; making any changes to any genome or total DNA composition within a strain isolated from nature as a result of joining with any different microbial strain; and any combination of the foregoing. The term modified microbial strain includes strains having (a) one or more heterologous nucleotide sequences, (b) one or more non-naturally occurring copies of a nucleotide sequence isolated from nature (i.e., additional copies of a gene naturally occurring in the microbial strain from which the modified microbial strain is derived), (c) lacking one or more nucleotide sequences originally present in a natural reference strain by, for example, deleting the nucleotide sequence, and (d) added extrachromosomal DNA. In some embodiments, the modified microbial strain comprises a combination of two or more nucleotide sequences (e.g., two or more naturally occurring genes that do not naturally occur in the same microbial strain), or comprises a nucleotide sequence isolated from nature at a locus different from the natural locus.

[0070] As used herein, the term "native" refers to a polynucleotide or polypeptide that occurs naturally in a host cell.

[0071] As used herein, the term "naturally occurring" refers to any substance (e.g., a protein, amino acid, or nucleic acid sequence) found in nature. Conversely, the term "non-naturally occurring" refers to any substance not found in nature (e.g., recombinant nucleic acid and protein sequences produced in a laboratory, modifications of wild-type sequences, formulations comprising one or more synthetic components, formulations comprising artificial combinations of components that otherwise occur in nature).

[0072] As used herein, the term "non-aqueous" refers to compositions that contain no more than trace amounts of water (ie, no more than 0.5% water by weight based on the total weight of the composition).

[0073] As used herein, the term "nutrient" refers to compounds or elements that can be used to nourish plants (eg, vitamins, macrominerals, micronutrients, trace minerals, organic acids, etc., necessary for plant growth and / or development).

[0074] As used herein, when used in relation to an organism and a protein, the term "obtained from" means that the protein is expressed in the organism, whether from a naturally occurring polynucleotide therein or from a heterologous polynucleotide introduced into the organism.

[0075] As used herein, the term "polynucleotide" encompasses DNA, RNA, heteroduplexes, and synthetic molecules capable of encoding polypeptides. Polynucleotides can be single-stranded or double-stranded, and can include chemical modifications. The terms "nucleic acid" and "polynucleotide" are used interchangeably. Because the genetic code is degenerate, more than one codon can be used to encode a specific amino acid, and the present compositions and methods encompass nucleotide sequences encoding a specific amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in a 5' to 3' orientation.

[0076] As used herein, the term "nucleic acid construct" refers to a single-stranded or double-stranded polynucleotide that is isolated from a naturally occurring gene or modified in a manner not originally found in nature to contain a nucleic acid segment or is synthetic and comprises one or more control sequences operably linked to the nucleic acid sequence.

[0077] As used herein, the term "operably linked" means that the specified components are in a relationship (including but not limited to juxtaposition) that allows them to function in an intended manner. For example, a regulatory sequence is operably linked to a coding sequence so that the expression of the coding sequence is under the control of the regulatory sequence.

[0078] As used herein, the term "phosphate solubilizing microorganism" refers to a microorganism that is capable of converting insoluble phosphate into a soluble form of phosphate.

[0079] As used herein, the term "plant pathogenic pests" includes any organisms or viruses that have a negative impact on plants, including but not limited to organisms and viruses that spread diseases, damage host plants and / or compete for soil nutrients. The term "plant pathogenic pests" covers organisms and viruses that are known to be associated with plants and cause harmful effects on the health and / or vitality of plants. Plant pathogenic pests include but are not limited to arachnids (e.g., mites, ticks, spiders, etc.), bacteria, fungi, gastropods (e.g., slugs, snails, etc.), invasive plants (e.g., weeds), insects (e.g., whiteflies, thrips, weevils, etc.), nematodes (e.g., root knot nematodes, soybean cyst nematodes, etc.), rodents and viruses (e.g., tobacco mosaic virus (TMV), tomato spotted wilt virus (TSWV), cauliflower mosaic virus (CaMV), etc.).

[0080] As used herein, the term "plant" includes all plant populations, including but not limited to agronomic, floricultural, horticultural and forestry plants. The term "plant" encompasses plants obtained by conventional plant breeding and optimization methods (e.g., marker-assisted selection) and plants obtained by genetic engineering, including cultivars that may be protected by plant breeders' rights and those that are not protected.

[0081] As used herein, the term "plant cell" refers to a cell of a whole plant, a cell taken from a plant, or a cell derived from a cell taken from a plant. Thus, the term "plant cell" includes cells in seeds, suspension cultures, embryos, meristematic regions, callus tissue, leaves, buds, gametophytes, sporophytes, pollen, and microspores.

[0082] As used herein, the term "plant growth regulator" refers to an agent or combination of agents whose application accelerates or delays the growth / maturity rate of a plant by a direct physiological effect on the plant or otherwise changes the behavior of the plant by a direct physiological effect on the plant. "Plant growth regulator" should not be interpreted as including any agent or combination of agents excluded from the definition of "plant regulator" stated in Section 2(v) of the Federal Insecticide, Fungicide, and Rodenticide Act (7 U.S.C. § 136 (v)). Therefore, "plant growth regulator" does not cover microorganisms applied to plants, plant parts or plant growth media to enhance the availability and / or uptake of nutrients, nutrients necessary for normal plant growth, soil amendments applied to improve soil characteristics that are conducive to plant growth, or vitamin hormone products as defined in 40 C.FR § 152.6 (f).

[0083] As used herein, the term "plant part" refers to any part of a plant, including cells and tissues derived from a plant. Thus, the term "plant part" may refer to any plant component or organ (e.g., blade, stem, root, etc.), plant tissue, plant cell, and seed. Examples of plant parts include, but are not limited to, anthers, embryos, flowers, fruits, fruiting bodies, blades, ovules, pollen, rhizomes, roots, seeds, buds, stems, and tubers, as well as scions, stock, protoplasts, callus, etc.

[0084] As used herein, the term "plant propagation material" refers to a plant part from which a complete plant can be generated. Examples of plant propagation materials include, but are not limited to, cuttings (e.g., leaves, stems), rhizomes, seeds, tubers, and cells / tissues that can be cultured into a complete plant.

[0085] As used herein, the term "protein" is not intended to refer to a specific amino acid chain length, and encompasses peptides, oligopeptides and polypeptides. It should be understood that the term "protein" also encompasses two or more polypeptides combined to form an encoded product, as well as hybrid polypeptides and fusion proteins.

[0086] As used herein, the term "purified" refers to polynucleotides, proteins, or cells that are substantially free of other components as determined by analytical techniques well known in the art (e.g., purified polynucleotides or proteins can form discrete bands in an electrophoretic gel, a chromatography eluate, and / or a medium subjected to density gradient centrifugation). A purified polynucleotide or protein is at least about 50% pure, typically at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percentage by weight or by mole). In a related sense, a composition is enriched for a molecule when the concentration of the molecule is substantially increased after application of a purification or enrichment technique. The term "enriched" refers to compounds, polynucleotides, proteins, cells, nucleic acids, amino acids or other designated materials or components that are present in a composition at a relative or absolute concentration greater than that of the starting composition.

[0087] In one aspect, the term "purified" as used herein refers to a protein or cell that is substantially free of components (especially insoluble components) from the producing organism. In other aspects, the term "purified" refers to a protein that is substantially free of insoluble components (especially insoluble components) from the natural organism from which it is obtained. In one aspect, the protein is separated from some soluble components of the organism and culture medium from which it is recovered. The protein can be purified (i.e., separated) by one or more of the unit operations filtration, precipitation, or chromatography.

[0088] Therefore, protein can be purified so that only a small amount of other proteins, particularly other proteins, are present. As used herein, the term "purified" can refer to the removal of other components present in the cell of the protein source, particularly other proteins and most particularly other enzymes. Protein can be "substantially pure", i.e., free of other components from the organism producing it (e.g., a host organism for recombinantly producing the protein). In one aspect, by the weight of the total protein material present in the preparation, the protein is at least 40% pure. In one aspect, by the weight of the total protein material present in the preparation, the protein is at least 50%, 60%, 70%, 80% or 90% pure. As used herein, "substantially pure protein" can refer to a protein preparation containing by weight up to 10%, preferably up to 8%, more preferably up to 6%, more preferably up to 5%, more preferably up to 4%, more preferably up to 3%, even more preferably up to 2%, most preferably up to 1% and even most preferably up to 0.5% of the protein and other protein materials associated with it naturally or recombinantly.

[0089] Thus, it is preferred that a substantially pure protein is at least 92% pure, preferably at least 94% pure, more preferably at least 95% pure, more preferably at least 96% pure, more preferably at least 97% pure, more preferably at least 98% pure, even more preferably at least 99% pure, most preferably at least 99.5% pure, based on the weight of the total protein material present in the preparation. The proteins of the present disclosure are preferably in substantially pure form (i.e., the preparation is substantially free of other protein material). This can be achieved, for example, by preparing the protein by well-known recombinant methods or by classical purification methods.

[0090] As used herein, the term "recombinant" is used in its conventional sense to refer to the manipulation (e.g., cutting and rejoining) of a nucleic acid sequence to form a sequence group that is different from that found in nature. The term recombinant refers to a cell, nucleic acid, protein, or vector that has been modified from its native state. Thus, for example, a recombinant cell expresses genes not found in the native (non-recombinant) form of the cell, or expresses native genes at different levels or under different conditions than those found in nature. The term "recombinant" is synonymous with "genetically modified" and "transgenic".

[0091] As used herein, the terms "recover" and "recovery" refer to removing a protein from at least one fermentation broth component selected from the list of cells, nucleic acids or other specified materials, such as recovering a protein from a whole fermentation broth or from a cell-free fermentation broth by harvesting protein crystals, by filtration (e.g., depth filtration (by using filter aids or packed filter media, cloth filtration in box filters, drum filtration, drum filtration, rotary vacuum drum filters, candle filters, horizontal leaf filters or the like, sheet or pad filtration using a frame or modular arrangement) or membrane filtration (using plate filtration, modular filtration, candle filtration, microfiltration, cross-flow, dynamic cross-flow or ultrafiltration in dead-end operation)) or by centrifugation (using a decanter centrifuge, a disk stack centrifuge, a hyrdo cyclone or the like) or by precipitating the protein and using related solid-liquid separation methods to harvest the protein from a broth medium by using size fractionation. Recovery encompasses the isolation and / or purification of the protein.

[0092] As used herein, the relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity".

[0093] For the purpose of this disclosure, the sequence identity between two amino acid sequences is determined as the output of "longest identity" using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J.Mol.Biol. [Journal of Molecular Biology] 48: 443-453), which is implemented in the Needle program of the EMBOSS software package (EMBOSS: European Molecular Biology Open Software Suite (The European Molecular Biology Open Software Suite), Rice et al., 2000, Trends Genet. [Genetics Trend] 16: 276-277) (preferably 6.6.0 version or later). The parameters used are gap opening penalty 10, gap extension penalty 0.5 and EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, it is necessary to specify the non-simplified (-nobrief) option in the command line. The output of the "longest identity" marked by Needle is calculated as follows:

[0094] (number of identical residues x 100) / (length of alignment - total number of gaps in the alignment)

[0095] For the purpose of this disclosure, the sequence identity between two polynucleotide sequences is determined as the output of "longest identity" using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra), which is implemented in the Needle program of the EMBOSS software package (EMBOSS: European Molecular Biology Open Software Suite, Rice et al., 2000, supra) (preferred 6.6.0 version or later). The parameters used are gap opening penalty 10, gap extension penalty 0.5 and EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. In order for the Needle program to report the longest identity, it is necessary to specify the non-simplified (nobrief) option in the command line. The output calculation of the "longest identity" of the Needle mark is as follows:

[0096] (Identical deoxyribonucleotides x 100) / (Alignment length - Total number of gaps in the alignment).

[0097] As used herein, the term "signal peptide" refers to an amino acid sequence attached to the N-terminal portion of a protein that promotes secretion of the protein outside the cell. The mature form of the extracellular protein lacks a signal peptide, which is cleaved off during the secretion process.

[0098] As used herein, the terms "stabilizing compound" and "stabilizer" refer to an agent or combination of agents whose administration enhances the stability of an enzyme.

[0099] As used herein, the term "subsequence" refers to a polynucleotide lacking one or more nucleotides at the 5' and / or 3' end of a mature protein coding sequence; wherein the subsequence encodes a fragment having enzymatic activity.

[0100] As used herein, the term "variant" refers to a protein comprising an artificial mutation (i.e., substitution, insertion (including extension) and / or deletion (e.g., truncation)) at one or more positions. Substitution means replacing the amino acid occupying a certain position with a different amino acid; deletion means removing the amino acid occupying a certain position; and insertion means adding 1-5 amino acids (e.g., 1-3 amino acids, particularly 1 amino acid) adjacent to and immediately following the amino acid occupying a certain position.

[0101] As used herein, the term "wild-type" with respect to an amino acid sequence or a nucleic acid sequence means that the amino acid sequence or the nucleic acid sequence is a native or naturally occurring sequence.

[0102] Although certain aspects of the present disclosure will be described hereinafter with reference to embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the present disclosure as defined by the claims.

[0103] All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety, unless they contradict any disclosure expressly set forth herein.

[0104] The present disclosure provides proteins that can be used to: a) prevent, treat, inhibit and / or eliminate infestations / infections caused by a wide range of pests, including but not limited to plant pathogenic pests such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; b) treat surfaces / materials susceptible to infestation / infection; c) clean infested / infected surfaces / materials; d) reduce the severity of diseases in plants and plant parts directly or indirectly affected by plant pathogenic pests; e) improve the plant growth environment; f) increase the availability of nutrients in the plant growth medium; g) reduce the need to achieve the desired one or more amounts of exogenous fertilizer required to produce fruit; h) improve plant growth, development and yield characteristics; i) extend the storage life of harvested plants and plant parts; j) delay the maturation of plants and plant parts; k) accelerate the maturation of plants and plant parts; l) improve the efficacy of biological / chemical pesticides; m) prevent, treat, inhibit and / or eliminate pesticide-induced resistance / phytotoxicity; as well as polynucleotides encoding such proteins, organisms expressing such proteins, formulations comprising such proteins, polynucleotides and organisms, and methods of using such proteins, polynucleotides, organisms and formulations in agriculture and other fields of endeavor.

[0105] As will be appreciated by those skilled in the art, the proteins, polynucleotides and organisms of the present disclosure can be used (and can be formulated for use) at any one or more times throughout the agronomic, floricultural, horticultural and forestry processes (e.g., before planting, at planting, after planting, before germination, after germination, before emergence, at emergence, after emergence, before the vegetative stage, during the vegetative stage, after the vegetative stage, before the reproductive stage, during the reproductive stage, after the reproductive stage, before flowering, at flowering, after flowering, before fruiting, at fruiting, after fruiting, before maturity, at maturity, after maturity, before harvesting, at harvesting, after harvesting, before transport / storage, during transport / storage and / or after transport / storage). Thus, the proteins of the present disclosure can be formulated for any suitable application method, including but not limited to application on seeds, in-furrow application, foliar application, pre-harvest application and post-harvest application.

[0106] As will be further understood by those skilled in the art, the proteins, polynucleotides, organisms and formulations of the present disclosure can achieve desired one or more results (including prevention, treatment, inhibition and / or elimination of infestation / infection) without toxicity. As will be further explained in detail below, the compositions of the present disclosure can exert their effects by various non-lethal means, such as, for example, reducing harmful organisms by degrading food sources to be attracted by treated surfaces. In addition, in many cases, the originally toxic proteins of the present disclosure can be used in non-lethal doses to enhance the efficacy of various chemical pesticides and biological pesticides and / or to expand their target harmful organism range.

[0107] Finally, it will be appreciated by those skilled in the art that the proteins, polynucleotides, organisms and formulations disclosed herein can be used in combination to achieve a desired result or results. Thus, the disclosure extends to formulations comprising two or more proteins disclosed herein, hybrid proteins comprising two or more different catalytic domains, fusion proteins comprising two or more enzyme polypeptides, and the like. Although certain combinations will be described in detail below, it should be understood that the disclosure is not limited to those combinations, but extends to all possible combinations of the proteins, formulations, polynucleotides and organisms described herein.

[0108] In some embodiments, the proteins of the present disclosure exhibit one or more catalytic activities belonging to Enzyme Commission Classification Number 1 (EC1). For example, in some embodiments, the proteins of the present disclosure exhibit glucose oxidase, cellobiose dehydrogenase, amino acid oxidase, laccase, catalase, peroxidase and / or oxygenase activities, which can be used to a) prevent / treat / inhibit / eliminate / reduce the harmful effects of various pests / infestations / infections caused by them, including but not limited to plant pathogenic pests such as mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; b) reduce the severity of diseases in plants affected by one or more plant pathogenic pests. c) pre-treating surfaces / materials susceptible to infestation / infection by pests; d) cleaning surfaces / materials infested / infected by pests; e) improving the environment for plant growth; f) increasing nutrient availability in the plant growth medium; g) reducing the amount of exogenous fertilizer required to achieve the desired results; h) improving plant growth, development and yield characteristics; i) extending the storage life of harvested plants and plant parts; j) delaying / accelerating the maturation of plants or plant parts; k) increasing the efficacy of chemical pesticides; and / or l) reducing resistance / phytotoxicity induced by chemical pesticides.

[0109] In some embodiments, the proteins of the disclosure exhibit one or more oxidoreductase activities belonging to EC 1, and optionally comprise, consist essentially of, or consist of an amino acid sequence that is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the amino acid sequences set forth herein as SEQ ID NOs: 1-15 and 183-2755.

[0110] In some embodiments, the proteins of the present disclosure exhibit one or more oxidoreductase activities belonging to EC 1.1, such as oxidase activities belonging to EC 1.1.3 (e.g., glucose oxidase activity belonging to EC 1.1.3.4, hexose oxidase activity belonging to EC 3.1.1.5, galactose oxidase activity belonging to EC 1.1.3.9) and / or oxidase activities belonging to EC 1.1.99 (e.g., cellobiose oxidase activity belonging to EC 1.1.99.18), and optionally comprise a polypeptide as described herein as SEQ ID 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, one, two, three, four, five or more of the amino acid sequences set forth in NO:1-8, or consisting essentially of, one, two, three, four, five or more of about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, the amino acid sequence.

[0111] In some embodiments, the protein is selected from the group consisting of:

[0112] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 1-5;

[0113] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 1-5;

[0114] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 92-96, or a cDNA sequence thereof;

[0115] d) a polypeptide derived from any one of SEQ ID NOs: 1-5 by substitution, deletion or insertion of one or more amino acids;

[0116] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-5 by substitution, deletion or insertion of one or more amino acids;

[0117] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0118] g) A fragment of the polypeptide of any one of a) to f)

[0119] Wherein the polypeptide has glucose oxidase activity belonging to EC 1.1.3.4. Examples of proteins exhibiting glucose oxidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 1-5 are set forth herein as SEQ ID NOs: 183-2205.

[0120] In some such embodiments, the protein is derived from Aspergillus (e.g., A. chevalieri, A. cristatus, A. flavus, A. niger, A. niveoglaucus, A. nomiae, A. oryzae., A. terreus, A. tubingensis), Beauveria (e.g., B. bassiana), Escherichia (e.g., E. coli), Komagataella (e.g., , K. pastoris), Penicillium (e.g., P. adametzii, P. amagasakiense, P. chrysogenum, P. decumbens, P. expansum, P. polonicum, P. viridicatum), or Talaromyces (e.g., T. bacillisporus, T. flavus, T. stipitatus, T. variabilis). For example, in some embodiments, the protein is a native Aspergillus (e.g., A. shevarii, A. cristatus, A. flavus, A. niger, A. nivalis-grayeus, A. nomiae, A. oryzae, A. terreus, A. tubingensis), Beauveria (e.g., Beauveria bassiana), Escherichia (e.g., Escherichia coli), Komagata (e.g., Komagata pastoriensis), Penicillium (e.g., Penicillium ada, Penicillium nigasaki, Penicillium chrysogenum, Penicillium decumbentum, Penicillium expansum, Penicillium polishum, Penicillium pure green), or Talaromyces (e.g., Talaromyces baculum, Talaromyces flavosum, Talaromyces pedunculata, Talaromyces variabilis) glucose oxidase, Or it is a functional fragment / mutant / variant of glucose oxidase from natural Aspergillus (e.g., Aspergillus chewani, Aspergillus cristatus, Aspergillus flavus, Aspergillus niger, Aspergillus snow-white-gray green, A. nomiae, Aspergillus oryzae, Aspergillus terreus, Aspergillus tubingensis), Beauveria (e.g., Beauveria bassiana), Escherichia (e.g., Escherichia coli), Komagata (e.g., Komagata pastoriana), Penicillium (e.g., Penicillium ada, Penicillium nigasaki, Penicillium chrysogenum, Penicillium decumbent, Penicillium expansum, Penicillium polishum, Penicillium pure green), or Talaromyces (e.g., Talaromyces baculoides, Talaromyces luteus, Talaromyces stalked, Talaromyces variabilis) .

[0121] In some embodiments, the protein is selected from the group consisting of:

[0122] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 6-8;

[0123] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 6-8;

[0124] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 97-99 or their cDNA sequences;

[0125] d) a polypeptide derived from any one of SEQ ID NOs: 6-8 by substitution, deletion or insertion of one or more amino acids;

[0126] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 6-8 by substitution, deletion or insertion of one or more amino acids;

[0127] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0128] g) A fragment of the polypeptide of any one of a) to f)

[0129] Wherein the polypeptide has cellobiose oxidase activity belonging to EC 1.1.99.18. Examples of proteins that exhibit cellobiose oxidase activity and have an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 6-8 are set forth herein as SEQ ID NOs: 2206-2217.

[0130] In some such embodiments, the protein is derived from Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora, or Remersonia. For example, in some embodiments, the protein is a native Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora, or Remersonia cellobiose oxidase, or a functional fragment / mutant / variant of a native Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora, or Remersonia cellobiose oxidase.

[0131] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more oxidoreductase activities belonging to EC 1.1. See, for example, CN 101348794-A; CN 101348795-A; CN102517304-A; CN 103275942-A; CN 103525778-A; CN 103614350-A; CN 103981159-A; CN104312989-A; CN 104711273-A; CN 104711274-A; CN 105002147-A; CN 105420252-A; CN105746635-A; CN 105950577-A; CN 105950578-A; CN 106119219-A; CN 107012130-A; CN107988177-A; CN 108003244-A; CN 108004256-A; CN 108118036-A; CN 108118037-A; CN108118038-A; CN 108251389-A; CN 108251390-A; CN 108251391-A; CN 108251392-A; CN108374001-A; CN 108893453-A; CN 109207446-A; CN 109321586-A; CN 109423483-A; CN109666657-A; CN 110577939-A; CN 110592034-A; CN 110628738-A; CN 110885801-A; CN111004786-A; CN 112143717-A; CN 112760299-A; CN 112877306-A; CN 113061189-A; CN113403290-A; CN 113528476-A; CN 113862233-A; CN 114058637-A; CN 114181916-A; CN114395540-A; CN 114395541-A; CN 114736879-A;CN 114736880-A; CN 114736881-A; CN115029327-A; CN 115029328-A; CN 115612628-A; CN 1229139-A; EP 1892529-A1; EP2415863-A1; EP 2562250-A1; EP 2796547-A1; EP 3572503-A1; EP 3984368-A1; FR2979918-A1; JP 2011139677-A;JP 2012157315-A;JP 2015002686-A;JP 2018198581-A;US10233430-B1;US 2004053425-A1;US 2022283151-A1;WO 2010039840-A1;WO2010053161-A1;WO 2010121933-A1;WO 2010135499-A1;WO 2011068050-A1;WO2012068236-A2;WO 2013026575-A2;WO 2013159005-A2;WO 2013181760-A1;WO2014000746-A1;WO2014013073-A1;WO 2014081700-A1;WO 2014114810-A1;WO2014173822-A2;WO 2015109405-A1;WO 2016026842-A1;WO 2016031611-A1;WO2016090472-A1;WO 2016090473-A1;WO 2016050905-A1;WO 2018039802-A1;WO2019110497-A1;WO 2020125700-A1;WO 2020239064-A1;WO 2020254336-A1;WO2022138668-A1;WO 2022256274-A1;WO 2023004432-A2;WO 2023288294-A1;WO 8912675-A;WO 9521924-A1。;

[0132] In some embodiments, the proteins of the present disclosure exhibit one or more oxidoreductase activities belonging to EC 1.4, such as oxidase activities belonging to EC 1.4.3 (e.g., D-aspartate oxidase activity belonging to EC 1.4.3.1, L-amino acid oxidase activity belonging to EC 1.4.3.2, D-amino acid oxidase activity belonging to EC 1.4.3.3, D-glutamate oxidase activity belonging to EC 1.4.3.7, L-glutamate oxidase activity belonging to EC 1.4.3.11, cyclohexylamine oxidase activity belonging to EC 1.4.3.12, protein lysine-6-oxidase activity belonging to EC 1.4.3.13, L-lysine oxidase activity belonging to EC 1.4.3.14, D-glutamate (D-aspartate) oxidase activity belonging to EC 1.4.3.15, L-aspartate oxidase activity belonging to EC 1.4.3.16, glycine oxidase activity belonging to EC 1.4.3.19, L-lysine 6-oxidase activity belonging to EC 1.4.3.20, and L-arginine oxidase activity belonging to EC 1.4.3.25).

[0133] In some embodiments, the proteins of the disclosure exhibit one or more oxidase activities belonging to EC 1.10, such as activities belonging to EC 1.10.3 (e.g., laccase activities belonging to EC 1.10.3.2), and optionally comprise a polypeptide having the same amino acid sequence as described herein as SEQ ID NO:9 is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence shown in NO:9.

[0134] In some embodiments, the protein is selected from the group consisting of:

[0135] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:9;

[0136] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:9;

[0137] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 100 or its cDNA sequence;

[0138] d) a polypeptide derived from any one of SEQ ID NO: 9 by substitution, deletion or insertion of one or more amino acids;

[0139] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 9 by substitution, deletion or insertion of one or more amino acids;

[0140] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0141] g) A fragment of the polypeptide of any one of a) to f)

[0142] Wherein the polypeptide has laccase activity belonging to EC 1.10.3.2. Examples of proteins exhibiting laccase activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 9 are set forth herein as SEQ ID NOs: 2218-2251.

[0143] In some such embodiments, the protein is derived from Chaetomium, Chrysocorona, Melanocarpus, Myceliophthora, Mycoccus, or Thermothelomyces. For example, in some embodiments, the protein is a native Chaetomium, Chrysocorona, Melanocarpus, Myceliophthora, Mycoccus, or Thermothelomyces laccase, or a functional fragment / mutant / variant of a native Chaetomium, Chrysocorona, Melanocarpus, Myceliophthora, Mycoccus, or Thermothelomyces laccase.

[0144] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more oxidase activities belonging to EC 1.10. See, for example, EP 3444323-A1; IN9601521-I4; US2008148432-A1; US ​​2009155415-A1; US ​​2012227131-A1; US ​​2022298533-A1; US ​​6060442-A; WO 2009075860-A2; WO 2012068236-A2; WO 2013181760-A1; WO 2014081700-A1; WO2015109405-A1; WO 2016029107-A1; WO 2016090059-A1; WO 2016090474-A1; WO2017089304-A1; WO 2022029293-A1; WO 2022270590-A1; WO 2023288294-A1; WO 9838286-A1.

[0145] In some embodiments, the enzyme of the present disclosure exhibits peroxidase activity belonging to EC 1.11, such as peroxidase activity belonging to EC 1.11.1 (e.g., catalase activity belonging to EC 1.11.1.6, peroxidase activity belonging to EC 1.11.1.7, lignin peroxidase activity belonging to EC 1.11.1.14), and optionally comprises a peroxidase activity belonging to SEQ ID NO: 11. 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, one or more of the amino acid sequences set forth in NOs: 10-13.

[0146] In some embodiments, the protein is selected from the group consisting of:

[0147] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 10-12;

[0148] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 10-12;

[0149] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 101-103 or their cDNA sequences;

[0150] d) a polypeptide derived from any one of SEQ ID NOs: 10-12 by substitution, deletion or insertion of one or more amino acids;

[0151] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 10-12 by substitution, deletion or insertion of one or more amino acids;

[0152] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0153] g) A fragment of the polypeptide of any one of a) to f)

[0154] Wherein the polypeptide has catalase activity belonging to EC 1.11.1.6. Examples of proteins exhibiting catalase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 10-12 are set forth herein as SEQ ID NOs: 2252-2296.

[0155] In some such embodiments, the protein is derived from Aspergillus, Myceliophthora, Penicillium, Rasamsonia, Talaromyces, or Thermoascus. For example, in some embodiments, the protein is a native Aspergillus, Myceliophthora, Penicillium, Rasamsonia, Talaromyces, or Thermoascus catalase, or a functional fragment / mutant / variant of a native Aspergillus, Myceliophthora, Penicillium, Rasamsonia, Talaromyces, or Thermoascus catalase.

[0156] In some embodiments, the protein is selected from the group consisting of:

[0157] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:13;

[0158] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:13;

[0159] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 104 or its cDNA sequence;

[0160] d) a polypeptide derived from any one of SEQ ID NO: 13 by substitution, deletion or insertion of one or more amino acids;

[0161] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 13 by substitution, deletion or insertion of one or more amino acids;

[0162] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0163] g) A fragment of the polypeptide of any one of a) to f)

[0164] Wherein the polypeptide has peroxidase activity belonging to EC 1.11.1.7. Examples of proteins exhibiting peroxidase activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 13 are set forth herein as SEQ ID NOs: 2297-2381.

[0165] In some such embodiments, the protein is derived from Arthromyces or Coprinopsis. For example, in some embodiments, the protein is a native Arthromyces or Coprinopsis peroxidase, or a functional fragment / mutant / variant of a native Arthromyces or Coprinopsis peroxidase.

[0166] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more peroxidase activities belonging to EC 1.11. See, e.g., CN 105441400-A; CN 108070574-A; CN112522227-A; EP 2295582-A2; EP 486067-A2; JP2007143405-A; JP 2010044058-A; KR2011013726-A; US 2005108791-A1; US ​​2007118916-A1; US ​​2008148432-A1; US2013074202-A1; US ​​2020306342-A1; WO 2004108765-A2; WO 2006114616-A1; WO2007020428-A1; WO 2007044043-A2; WO 2009104622-A1; WO 2010027755-A1; WO2011068297-A1; WO 2012068236-A2; WO 2012072777-A1; WO 2012130120-A1; WO2013091547-A1; WO 2014018368-A2; WO 2014081700-A1; WO 2014202616-A2; WO2015048332-A2; WO 2015182941-A1; WO 2017040907-A1;WO 2018089391-A1; WO2020200321-A1; WO 2020200322-A1; WO 2022074170-A1; WO 2022251056-A1; WO2023002065-A2; WO 2023019266-A2; WO 9317721-A1; WO 9318166-A2; WO 9510602-A1; WO9515391-A2; WO 9810060-A1; WO 9835026-A1.

[0167] In some embodiments, the proteins of the present disclosure exhibit one or more oxygenase activities belonging to EC 1.14, such as an oxygenase activity belonging to EC 1.14.16 (e.g., phenylalanine 4-monooxygenase activity belonging to EC 1.14.16.1, tyrosine 3-monooxygenase activity belonging to EC 1.14.16.2, tryptophan 5-monooxygenase activity belonging to EC 1.14.16.4, phenylalanine 3-monooxygenase activity belonging to EC 1.14.16.7), an oxygenase activity belonging to EC 1.14.18 (e.g., tyrosinase activity belonging to EC 1.14.18.1), and / or an oxygenase activity belonging to EC 1.14.99 (e.g., lytic chitin monooxygenase activity belonging to EC 1.14.99.53, lytic cellulose monooxygenase activity belonging to EC 1.14.99.54, 1.14.99.55 lytic starch monooxygenase activity, belonging to EC 1.14.99.56 lytic cellulose monooxygenase activity, belonging to EC 1.14.99.56 lytic cellulose monooxygenase activity), and optionally comprising the same as described herein as SEQ ID %, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, one or more of the amino acid sequences set forth in NOs:14-15.

[0168] In some embodiments, the protein is selected from the group consisting of:

[0169] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 14-15;

[0170] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 14-15;

[0171] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 105-106, or a cDNA sequence thereof;

[0172] d) a polypeptide derived from any one of SEQ ID NOs: 14-15 by substitution, deletion or insertion of one or more amino acids;

[0173] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 14-15 by substitution, deletion or insertion of one or more amino acids;

[0174] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0175] g) A fragment of the polypeptide of any one of a) to f)

[0176] Wherein the polypeptide has a lytic cellulose monooxygenase activity belonging to EC 1.14.99.56. Examples of proteins exhibiting lytic cellulose monooxygenase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 14-15 are set forth herein as SEQ ID NOs: 2382-2755.

[0177] In some such embodiments, the protein is derived from Penicillium, Rosalia, or Thermoascus. For example, in some embodiments, the protein is a native Penicillium, Rosalia, or Thermoascus monooxygenase, or a functional fragment / mutant / variant of a native Penicillium, Rosalia, or Thermoascus monooxygenase.

[0178] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more oxygenase activities belonging to EC 1.14. See, for example, CN 103232949-A; CN 103255072-A; CN106544329-A; CN 109554355-A; CN 110093326-A; JP 2016039821-A; US 2008299613-A1; US2011099671-A1; US ​​2014075603-A1; US ​​2018019412-A1; US ​​2019153414-A1; WO2011080267-A2; WO 2011121768-A1; WO 2011153516-A2; WO 2012000892-A1; WO2012021394-A1; WO 2012021395-A1; WO 2012044835-A1; WO 2012044836-A1; WO2012068509-A1; WO 2012089023-A1; WO 2013028915-A2; WO 2013036898-A2; WO2013110242-A1; WO 2013119302-A2; WO 2014085251-A1; WO 2014093835-A1; WO2014138983-A1; WO 2014140165-A1; WO 2014202616-A2;WO 2014202711-A1; WO2015105835-A1; WO 2015187935-A1; WO 2016045569-A1; WO 2016090473-A1; WO2016145358-A1; WO 2017070219-A1; WO 2018019948-A1; WO 2018106656-A1; WO2018142002-A1; WO 2019005755-A1; WO 2019083831-A1; WO 2019229228-A1.

[0179] In some embodiments, the proteins of the disclosure exhibit one or more catalytic activities belonging to Enzyme Commission Classification Number 2 (EC2). For example, in some embodiments, the proteins of the present disclosure exhibit aminoacyl transferase activity and can be used to a) prevent / treat / inhibit / eliminate / reduce the harmful effects of various pests / infestations / infections caused thereby, including but not limited to plant pathogenic pests, such as mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; b) reduce one or more aspects of disease severity in plants affected by one or more plant pathogenic pests; c) pre-treat surfaces / materials susceptible to infestation / infection by pests; d) clean surfaces / materials infested / infected by pests; e) improve the environment in which plants grow; f) increase nutrient availability in the plant growth medium; g) reduce the amount of exogenous fertilizer required to achieve the desired results; h) improve plant growth, development and yield characteristics; i) extend the storage life of harvested plants and plant parts; j) delay / accelerate the maturation of plants or plant parts; k) improve the efficacy of chemical pesticides; and / or l) reduce chemical pesticide-induced resistance / phytotoxicity.

[0180] In some embodiments, the proteins of the disclosure exhibit transferase activity belonging to EC 2, and optionally comprise, consist essentially of, or consist of an amino acid sequence that is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the amino acid sequences set forth herein as SEQ ID NOs: 16 and 2756-2769.

[0181] In some embodiments, the proteins of the present disclosure exhibit one or more acyltransferase activities belonging to EC 2.3, such as aminoacyltransferase activities belonging to EC 2.3.2 (e.g., D-glutamyltransferase activity belonging to EC 2.3.2.1, γ-glutamyltransferase activity belonging to EC 2.3.2.2, aspartyltransferase activity belonging to EC 2.3.2.7, protein glutamate amine γ-glutamyltransferase activity belonging to EC 2.3.2.13, D-alanine γ-glutamyltransferase activity belonging to EC 2.3.2.14), and optionally comprise the aminoacyltransferase activity described herein as SEQ ID 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, one or more of the amino acid sequences shown in NO:16.

[0182] In some embodiments, the protein is selected from the group consisting of:

[0183] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:16;

[0184] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:16;

[0185] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 107 or its cDNA sequence;

[0186] d) a polypeptide derived from any one of SEQ ID NO: 16 by substitution, deletion or insertion of one or more amino acids;

[0187] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 16 by substitution, deletion or insertion of one or more amino acids;

[0188] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0189] g) A fragment of the polypeptide of any one of a) to f)

[0190] Wherein the polypeptide has a γ-glutamyltransferase activity belonging to EC 2.3.2.2. Examples of proteins exhibiting γ-glutamyltransferase activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 16 are set forth herein as SEQ ID NOs: 2756-2769.

[0191] In some such embodiments, the protein is derived from Bacillus. For example, in some embodiments, the protein is a native Bacillus γ-glutamyltransferase, or a fragment / mutant / variant of a native Bacillus γ-glutamyltransferase.

[0192] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more acyltransferase activities belonging to EC 2.3. See, for example, CN 107828754-A; CN 108611333-A; CN108929866-A; CN 112111468-A; CN 114806988-A; EP 441353-A; KR 1814024-B1; WO2003087149-A2; WO 2005075652-A1; WO 2014081884-A1; WO 2015048332-A2; WO2018234382-A1.

[0193] In some embodiments, the proteins of the present disclosure exhibit one or more catalytic activities belonging to Enzyme Commission Classification Number 3 (EC3). For example, in some embodiments, the proteins of the present disclosure exhibit lipase, triglyceride lipase, pectinesterase, phospholipase, lysophospholipase, cutinase, amylase, glucosidase, galactosidase, cellulase, glucanase, xylanase, ceramidase, dextranase, chitinase, chitosanase, galacturonase, fucosidase, lysozyme, xylosidase, lucosidass, pullulanase, mannosidase, amidase, aminidase, maltohydrolase, cellobiosidase, pectinase, mannanase, aminopeptidase, serine peptidase and / or metallopeptidase, asparaginase and / or glutaminase activity and can be used to a) prevent / treat / inhibit / eliminate / reduce the harmful effects of various pests / infestations / infections caused thereby, including but not limited to a) reducing one or more aspects of disease severity in plants affected by one or more phytopathogenic pests; c) pre-treating surfaces / materials susceptible to infestation / infection by pests; d) cleaning surfaces / materials infested / infected by pests; e) improving the environment in which plants grow; f) increasing nutrient availability in the plant growth medium; g) reducing the amount of exogenous fertilizer required to achieve the desired results; h) improving plant growth, development and yield characteristics; i) extending the storage life of harvested plants and plant parts; j) delaying / accelerating the maturation of plants or plant parts; k) improving the efficacy of chemical pesticides; and / or l) reducing chemical pesticide-induced resistance / phytotoxicity.

[0194] In some embodiments, the proteins of the disclosure exhibit esterase activity belonging to EC 3, and optionally comprise, consist essentially of, or consist of an amino acid sequence that is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the amino acid sequences set forth herein as SEQ ID NOs: 17-90 and 2770-72141.

[0195] In some embodiments, the proteins of the present disclosure exhibit one or more esterase activities belonging to EC 3.1, such as lipase activities belonging to EC 3.1.1 (e.g., triacylglycerol lipase activities belonging to EC 3.1.1.3, phospholipase A belonging to EC 3.1.1.4). 2 activity, lysophospholipase activity belonging to 3.1.1.5, pectinesterase activity belonging to 3.1.1.11, phospholipase A belonging to 3.1.1.32 1activity, lipoprotein lipase activity belonging to EC 3.1.1.34, cutinase activity belonging to 3.1.1.74), phosphatase activity belonging to EC 3.1.3 (e.g., alkaline phosphatase activity belonging to EC 3.1.3.1, acid phosphatase activity belonging to EC 3.1.3.2, 3-phytase activity belonging to EC 3.1.3.8, glucose-6-phosphatase activity belonging to EC 3.1.3.9, glucose-1-phosphatase activity belonging to EC 3.1.3.10, fructose-bisphosphatase activity belonging to EC 3.1.3.11, sugar-phosphatase activity belonging to EC 3.1.3.23, 4-phytase activity belonging to EC 3.1.3.26, fructose-2,6-bisphosphate 2-phosphatase activity belonging to EC 3.1.3.46, 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase activity, belonging to EC 3.1.3.72 5-phytase activity, belonging to EC 3.1.3.76 lipid phosphate phosphatase activity) and / or belonging to EC 3.1.4 hydrolase activity (e.g., belonging to 3.1.4.3 phospholipase C activity, belonging to EC 3.1.4.4 phospholipase D activity, belonging to 3.1.4.11 phosphoinositide phospholipase C activity), and optionally comprising the same as described herein as SEQ ID 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, consisting essentially of, or consisting of, one or more of the amino acid sequences set forth in NOs:17-33, 72147 and 72149.

[0196] In some embodiments, the protein is selected from the group consisting of:

[0197] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 17-22;

[0198] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 17-22;

[0199] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 108-113 or their cDNA sequences;

[0200] d) a polypeptide derived from any one of SEQ ID NOs: 17-22 by substitution, deletion or insertion of one or more amino acids;

[0201] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 17-22 by substitution, deletion or insertion of one or more amino acids;

[0202] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0203] g) A fragment of the polypeptide of any one of a) to f)

[0204] Wherein the polypeptide has triacylglycerol lipase activity belonging to EC 3.1.1.3. Examples of proteins exhibiting triacylglycerol lipase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 17-22 are set forth herein as SEQ ID NOs: 2778-10223.

[0205] In some embodiments, the protein is derived from Aspergillus, Bacillus, Cryphonectria, Fusarium, Haloquadratum, Humicola, Penicillium, Scytalidium, Talaromyces, Thermomyces, or Thermus. For example, in some embodiments, the protein is a native Aspergillus, Bacillus, Cryphonectria, Fusarium, Haloquadratum, Humicola, Penicillium, Scytalidium, Talaromyces, Thermomyces, or Thermus triacylglycerol lipase, or is a fragment / mutant / variant of a native Aspergillus, Bacillus, Cryphonectria, Fusarium, Haloquadratum, Humicola, Penicillium, Scytalidium, Talaromyces, Thermomyces, or Thermus triacylglycerol lipase.

[0206] In some embodiments, the protein is selected from the group consisting of:

[0207] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:23;

[0208] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:23;

[0209] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 114 or its cDNA sequence;

[0210] d) a polypeptide derived from any one of SEQ ID NO: 23 by substitution, deletion or insertion of one or more amino acids;

[0211] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 23 by substitution, deletion or insertion of one or more amino acids;

[0212] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0213] g) A fragment of the polypeptide of any one of a) to f)

[0214] The polypeptide has triglyceride lipase activity belonging to EC 3.1.1.3 and / or phospholipase A belonging to EC 3.1.1.32 1 Activity. Shows triglyceride lipase activity and / or phospholipase A 1 Examples of proteins that are active and have an amino acid sequence that is at least 70% identical to SEQ ID NO: 23 are set forth herein as SEQ ID NOs: 10243-15978.

[0215] In some embodiments, the protein is derived from Aspergillus, Bacillus, Fusarium, Struthio, Talaromyces or Thermomyces. For example, in some embodiments, the protein is a native Aspergillus, Bacillus, Fusarium, Struthio, Talaromyces or Thermomyces triacylglycerol lipase, or a fragment / mutant / variant of a native Aspergillus, Bacillus, Fusarium, Struthio, Talaromyces or Thermomyces triacylglycerol lipase.

[0216] In some embodiments, the protein is derived from Aspergillus, Bacillus, Fusarium, Ostrich, Talaromyces, or Thermomyces. For example, in some embodiments, the protein is a native Aspergillus, Bacillus, Fusarium, Ostrich, Talaromyces, or Thermomyces phospholipase A 1, or a naturally occurring Aspergillus, Bacillus, Fusarium, Ostrich, Talaromyces, or Thermomyces phospholipase A 1 fragments / mutants / variants of.

[0217] In some embodiments, the protein is selected from the group consisting of:

[0218] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:24;

[0219] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:24;

[0220] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 115 or its cDNA sequence;

[0221] d) a polypeptide derived from any one of SEQ ID NO: 24 by substitution, deletion or insertion of one or more amino acids;

[0222] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 24 by substitution, deletion or insertion of one or more amino acids;

[0223] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0224] g) A fragment of the polypeptide of any one of a) to f)

[0225] Wherein the polypeptide has lysophospholipase activity belonging to EC 3.1.1.5. Examples of proteins exhibiting lysophospholipase activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 24 are set forth herein as SEQ ID NOs: 15979-15981.

[0226] In some embodiments, the protein is derived from Aspergillus. For example, in some embodiments, the protein is a native Aspergillus lysophospholipase, or a fragment / mutant / variant of a native Aspergillus lysophospholipase.

[0227] In some embodiments, the protein is selected from the group consisting of:

[0228] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:25;

[0229] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:25;

[0230] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 116 or its cDNA sequence;

[0231] d) a polypeptide derived from any one of SEQ ID NO: 25 by substitution, deletion or insertion of one or more amino acids;

[0232] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 25 by substitution, deletion or insertion of one or more amino acids;

[0233] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0234] g) A fragment of the polypeptide of any one of a) to f)

[0235] Wherein the polypeptide has pectinesterase activity belonging to EC 3.1.1.11. Examples of proteins exhibiting pectinesterase activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 25 are set forth herein as SEQ ID NOs: 2770-2777.

[0236] In some embodiments, the protein is derived from Aspergillus. For example, in some embodiments, the protein is a native Aspergillus pectinesterase, or a fragment / mutant / variant of a native Aspergillus pectinesterase.

[0237] In some embodiments, the protein is selected from the group consisting of:

[0238] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:26;

[0239] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:26;

[0240] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 117 or its cDNA sequence;

[0241] d) a polypeptide derived from any one of SEQ ID NO: 26 by substitution, deletion or insertion of one or more amino acids;

[0242] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 26 by substitution, deletion or insertion of one or more amino acids;

[0243] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0244] g) A fragment of the polypeptide of any one of a) to f)

[0245] wherein the polypeptide has a phospholipase A belonging to EC 3.1.1.32 1 Activity. Phospholipase A 1 Examples of proteins that are active and have an amino acid sequence that is at least 70% identical to SEQ ID NO: 26 are set forth herein as SEQ ID NOs: 10224-10242.

[0246] In some embodiments, the protein is derived from Evansstolkia. For example, in some embodiments, the protein is native Evansstolkia phospholipase A 1, or native Evansstolkia phospholipase A 1 fragments / mutants / variants of.

[0247] In some embodiments, the protein is selected from the group consisting of:

[0248] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 27-31, 72147, and 72149;

[0249] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 27-31, 72147 and 72149;

[0250] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 118-122, 72148 and 72150, or a cDNA sequence thereof;

[0251] d) a polypeptide derived from any one of SEQ ID NOs: 27-31, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0252] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 27-31, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0253] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0254] g) A fragment of the polypeptide of any one of a) to f)

[0255] Wherein the polypeptide has a cutinase activity belonging to EC 3.1.1.74. Examples of proteins exhibiting cutinase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 27-31, 72147 and 72149 are set forth herein as SEQ ID NOs: 15982-16004.

[0256] In some embodiments, the protein is derived from Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Mycorrhiza, Pyrenophora, Thermochaetoides, or Trichoderma. For example, in some embodiments, the protein is a native Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Mycorrhiza, Pyrenophora, Thermochaetoides, or Trichoderma cutinase, or is a fragment / mutant / variant of a native Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Mycorrhiza, Pyrenophora, Thermochaetoides, or Trichoderma cutinase.

[0257] In some embodiments, the protein is selected from the group consisting of:

[0258] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:32;

[0259] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:32;

[0260] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 123 or its cDNA sequence;

[0261] d) a polypeptide derived from any one of SEQ ID NO: 32 by substitution, deletion or insertion of one or more amino acids;

[0262] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 32 by substitution, deletion or insertion of one or more amino acids;

[0263] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0264] g) A fragment of the polypeptide of any one of a) to f)

[0265] Wherein the polypeptide has a phospholipase C activity belonging to EC 3.1.4.3. Examples of proteins exhibiting phospholipase C activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 32 are set forth herein as SEQ ID NOs: 16396-16412.

[0266] In some embodiments, the protein is derived from Pseudomonas. For example, in some embodiments, the protein is a native Pseudomonas phospholipase C, or a fragment / mutant / variant of a native Pseudomonas phospholipase C.

[0267] In some embodiments, the protein is selected from the group consisting of:

[0268] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:33;

[0269] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:33;

[0270] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 124 or its cDNA sequence;

[0271] d) a polypeptide derived from any one of SEQ ID NO: 33 by substitution, deletion or insertion of one or more amino acids;

[0272] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 33 by substitution, deletion or insertion of one or more amino acids;

[0273] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0274] g) A fragment of the polypeptide of any one of a) to f)

[0275] Wherein the polypeptide has phosphoinositide phospholipase C activity belonging to EC 3.1.4.11. Examples of proteins exhibiting phosphoinositide phospholipase C activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 33 are set forth herein as SEQ ID NOs: 16005-16395.

[0276] In some embodiments, the protein is derived from Bacillus, Saccharomyces cerevisiae, or Lysinibacillus. For example, in some embodiments, the protein is a native Bacillus, Saccharomyces cerevisiae, or Lysinibacillus phosphoinositide phospholipase C, or a fragment / mutant / variant of a native Bacillus, Saccharomyces cerevisiae, or Lysinibacillus phosphoinositide phospholipase C.

[0277] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more esterase activities belonging to EC 3.1. See, e.g., CA 2715086-A1; CN 102604913-A; CN103045559-A; CN 103243038-A; CN 103555600-A; CN 103865896-A; CN 103981160-A; CN104293744-A; CN 104878033-A; CN 105087614-A; CN 106591258-A; CN 106632683-A; CN106635846-A; CN 106676084-A; CN 106884030-A; CN 107151660-A; CN 107488644-A; CN107488645-A; CN 107488646-A; CN 107488647-A; CN 107488648-A; CN 107815460-A; CN108118039-A; CN 108239626-A; CN 108239627-A; CN 108277212-A; CN 108315312-A; CN108359655-A; CN 108913675-A; CN 109321546-A; CN 109468301-A; CN 109776686-A; CN109929821-A; CN 110129301-A; CN 110760531-A; CN 111378583-A; CN 112175976-A; CN112574974-A; CN 112592907-A; CN 112608912-A; CN 113025595-A; CN 113025596-A; CN113122520-A; CN 113215130-A; CN 113338044-A; CN 113736817-A; CN 113755509-A; CN113846074-A; CN 114317490-A; CN 114621941-A;CN 115521925-A; CN 115717134-A; DE102016204813-A1; EP 2145904-A1; EP 2623586-; 2; EP 305216-A; EP 3091080-A1; EP3101108-A1; EP 3101109-A1; EP 3284811-A1; EP 3287513-A1; EP 3301145-A1; EP3301147-A1; EP 3301156-A1;<h2 style=";text-align:left;direction:ltr">EP 3301161-A1;EP 3301162-A1;EP 3301163-A1;EP3301165-A1;EP 3301166-A1;EP 3301169-A1;JP 09249891-A;JP 09249893-A;JP2019165727-A;US 2005287250-A1;US 2007173430-A1;US 2009162480-A1;US2009217463-A1;US 2009217464-A1;US 2009221033-A1;US 2009221034-A1;US2011312057-A1;US 2013316458-A1;US 2018094228-A1;US 2019093054-A1;US2020306342-A1;US 2021015105-A1;US 2022177812-A1;US 9102933-B1;WO 2000060063-A1;WO 200011211-A1;WO 200034450-A1;WO 200127251-A1;WO 200192502-A1;WO200255679-A2;WO 200262973-A2;WO 200266622-A2;WO 200295127-A2;WO 2003060112-A1;WO 2003089620-A2;WO 2004099400-A2;WO 2004111216-A2;WO 2005032496-A2;WO2005086900-A2;WO 2006084470-A2;WO 2006136159-A2;WO 2006136160-A2;WO2007080197-A2;WO 2007087243-A2;WO 2007087318-A2;WO 2007087319-A2;WO2007087508-A2;WO 2008073169-A2;WO 2008079685-A2;WO 2008122640-A2;WO2009071550-A1;WO 2009083607-A1;WO 2009108941-A2;WO 2009133177-A1;WO2011046812-A1;WO 2011046815-A1;WO 2012027282-A2;WO 2012078741-A2;WO2012129548-A2;WO 2012173658-A1;WO 2013098205-A2;<h2 style=";text-align:left;direction:ltr">WO 2013113622-A1;WO2013149858-A1;WO 2013171072-A1;WO 2013181760-A1;WO 2014055778-A2;WO2014059360-A1;WO 2014059541-A1;WO 2014081700-A1;WO 2014081884-A1;WO2014147219-A1;WO 2014162001-A1;WO 2014184164-A1;WO 2014186464-A1;WO2015010009-A2;WO 2015017045-A1;WO 2015048332-A2;WO 2015067161-A1;WO2015085920-A1;WO 2015109405-A1;WO 2015110058-A1;WO 2015110562-A1;WO2015140275-A1;WO 2015144780-A2;WO2015173426-A1;WO 2016050661-A1;WO2016087401-A1;WO 2016090472-A1;WO 2016090473-A1;WO 2016090474-A1;WO2016091870-A1;WO 2016102356-A1;WO 2016107567-A1;WO 2016109758-A2;WO2016164596-A2;WO 2017001673-A1;WO 2017005640-A1;WO 2017015233-A1;WO2017093318-A1;WO 2017101801-A1;WO 2017161091-A1;WO 2017182666-A1;WO2018001959-A1;WO 2018015295-A1;WO 2018127486-A1;WO 2018171552-A1;WO2018188667-A1;WO 2019014118-A1;WO 2019060574-A1;WO 2019063499-A1;WO2019110462-A1;WO 2019137289-A1;WO 2019154951-A1;WO 2019154952-A1;WO2019154954-A1;WO 2019154955-A1;WO 2019215078-A1;WO 2019236717-A1;WO2020014407-A1;WO 2020046613-A1;<h2 style=";text-align:left;direction:ltr">WO 2020076697-A1;WO 2020088393-A1;WO2020103861-A1;WO 2020135657-A1;WO 2020135658-A1;WO 2020173817-A1;WO2020190782-A1;WO 2021037878-A1;WO 2021119304-A1;WO 2021170799-A1;WO2021239267-A1;WO 2022063699-A1;WO 2022090361-A2;WO 2022103725-A1;WO2022173694-A1;WO 2023032952-A1;WO 2023288294-A1;WO 9205249-A;WO 9219726-A1;WO9425575-A1;WO 9425577-A1;WO 9522615-A1;WO 9613580-A1;WO 9704079-A1;WO9707202-A1;WO 9707205-A1;WO 9707206-A1<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0278] In some embodiments, the proteins of the present disclosure exhibit one or more glycosylase activities belonging to EC 3.2, such as glycosidase activities belonging to EC 3.2.1 (e.g., α-amylase activity belonging to EC 3.2.1.1, β-amylase activity belonging to EC 3.2.1.2, glucan 1,4-α-glucosidase activity belonging to 3.2.1.3, cellulase activity belonging to 3.2.1.4, endo-1,3(4)-β-glucanase activity belonging to 3.2.1.6, inulinase activity belonging to 3.2.1.7, endo-1,4-β-xylanase activity belonging to 3.2.1.8, oligo-1,6- glucosidase activity, dextranase activity belonging to 3.2.1.11, chitinase activity belonging to 3.2.1.14, endo-polygalacturonase (pectinase) activity belonging to 3.2.1.15, lysozyme activity belonging to 3.2.1.17, α-glucosidase activity belonging to 3.2.1.20, β-glucosidase activity belonging to 3.2.1.21, α-galactosidase activity belonging to 3.2.1.22, β-galactosidase activity belonging to 3.2.1.23 Enzyme activity, α-mannosidase activity belonging to 3.2.1.24, β-mannosidase activity belonging to 3.2.1.25, β-fructofuranosidase activity belonging to 3.2.1.26, α,α-trehalase activity belonging to 3.2.1.28, endo-1,3-β-xylanase activity belonging to 3.2.1.32, amylo-1,6-glucosidase activity belonging to EC3.2.1.33, xylan 1,4-β-xylosidase activity belonging to 3.2.1.37 activity, endo-1,3-β-D-glucosidase activity belonging to 3.2.1.39, pullulanase activity belonging to 3.2.1.41, α-L-arabinofuranosidase activity belonging to 3.2.1.55, 1,3-β-glucosidase activity belonging to 3.2.1.58, endo-1,3-α-glucosidase activity belonging to 3.2.1.59, 1,6-α-glucosidase activity belonging to EC3.2.1.70, Glucan endo-1,2-β-glucosidase activity belonging to EC 3.2.1.71, xylan 1,3-β-xylosidase activity belonging to EC 3.2.1.72, licheninase activity belonging to 3.2.1.73, glucan 1,4-β-glucosidase activity belonging to EC 3.2.1.74, glucan endo-1,6-β-glucosidase activity belonging to 3.2.1.75, mannan 1,2-(1,3)-α-mannosidase activity belonging to EC 3.2.1.77, mannan endo-1,4-β-mannosidase activity belonging to 3.2.1.78, glucan 1,3-α-glucosidase activity belonging to EC 3.2.1.84, glucan 1,3-α-glucosidase activity belonging to 3.2.1.91, cellulose 1,4-β-cellobiosidase activity, peptidoglycan β-N-acetylmuramidase activity, endo-α-N-acetylgalactosaminidase activity, EC 3.2.1.97, mannan 1,4-mannobiosidase activity, EC 3.2.1.100, mannan endo-1,6-α-mannosidase activity, EC 3.2.1.101, endogalactosaminidase activity, EC 3.2.1.109, 1,3-α-L-fucosidase activity, EC 3.2.1.111, 2-deoxyglucosidase activity, EC 3.2.1.112, Glycoprotein endo-α-1,2-mannosidase activity belonging to EC 3.2.1.130, chitosanase activity belonging to 3.2.1.132, glucan 1,4-α-maltohydrolase activity belonging to 3.2.1.133, mannan exo-1,2-1,6-α-mannosidase activity belonging to EC 3.2.1.137, 1,6-α-D-mannosidase activity belonging to 3.2.1.163, 1,4-β-cellobiosidase activity belonging to 3.2.1.176, galactan endo-β-1,3-galactanase activity belonging to EC 3.2.1.181, α-mannan endo-1,2-α-mannanase activity belonging to EC 3.2.1.198, 3.2.1.200 exo-chitinase activity, exo-chitinase activity belonging to EC 3.2.1.201), and optionally comprising the same as SEQ ID NO:34-80, 45906 and 72144 as shown in one or more of about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical amino acid sequence.

[0279] In some embodiments, the protein is selected from the group consisting of:

[0280] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 34-40;

[0281] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 34-40;

[0282] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 125-131 or a cDNA sequence thereof;

[0283] d) a polypeptide derived from any one of SEQ ID NOs: 34-40 by substitution, deletion or insertion of one or more amino acids;

[0284] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 34-40 by substitution, deletion or insertion of one or more amino acids;

[0285] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0286] g) A fragment of the polypeptide of any one of a) to f)

[0287] Wherein the polypeptide has an alpha-amylase activity belonging to EC 3.2.1.1. Examples of proteins exhibiting alpha-amylase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 34-40 are set forth herein as SEQ ID NOs: 16413-45041.

[0288] In some embodiments, the protein is derived from Alicyclobacillus, Alkalihalobacillus, Anoxybacillus, Aspergillus, Bacillus, Cytophaga, Exiguobacterium, Geobacillus, Hamigera, Homo sapiens, Jeotgalibacillus, Neosartorya, Penicillium, Priestia, Pyrococcus, Rosalia, Sutcliffiella, or Thermoascus. For example, in some embodiments, the protein is a natural Alicyclobacillus, Alkaline Halobacter, Anoxic Bacillus, Aspergillus, Bacillus, Cellulophagus, Exiguobacterium, Geobacillus, Uncinaria, Homo sapiens, Seafood Bacillus, Neosartorya, Penicillium, Priesteria, Pyrococcus, Rosalia, Saxcliffia, or Thermoascus alpha-amylase, or is a fragment / mutant / variant of a natural Alicyclobacillus, Alkaline Halobacter, Anoxic Bacillus, Aspergillus, Bacillus, Cellulophagus, Exiguobacterium, Geobacillus, Uncinaria, Homo sapiens, Seafood Bacillus, Neosartorya, Penicillium, Priesteria, Pyrococcus, Rosalia, Saxcliffia, or Thermoascus alpha-amylase.

[0289] In some embodiments, the protein is selected from the group consisting of:

[0290] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:41-42;

[0291] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:41-42;

[0292] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 132-133 or their cDNA sequences;

[0293] d) a polypeptide derived from any one of SEQ ID NOs: 41-42 by substitution, deletion or insertion of one or more amino acids;

[0294] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 41-42 by substitution, deletion or insertion of one or more amino acids;

[0295] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0296] g) A fragment of the polypeptide of any one of a) to f)

[0297] Wherein the polypeptide has glucan 1,4-α-glucosidase activity belonging to EC 3.2.1.3. Examples of proteins exhibiting glucan 1,4-α-glucosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 41-42 are shown herein as SEQ ID NOs: 45756-45904.

[0298] In some embodiments, the protein is derived from Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rosacea or Saccharomycopsis. For example, in some embodiments, the protein is a natural Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rosacea or Saccharomycopsis glucan 1,4-α-glucosidase, or a fragment / mutant / variant of a natural Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rosacea or Saccharomycopsis glucan 1,4-α-glucosidase.

[0299] In some embodiments, the protein is selected from the group consisting of:

[0300] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:43-45;

[0301] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:43-45;

[0302] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 134-136 or their cDNA sequences;

[0303] d) a polypeptide derived from any one of SEQ ID NOs: 43-45 by substitution, deletion or insertion of one or more amino acids;

[0304] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 43-45 by substitution, deletion or insertion of one or more amino acids;

[0305] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0306] g) A fragment of the polypeptide of any one of a) to f)

[0307] Wherein the polypeptide has cellulase activity belonging to EC 3.2.1.4. Examples of proteins exhibiting cellulase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 43-45 are set forth herein as SEQ ID NOs: 45913-48750.

[0308] In some embodiments, the protein is derived from Acremonium, Alteromonas, Ascomycota, Aspergillus, Bacillus, Chaetomium, Clonostachys, Corynascus, Cylindrocarpon, Escherichia, Fusarium, Humicola, Madurella, Melanocarpus, Myceliophthora, Neurospora, Podospora, Remersonia, Stigmata, Sordaria, Staphylotrichum, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Trichocladium, Trichothecium, or Triticum. For example, in some embodiments, the protein is a native Acremonium, Alteromonas, Ascomycota, Aspergillus, Bacillus, Chaetomium, Spiropolysporus, Corymbinocytosis, Cylindrosporium, Escherichia, Fusarium, Humicola, Madura, Melanocarpus, Myceliophthora, Neurospora, Podospora, Remersonia, Cylindrosporium, Sordella, Cyclospora, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Helminthosporium, Trichothecene, or Triticum cellulase. , or a fragment / mutant / variant of a native Acremonium, Alteromonas, Ascomycota, Aspergillus, Bacillus, Chaetomium, Spirocystis, Corymbia, Cylindrosporium, Escherichia, Fusarium, Humicola, Maduraciella, Melanocarpus, Myceliophthora, Neurospora, Podospora, Remersonia, Cylindrocystis, Sordella, Cyclospora, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Helminthosporium, Trichothecene, or Triticum cellulase.

[0309] In some embodiments, the protein is selected from the group consisting of:

[0310] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:46;

[0311] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:46;

[0312] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 137 or its cDNA sequence;

[0313] d) a polypeptide derived from any one of SEQ ID NO: 46 by substitution, deletion or insertion of one or more amino acids;

[0314] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 46 by substitution, deletion or insertion of one or more amino acids;

[0315] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0316] g) A fragment of the polypeptide of any one of a) to f)

[0317] Wherein the polypeptide has endo-1,3(4)-β-glucanase activity belonging to EC 3.2.1.6. Examples of proteins exhibiting endo-1,3(4)-β-glucanase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 46 are set forth herein as SEQ ID NOs: 49229-49346.

[0318] In some embodiments, the protein is derived from Bacillus, Bispora, Hordeum, or Paenibacillus. For example, in some embodiments, the protein is a native Bacillus, Bispora, Hordeum, or Paenibacillus endo-1,3(4)-β-glucanase, or a fragment / mutant / variant of a native Bacillus, Bispora, Hordeum, or Paenibacillus endo-1,3(4)-β-glucanase.

[0319] In some embodiments, the protein is selected from the group consisting of:

[0320] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:47;

[0321] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:47;

[0322] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 138 or its cDNA sequence;

[0323] d) a polypeptide derived from any one of SEQ ID NO: 47 by substitution, deletion or insertion of one or more amino acids;

[0324] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 47 by substitution, deletion or insertion of one or more amino acids;

[0325] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0326] g) A fragment of the polypeptide of any one of a) to f)

[0327] Wherein the polypeptide has inulinase activity belonging to EC 3.2.1.7. Examples of proteins exhibiting inulinase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 47 are set forth herein as SEQ ID NOs: 49347-49419.

[0328] In some embodiments, the protein is derived from Aspergillus, Penicillium, Pseudomonas, or Talaromyces. For example, in some embodiments, the protein is a natural Aspergillus, Penicillium, Pseudomonas, or Talaromyces inulinase, or a fragment / mutant / variant of a natural Aspergillus, Penicillium, Pseudomonas, or Talaromyces inulinase.

[0329] In some embodiments, the protein is selected from the group consisting of:

[0330] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:48-53;

[0331] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:48-53;

[0332] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 139-144 or their cDNA sequences;

[0333] d) a polypeptide derived from any one of SEQ ID NOs: 48-53 by substitution, deletion or insertion of one or more amino acids;

[0334] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 48-53 by substitution, deletion or insertion of one or more amino acids;

[0335] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0336] g) A fragment of the polypeptide of any one of a) to f)

[0337] Wherein the polypeptide has endo-1,4-β-xylanase activity belonging to EC 3.2.1.8. Examples of proteins exhibiting endo-1,4-β-xylanase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 48-53 are set forth herein as SEQ ID NOs: 49453-49912.

[0338] In some embodiments, the protein is derived from Anaerocellum, Aspergillus, Bacillus, Caldicellulosiruptor, Clostridium, Dicytoglomus, Evansstolkia, Hordeum, Lactobacillus, Malbranchea, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rosalia, Saccharomyces, Talaromyces, Thermoclostridium, Thermomyces, Thermus, or Viridiplantae. For example, in some embodiments, the protein is a native anaerobic cellulolytic bacteria, Aspergillus, Bacillus, Thermocellulosus, Clostridium, Dictyoglobulus, Evansstolkia, Hordeum, Lactobacillus, Trichoderma, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rosalia, Saccharomyces, Talaromyces, Thermoclostridium, Thermomyces, Thermus, or Viride endo-1,4-β-xylanase , or a fragment / mutant / variant of a natural anaerobic cellulolytic bacteria, Aspergillus, Bacillus, Thermocellulosus, Clostridium, Dictyoglobulus, Evansstolkia, Hordeum, Lactobacillus, Trichoderma, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rosalia, Saccharomyces, Talaromyces, Thermoclostridium, Thermomyces, Thermus, or a green plant kingdom endo-1,4-β-xylanase.

[0339] In some embodiments, the protein is selected from the group consisting of:

[0340] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:54;

[0341] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:54;

[0342] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 145 or its cDNA sequence;

[0343] d) a polypeptide derived from any one of SEQ ID NO: 54 by substitution, deletion or insertion of one or more amino acids;

[0344] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 54 by substitution, deletion or insertion of one or more amino acids;

[0345] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0346] g) A fragment of the polypeptide of any one of a) to f)

[0347] Wherein the polypeptide has dextranase activity belonging to EC 3.2.1.11. Examples of proteins exhibiting dextranase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 54 are set forth herein as SEQ ID NOs: 45063-45071.

[0348] In some embodiments, the protein is selected from the group consisting of:

[0349] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:56;

[0350] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:56;

[0351] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 147 or its cDNA sequence;

[0352] d) a polypeptide derived from any one of SEQ ID NO: 56 by substitution, deletion or insertion of one or more amino acids;

[0353] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 56 by substitution, deletion or insertion of one or more amino acids;

[0354] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0355] g) A fragment of the polypeptide of any one of a) to f)

[0356] Wherein the polypeptide has lysozyme activity belonging to EC 3.2.1.17. Examples of proteins exhibiting lysozyme activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 56 are set forth herein as SEQ ID NOs: 45443-45456.

[0357] In some embodiments, the protein is derived from Synechocystis or Sodiomyces. For example, in some embodiments, the protein is a native Synechocystis or Sodiomyces lysozyme, or a fragment / mutant / variant of a native Synechocystis or Sodiomyces lysozyme.

[0358] In some embodiments, the protein is selected from the group consisting of:

[0359] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:57;

[0360] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:57;

[0361] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 148 or its cDNA sequence;

[0362] d) a polypeptide derived from any one of SEQ ID NO: 57 by substitution, deletion or insertion of one or more amino acids;

[0363] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 57 by substitution, deletion or insertion of one or more amino acids;

[0364] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0365] g) A fragment of the polypeptide of any one of a) to f)

[0366] Wherein the polypeptide has β-glucosidase activity belonging to EC 3.2.1.21. Examples of proteins exhibiting β-glucosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 57 are set forth herein as SEQ ID NOs: 45457-45754.

[0367] In some embodiments, the protein is derived from Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rosatella, Schizosaccharomyces, or Thermoascus. For example, in some embodiments, the protein is a native Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rosatella, Schizosaccharomyces, or Thermoascus beta-glucosidase, or a fragment / mutant / variant of a native Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rosatella, Schizosaccharomyces, or Thermoascus beta-glucosidase.

[0368] In some embodiments, the protein is selected from the group consisting of:

[0369] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:58;

[0370] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:58;

[0371] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 149 or its cDNA sequence;

[0372] d) a polypeptide derived from any one of SEQ ID NO: 58 by substitution, deletion or insertion of one or more amino acids;

[0373] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 58 by substitution, deletion or insertion of one or more amino acids;

[0374] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0375] g) A fragment of the polypeptide of any one of a) to f)

[0376] Wherein the polypeptide has α-mannosidase activity belonging to EC 3.2.1.24. An example of a protein exhibiting α-mannosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO:58 is shown herein as SEQ ID NO:45755.

[0377] In some embodiments, the protein is derived from Neobacillus. For example, in some embodiments, the protein is a native Neobacillus α-mannosidase, or a fragment / mutant / variant of a native Neobacillus α-mannosidase.

[0378] In some embodiments, the protein is selected from the group consisting of:

[0379] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 59-60 and 45906;

[0380] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 59-60 and 45906;

[0381] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 150-151 and 72146 or a cDNA sequence thereof;

[0382] d) a polypeptide derived from any one of SEQ ID NOs: 59-60 and 45906 by substitution, deletion or insertion of one or more amino acids;

[0383] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 59-60 and 45906 by substitution, deletion or insertion of one or more amino acids;

[0384] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0385] g) A fragment of the polypeptide of any one of a) to f)

[0386] Wherein the polypeptide has endo-1,3-β-D-glucosidase activity belonging to EC 3.2.1.39. Examples of proteins that exhibit endo-1,3-β-D-glucosidase activity and have an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 59-60 and 45906 are shown herein as SEQ ID NOs: 45905-45912.

[0387] In some embodiments, the protein is derived from Trichoderma. For example, in some embodiments, the protein is a native Trichoderma endo-1,3-β-D-glucosidase, or a fragment / mutant / variant of a native Trichoderma endo-1,3-β-D-glucosidase.

[0388] In some embodiments, the protein is selected from the group consisting of:

[0389] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:61;

[0390] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:61;

[0391] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 152 or its cDNA sequence;

[0392] d) a polypeptide derived from any one of SEQ ID NO: 61 by substitution, deletion or insertion of one or more amino acids;

[0393] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 61 by substitution, deletion or insertion of one or more amino acids;

[0394] f) a polypeptide derived from the polypeptide of any one of a) to f), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0395] g) A fragment of the polypeptide of any one of a) to g)

[0396] Wherein the polypeptide has pullulanase activity belonging to EC 3.2.1.41. Examples of proteins exhibiting pullulanase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 61 are set forth herein as SEQ ID NOs: 48751-49148.

[0397] In some embodiments, the protein is derived from Bacillus, Geobacillus, or Pulluanibacillus. For example, in some embodiments, the protein is a native Bacillus, Geobacillus, or Pulluanibacillus pullulanase, or a fragment / mutant / variant of a native Bacillus, Geobacillus, or Pulluanibacillus pullulanase.

[0398] In some embodiments, the protein is selected from the group consisting of:

[0399] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:62;

[0400] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:62;

[0401] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 153 or its cDNA sequence;

[0402] d) a polypeptide derived from any one of SEQ ID NO: 62 by substitution, deletion or insertion of one or more amino acids;

[0403] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 62 by substitution, deletion or insertion of one or more amino acids;

[0404] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0405] g) A fragment of the polypeptide of any one of a) to f)

[0406] Wherein the polypeptide has α-L-arabinofuranosidase activity belonging to EC 3.2.1.55. Examples of proteins exhibiting α-L-arabinofuranosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 62 are shown herein as SEQ ID NOs: 49149-49209.

[0407] In some embodiments, the protein is derived from Acremonium, Endocytosis, Actinomadura, Actinoplanes, Aspergillus, Aureobasidium, Chaetomium, Gliomastix, Humicola, Hypocrea, Microdochium, Myceliophthora, Oculimacula, Penicillium, Streptomyces, Streptosporangium, Talaromyces, Thielavia, Trichoderma, or Xylanibacterium. For example, in some embodiments, the protein is a native Acremonium, Acanthopanax, Actinomyces madurai, Actinomyces aeruginosa, Aspergillus, Acanthopanax, Chaetomium, Glechoma, Humicola, Hypocrea, Microdochium, Myceliophthora, Oculimacula, Penicillium, Streptomyces, Neurospora, Talaromyces, Thielavia, Trichoderma, or Xylanolyticus α-L-arabinofuranosidase , or a fragment / mutant / variant of a native Acremonium, Terminalia, Madura, Actinomyces, Aspergillus, Acanthopanax, Chaetomium, Glechoma, Humicola, Hypocrea, Microsporum, Myceliophthora, Oculimacula, Penicillium, Streptomyces, Neurospora, Talaromyces, Thielavia, Trichoderma or Xylanolyticus α-L-arabinofuranosidase.

[0408] In some embodiments, the protein is selected from the group consisting of:

[0409] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 63-64;

[0410] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 63-64;

[0411] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 154-155, or a cDNA sequence thereof;

[0412] d) a polypeptide derived from any one of SEQ ID NOs: 63-64 by substitution, deletion or insertion of one or more amino acids;

[0413] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 63-64 by substitution, deletion or insertion of one or more amino acids;

[0414] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0415] g) A fragment of the polypeptide of any one of a) to f)

[0416] Wherein the polypeptide has endo-1,3-α-glucosidase activity belonging to EC 3.2.1.59. Examples of proteins exhibiting endo-1,3-α-glucosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 63-64 are shown herein as SEQ ID NOs: 49210-49228.

[0417] In some embodiments, the protein is derived from the genus Spirocystis, Hypocrea, Myceliophthora, or Trichoderma. For example, in some embodiments, the protein is a native Spirocystis, Hypocrea, Myceliophthora, or Trichoderma glucan endo-1,3-α-glucosidase, or a fragment / mutant / variant of a native Spirocystis, Hypocrea, Myceliophthora, or Trichoderma glucan endo-1,3-α-glucosidase.

[0418] In some embodiments, the protein is selected from the group consisting of:

[0419] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:65;

[0420] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:65;

[0421] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 156 or its cDNA sequence;

[0422] d) a polypeptide derived from any one of SEQ ID NO: 65 by substitution, deletion or insertion of one or more amino acids;

[0423] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 65 by substitution, deletion or insertion of one or more amino acids;

[0424] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0425] g) A fragment of the polypeptide of any one of a) to f)

[0426] Wherein the polypeptide has lichenase activity belonging to EC 3.2.1.73. Examples of proteins exhibiting lichenase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 65 are set forth herein as SEQ ID NOs: 49420-49446.

[0427] In some embodiments, the protein is derived from Bacillus or Salipaludibacillus. For example, in some embodiments, the protein is a native Bacillus or Salipaludibacillus lichenase, or a fragment / mutant / variant of a native Bacillus or Salipaludibacillus lichenase.

[0428] In some embodiments, the protein is selected from the group consisting of:

[0429] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 66-67;

[0430] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 66-67;

[0431] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 157-158 or their cDNA sequences;

[0432] d) a polypeptide derived from any one of SEQ ID NOs: 66-67 by substitution, deletion or insertion of one or more amino acids;

[0433] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 66-67 by substitution, deletion or insertion of one or more amino acids;

[0434] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0435] g) A fragment of the polypeptide of any one of a) to f)

[0436] Wherein the polypeptide has endo-1,6-β-glucosidase activity belonging to EC 3.2.1.75. Examples of proteins exhibiting endo-1,6-β-glucosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 66-67 are shown herein as SEQ ID NOs: 49447-49451.

[0437] In some embodiments, the protein is derived from Trichoderma. For example, in some embodiments, the protein is a native Trichoderma endo-1,6-β-glucosidase, or a fragment / mutant / variant of a native Trichoderma endo-1,6-β-glucosidase.

[0438] In some embodiments, the protein is selected from the group consisting of:

[0439] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 68 and 72144;

[0440] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 68 and 72144;

[0441] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 159 and 72145, or a cDNA sequence thereof;

[0442] d) a polypeptide derived from any one of SEQ ID NOs: 68 and 72144 by substitution, deletion or insertion of one or more amino acids;

[0443] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 68 and 72144 by substitution, deletion or insertion of one or more amino acids;

[0444] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0445] g) A fragment of the polypeptide of any one of a) to f)

[0446] Wherein the polypeptide has endomannan-1,4-β-mannosidase activity belonging to EC 3.2.1.78. An example of a protein exhibiting endomannan-1,4-β-mannosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 68 and 72144 is shown herein as SEQ ID NO: 49452.

[0447] In some embodiments, the protein is derived from Halobacter spp. For example, in some embodiments, the protein is a native Halobacter spp. endo-1,4-β-mannosidase, or a fragment / mutant / variant of a native Halobacter spp. endo-1,4-β-mannosidase.

[0448] In some embodiments, the protein is selected from the group consisting of:

[0449] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:69;

[0450] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:69;

[0451] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 160 or its cDNA sequence;

[0452] d) a polypeptide derived from any one of SEQ ID NO: 69 by substitution, deletion or insertion of one or more amino acids;

[0453] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 69 by substitution, deletion or insertion of one or more amino acids;

[0454] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0455] g) A fragment of the polypeptide of any one of a) to f)

[0456] Wherein the polypeptide has endomannan-1,6-α-mannosidase activity belonging to EC 3.2.1.101. An example of a protein exhibiting endomannan-1,6-α-mannosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 69 is shown herein as SEQ ID NO: 45042.

[0457] In some embodiments, the protein is derived from Talaromyces. For example, in some embodiments, the protein is a native Talaromyces endo-1,6-α-mannosidase, or a fragment / mutant / variant of a native Talaromyces endo-1,6-α-mannosidase.

[0458] In some embodiments, the protein is selected from the group consisting of:

[0459] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:70-75;

[0460] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:70-75;

[0461] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 161-166 or a cDNA sequence thereof;

[0462] d) a polypeptide derived from any one of SEQ ID NOs: 70-75 by substitution, deletion or insertion of one or more amino acids;

[0463] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 70-75 by substitution, deletion or insertion of one or more amino acids;

[0464] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0465] g) A fragment of the polypeptide of any one of a) to f)

[0466] Wherein the polypeptide has endogalactosaminidase activity belonging to EC 3.2.1.109. Examples of proteins exhibiting endogalactosaminidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 70-75 are set forth herein as SEQ ID NOs: 45043-45062.

[0467] In some embodiments, the protein is derived from Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urunula. For example, in some embodiments, the protein is a native Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urunula endogalactosidase, or is a fragment / mutant / variant of a native Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urunula endogalactosidase.

[0468] In some embodiments, the protein is selected from the group consisting of:

[0469] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:76-77;

[0470] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:76-77;

[0471] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 167-168 or a cDNA sequence thereof;

[0472] d) a polypeptide derived from any one of SEQ ID NOs: 76-77 by substitution, deletion or insertion of one or more amino acids;

[0473] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 76-77 by substitution, deletion or insertion of one or more amino acids;

[0474] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0475] g) A fragment of the polypeptide of any one of a) to f)

[0476] The polypeptide has glycoprotein endo-α-1,2-mannosidase activity belonging to EC 3.2.1.130 and / or α-mannan endo-1,2-α-mannanase activity belonging to EC 3.2.1.198.

[0477] In some embodiments, the protein is derived from Chryseobacterium or Lysobacter. For example, in some embodiments, the protein is a natural Chryseobacterium or Lysobacter glycoprotein endo-α-1,2-mannosidase, or a fragment / mutant / variant of a natural Chryseobacterium or Lysobacter glycoprotein endo-α-1,2-mannosidase. Similarly, in some embodiments, the protein is a natural Chryseobacterium or Lysobacter α-mannan endo-1,2-α-mannanase, or a fragment / mutant / variant of a natural Chryseobacterium or Lysobacter α-mannan endo-1,2-α-mannanase.

[0478] In some embodiments, the protein is selected from the group consisting of:

[0479] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:78;

[0480] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:78;

[0481] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 169 or its cDNA sequence;

[0482] d) a polypeptide derived from any one of SEQ ID NO: 78 by substitution, deletion or insertion of one or more amino acids;

[0483] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 78 by substitution, deletion or insertion of one or more amino acids;

[0484] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0485] g) A fragment of the polypeptide of any one of a) to f)

[0486] Wherein the polypeptide has glucan 1,4-α-maltose hydratase activity belonging to EC 3.2.1.133. Examples of proteins exhibiting glucan 1,4-α-maltose hydratase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 78 are shown herein as SEQ ID NOs: 45072-45408.

[0487] In some embodiments, the protein is derived from Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus. For example, in some embodiments, the protein is a natural Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus glucan 1,4-α-maltose hydratase, or a fragment / mutant / variant of a natural Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus glucan 1,4-α-maltose hydratase.

[0488] In some embodiments, the protein is selected from the group consisting of:

[0489] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:79;

[0490] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:79;

[0491] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 170 or its cDNA sequence;

[0492] d) a polypeptide derived from any one of SEQ ID NO: 79 by substitution, deletion or insertion of one or more amino acids;

[0493] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 79 by substitution, deletion or insertion of one or more amino acids;

[0494] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0495] g) A fragment of the polypeptide of any one of a) to f)

[0496] Wherein the polypeptide has 1,6-α-D-mannosidase activity belonging to EC 3.2.1.163. Examples of proteins exhibiting 1,6-α-D-mannosidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 79 are shown herein as SEQ ID NOs: 45437-45442.

[0497] In some embodiments, the protein is derived from Aspergillus, Evansstolkia, Penicillium, Rosalia, Talaromyces, or Thermomyces. For example, in some embodiments, the protein is a native Aspergillus, Evansstolkia, Penicillium, Rosalia, Talaromyces, or Thermomyces 1,6-α-D-mannosidase, or a fragment / mutant / variant of a native Aspergillus, Evansstolkia, Penicillium, Rosalia, Talaromyces, or Thermomyces 1,6-α-D-mannosidase.

[0498] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more glycosylase activities belonging to EC 3.2. See, e.g., AU2016101771-A4; AU2017203481-A1; BY20193-C1; CN101134949-A; CN101139556-A; CN101173226-A; CN101298604-A; CN101457230-A; CN101492661-A; CN101659948-A; CN101824401-A; CN101870956-A; CN101899458-A; CN101962633-A; CN102021191-A; CN102477437-A; CN1024 77438-A; CN102492707-A; CN102703480-A; CN102796751-A; CN102827821-A; CN102851266-A; CN102994475-A; CN103060290-A; CN103184163- A; CN103194419-A; CN103343111-A; CN103525793-A; CN103555751-A; CN103789285-A; CN103805579-A; CN103834606-A; CN103966188-A; CN10 CN104498456-A; CN104561060-A; CN10478954 3-A; CN104862290-A; CN104928270-A; CN105039288-A; CN105062991-A; CN105155324-A; CN105176947-A; CN105177084-A; CN105441415-A; CN 105623937-A; CN105671019-A; CN105671022-A; CN105695435-A; CN105734034-A; CN105802940-A; CN105802943-A; CN105886520-A; CN105907 775-A; CN105969783-A; CN106084016-A; CN106148235-A; CN106190934-A; CN106754825-A; CN106754826-A; CN106801046-A; CN106929495-A;CN107022588-A;CN107058264-A;CN107236692-A;CN107312763-A;CN107326020-A;CN107475219-A;CN107513527-A;CN107586767-A;CN107603965-A;CN108102934-A;CN108588056-A;CN108611339-A;CN108623652-A;CN108795781-A;CN108823186-A;CN108841809-A;CN109022396-A;CN109055439-A;CN109207458-A;CN109234339-A;CN109321552-A;CN109370973-A;CN109439607-A;CN109439641-A;CN109486689-A;CN109486791-A;CN109777795-A;CN109810961-A;CN109825466-A;CN109897842-A;CN110066777-A;CN110157688-A;CN110229800-A;CN110343687-A;CN110423737-A;CN110495549-A;CN110592051-A;CN110628748-A;CN110699337-A;CN110713999-A;CN110724645-A;CN110724646-A;CN110951628-A;CN111454929-A;CN111500558-A;CN111518792-A;CN111621490-A;CN111793613-A;CN111826377-A;CN112063678-A;CN112342208-A;CN112522238-A;CN112552382-A;CN112680433-A;CN112795554-A;CN112795555-A;CN113151327-A;CN113234705-A;CN113584075-A;CN113667662-A;CN113717864-A;CN113817709-A;CN113881654-A;CN114350637-A;CN114369588-A;CN114457056-A;CN114606216-A;CN114686386-A;CN114752583-A;CN114790451-A;CN115029334-A;<h2 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[0499] In some embodiments, the proteins of the present disclosure exhibit one or more peptidase activities belonging to EC 3.4, such as aminopeptidase activity belonging to EC 3.4.11, serine endopeptidase activity belonging to EC 3.4.21 (e.g., chymotrypsin activity belonging to EC 3.4.21.1, trypsin activity belonging to EC 3.4.21.4, α-lytic endopeptidase activity belonging to EC 3.4.21.12, glutamyl endopeptidase activity belonging to EC 3.4.21.19, cucumisin activity belonging to EC 3.4.21.25, chymase activity belonging to EC 3.4.21.39, lysyl endopeptidase activity belonging to EC 3.4.21.50, leucyl endopeptidase activity belonging to EC 3.4.21.57, subtilisin activity belonging to 3.4.21.62), cysteine ​​endopeptidase activity belonging to 3.4.22 (e.g., cysteine ​​endopeptidase activity belonging to EC 3.4.21.63). 4.22.40), and / or metalloendopeptidase activity belonging to EC 3.4.24 (e.g., phytepsin activity belonging to EC 3.4.24.41). 3.4.24.28 bacillolysin activity), and optionally comprises, consists essentially of, or consists of an amino acid sequence that is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to one or more of the amino acid sequences set forth herein as SEQ ID NOs: 80-88.

[0500] In some embodiments, the proteins of the present disclosure exhibit serine endoprotease activity belonging to EC 3.4.21, and optionally comprise, consist essentially of, or consist of an amino acid sequence that is about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the amino acid sequences set forth herein as SEQ ID NOs: 80-86.

[0501] In some embodiments, the protein is selected from the group consisting of:

[0502] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 80-81;

[0503] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 80-81;

[0504] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 171-172 or a cDNA sequence thereof;

[0505] d) a polypeptide derived from any one of SEQ ID NOs: 80-81 by substitution, deletion or insertion of one or more amino acids;

[0506] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 80-81 by substitution, deletion or insertion of one or more amino acids;

[0507] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0508] g) A fragment of the polypeptide of any one of a) to f)

[0509] Wherein the polypeptide has serine endopeptidase activity belonging to EC 3.4.21. Examples of proteins exhibiting serine endopeptidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 80-81 are set forth herein as SEQ ID NOs: 49913-50777.

[0510] In some embodiments, the protein is derived from Cinereomyces, Dichomitus, Ganoderma, Grifola, Lenzites, Meripilus, Neolentinus, Nocardiopsis, Polyporus, or Trametes. For example, in some embodiments, the protein is a native Cinereomyces, Formospora, Ganoderma, Grifola, Levaccine, Grifola, Neo-Lentinus, Pseudomonas, Polyporus, or Trametes serine endopeptidase, or a fragment / mutant / variant of a native Cinereomyces, Formospora, Ganoderma, Grifola, Levaccine, Grifola, Neo-Lentinus, Pseudomonas, Polyporus, or Trametes serine endopeptidase.

[0511] In some embodiments, the protein is selected from the group consisting of:

[0512] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:82;

[0513] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:82;

[0514] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 173 or its cDNA sequence;

[0515] d) a polypeptide derived from any one of SEQ ID NO: 82 by substitution, deletion or insertion of one or more amino acids;

[0516] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 82 by substitution, deletion or insertion of one or more amino acids;

[0517] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0518] g) A fragment of the polypeptide of any one of a) to f)

[0519] Wherein the polypeptide has glutamyl endopeptidase activity belonging to EC 3.4.21.19. Examples of proteins exhibiting glutamyl endopeptidase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 82 are set forth herein as SEQ ID NOs: 50778-50953.

[0520] In some embodiments, the protein is derived from Bacillus. For example, in some embodiments, the protein is a native Bacillus glutamyl endopeptidase, or a fragment / mutant / variant of a native Bacillus glutamyl endopeptidase.

[0521] In some embodiments, the protein is selected from the group consisting of:

[0522] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 83-87;

[0523] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:83-87;

[0524] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SQ ID NOs: 174-178 or a cDNA sequence thereof;

[0525] d) a polypeptide derived from any one of SEQ ID NOs: 83-87 by substitution, deletion or insertion of one or more amino acids;

[0526] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 83-87 by substitution, deletion or insertion of one or more amino acids;

[0527] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0528] g) A fragment of the polypeptide of any one of a) to f)

[0529] Wherein the polypeptide has subtilisin activity belonging to EC 3.4.21.62. Examples of proteins exhibiting subtilisin activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 83-87 are set forth herein as SEQ ID NOs: 50954-70838.

[0530] In some embodiments, the protein is derived from alkaline Halobacter, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus. For example, in some embodiments, the protein is a natural alkaline Halobacter, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus subtilisin, or a fragment / mutant / variant of a natural alkaline Halobacter, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus subtilisin.

[0531] In some embodiments, the protein is selected from the group consisting of:

[0532] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:88;

[0533] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:88;

[0534] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 179 or its cDNA sequence;

[0535] d) a polypeptide derived from any one of SEQ ID NO: 88 by substitution, deletion or insertion of one or more amino acids;

[0536] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 88 by substitution, deletion or insertion of one or more amino acids;

[0537] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0538] g) A fragment of the polypeptide of any one of a) to f)

[0539] Wherein the polypeptide has a bacilliosin activity belonging to EC 3.4.24.28. Examples of proteins exhibiting bacilliosin activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 88 are set forth herein as SEQ ID NOs: 70839-71903.

[0540] In some embodiments, the protein is derived from Bacillus. For example, in some embodiments, the protein is a native Bacillus bacillisin, or a fragment / mutant / variant of a native Bacillus bacillisin.

[0541] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more peptidase activities belonging to EC 3.4. See, e.g., CA2829859-A1; CN102676561-A; CN102703482-A; CN103013960-A; CN103243081-A; CN103255156-A; CN103602653-A; CN104232610-A; CN105132397-A; CN105176951-A; CN106350530-; CN106801048-A; CN107384897-A; CN107828765-A; CN107937372-A; CN107937374-A; CN108004 C N110819612-A; CN110862979-A; CN110923221-A; CN110923222-; CN111004794-A; CN111334494-A; CN111575265-A; CN111893126-A; CN111909 C N113832130-A; CN113832131-A; CN113862244-A; CN114107266-A; CN114317502-; CN114540330-A; CN114561375-A; CN114574469-A; CN114591 C N1361279-A; CN1814746-A; CN1814755-A; CN1995343-A; DE102006022224-A1; DE102007044415-1; DE102007049830-A1; DE102007051092-A1;DE102008059446-A1;DE102008059447-A1;DE102009029513-A1;DE102010028951-A1;DE102011005354-A1;DE102011118032-A1;DE102012215642-A1;DE102012220101-A1;DE102013219467-A1;DE102013221206-A1;DE102014212643-A1;DE102014224825-A1;DE102014226681-A1;DE102015223270-A1;DE102016204814-A1;DE102016204815-A1;DE102016208463-A1;DE102016210628-A1;DE102017215628-A1;DE102017215629-A1;DE102017215631-A1;DE102017223275-A1;DE102018004206-A1;DE102018004207-A1;DE102019111047-A1;DE102019111057-A1;DE102019111075-A1;DE102019210806-A1;DE102020105720-A1;DE102020105721-A1;DE102020205381-A1;DE102020205400-A1;DE10260903-A1;DE19530816-A1;DE3821491-A;DE4224125-A1;DE4411223-A1;EP1160327-A2;EP133756-A;EP2100948-A1;EP2607468-A1;EP3106508-A1;EP3275988-A1;EP3301155-A1;EP3309244-A1;EP3323875-A1;EP3339423-A1;EP3660146-A1;EP3660151-A1;EP398539-A;EP405901-A;EP405902-A;EP415296-A;EP416967-A;EP430637-A;EP443476-A;EP482879-A;EP516200-A1;EP571049-A1;EP687733-A1;JP01137972-A;JP02076586-A;JP11137282-A;JP2004043660-A;JP2004313043-A;<h2 style=";text-align:left;direction:ltr">JP2008022828-A;JP2011234685-A;JP2016121081-A;JP201707963 9-A;JP2022045888-A;US2004091474-A1;US2004197894-A1;US2004 223962-A1;US2009087888-A1;US2012067373-A1;US2013123162-A1 ;US2015125925-A1;US2016032267-A1;US2019185788-A1;US201918 5789-A1;US2020306342-A1;US2021122997-A1;US2022098524-A1;U S4980288-A;US5260207-A;US5316935-A;US5316941-A;US5371008- A;US5472855-A;US5652136-A;US5677272-A;US5679630-A;US57190 21-A;US6017871-A;US6271012-1;US6312936-B1;US6440717-B1;WO 200022103-A1;WO 200024924-A2;WO200037599-A1;WO 200037621-A1;WO 200037622-A1;WO 200037623-A1;WO 200037624-A1;WO 200037625-A1;WO 200037626-A1;WO 200037627-A1;WO 200071683-A1;WO 200071684-A1;WO 200071685-A1;WO 200071686-A1;WO 200071687-A1;WO 200071688-A1;WO 200071689-A1;WO 200071690-A1;WO 200071691-A1;WO 200116285-A2;WO 200168821-A2;WO 200175087-A2;WO 200183559-A2;WO 200210183-A1;WO 200216547-A2;WO 200218588-A1;WO 200222796-A1;WO 200231133-A1;WO 200240997-A2;WO 200277289-A1;WO200288340-A2;WO 2003038082-A2;WO 2003054184-A1;WO 2003054185-A1;<h2 style=";text-align:left;direction:ltr">WO2003055974-A2;WO 2003057713-A2;WO 2003062381-A2;WO 2003093453-A2;WO2004003186-A2;WO 2004016752-A2;WO 2004042049-A1;WO 2004064744-A2;WO2004099401-A1;WO 2004111219-A1;WO 2005024002-A1;WO 2005035747-A1;WO2005078074-A2;WO 2005079826-A1;WO 2005095592-A2;WO 2005115445-A1;WO2005118793-A2;WO 2005123911-A2;WO2005123914-A1;WO 2005124012-A1;WO2006088325-A1;WO 2006136159-A2;WO 2006136160-A2;WO 2007006305-A1;WO2007019858-A2;WO 2007044993-A2;WO 2007080197-A2;WO 2007122175-A1;WO2008010925-A2;WO 2008112258-A2;WO 2008141281-A1;WO 2008153934-A2;WO2008153935-A2;WO 2009005647-A2;WO 2009021867-A2;WO 2009058518-A1;WO2009071550-A1;WO 2009074650-A2;WO 2009149144-A2;WO 2009149145-A2;WO2009149200-A2;WO 2010056640-A2;WO 2010056653-A2;WO 2010056671-A1;WO2010078462-A1;WO 2010123754-A1;WO 2011014278-A1;WO 2011036263-A1;WO2011072099-A2;WO 2011072117-A1;WO 2011091370-A1;WO 2011110625-A1;WO2011130076-A1;WO 2011130222-A2;WO 2011140316-A1;WO 2011140364-A1;WO2012080202-A1;WO 2012151480-A2;WO 2012151534-A1;<h2 style=";text-align:left;direction:ltr">WO 2013086219-A1;WO2013092635-A1;WO 2013110766-A1;WO 2013159032-A1;WO 2014037438-A1;WO2014055778-A2;WO 2014055782-A1;WO 2014081884-A1;WO 2014194034-A2;WO2014207228-A1;WO 2015038792-A1;WO 2015048332-A2;WO 2015048339-A2;WO2015065871-A1;WO 2015089441-A1;WO 2015089447-A1;WO 2015143360-A2;WO2015144932-A1;WO 2015144936-A1;WO 2015185689-A1;WO 2016040464-A1;WO2016046234-A2;WO 2016069552-A1;WO 2016069557-A1;WO 2016069563-A1;WO2016069569-A2;WO 2016097405-A1;WO 2016145428-A1;WO 2016164096-A1;WO2016174234-A2;WO 2016180928-A1;WO 2016183509-A1;WO 2016203064-A2;WO2016205710-A1;WO 2016205755-A1;WO 2017006266-A1;WO 2017050291-A1;WO2017081274-A1;WO 2017089093-A1;WO 2017089366-A1;WO 2017089456-A1;WO2017106676-A1;WO 2017177153-A1;WO 2017189720-A1;WO 2017192692-A1;WO2017210295-A1;WO 2017219011-A1;WO 2018015303-A1;WO 2018015304-A1;WO2018118917-A1;WO 2018118950-A1;WO 2018161899-A1;WO2018188667-A1;WO2018222990-A1;WO 2019048486-A1;WO 2019048495-A1;WO 2019108599-A1;WO2019180111-A1;WO 2019238761-A1;<h2 style=";text-align:left;direction:ltr">WO 2019245704-A1;WO 2019245705-A1;WO2019245838-A1;WO 2019245839-A1;WO 2020002255-A1;WO 2020007863-A1;WO2020023411-A1;WO 2020076697-A1;WO 2020112599-A1;WO 2020114968-A1;WO2020156419-A1;WO 2020169564-A1;WO 2020176443-A1;WO 2020188095-A1;WO2020200198-A1;WO 2020201403-A1;WO 2020207944-A1;WO 2020243738-A1;WO2021013685-A1;WO 2021013686-A1;WO 2021025872-A1;WO 2021030400-A1;WO2021080948-A2;WO 2021119304-A1;WO 2021122120-A2;WO 2021130167-A1;WO2021133701-A1;WO 2021148364-A1;WO 2021209548-A1;WO 2021230359-A1;WO2021231621-A1;WO 2021231623-A1;WO 2021248045-A2;WO 2022043547-A1;WO2022043563-A1;WO 2022043745-A1;WO 2022106400-A1;WO 2022129166-A1;WO2022171120-A1;WO 2022171667-A1;WO 2022175263-A2;WO 2022225696-A2;WO2022226158-A2;WO 2022261003-A1;WO 2023288294-A1;WO 8807581-A;WO 9102792-A;WO9106637-A;WO 9211348-A1;WO 9211357-A1;WO 9221760-A1;WO 9307276-A1;WO 9402618-A1;WO 9418329-A2;WO 9423053-A1;WO 9507991-A2;WO 9510591-A1;WO 9510615-A1;WO9523221-A1;WO 9523614-A1;WO 9530011-A2;WO 9628557-A2;WO 9628566-A2;WO9634935-A2; WO 9634946-A1; WO 9820115-A1; WO 9830682-A1; WO 9855634-A1; WO9920770-A2; WO 9927082-A1; WO 9967370-A1. ;

[0542] In some embodiments, the proteins of the present disclosure exhibit one or more hydrolase activities belonging to EC 3.5, such as amide hydrolase and amidase activities belonging to EC 3.5.1 (e.g., asparaginase activity belonging to EC 3.5.1.1, glutaminase activity belonging to 3.5.1.2, amidase activity belonging to 3.5.1.4, urease activity belonging to 3.5.1.5, biotinidase activity belonging to 3.5.1.12, nicotinamidase activity belonging to 3.5.1.19, nicotinamidase activity belonging to EC 3.5.1.33 N-acetylglucosamine deacetylase activity, belonging to 3.5.1.35 D-glutaminase activity, belonging to 3.5.1.38 glutaminase (asparaginase) activity, belonging to 3.5.1.41 chitin deacetylase activity, belonging to 3.5.1.43 peptidyl-glutaminase activity, belonging to 3.5.1.44 protein glutamine glutaminase activity, belonging to 3.5.1.50 pentanamidase activity, belonging to EC 3.5.1.104 peptidoglycan-N-acetylglucosamine deacetylase activity), belonging to EC 3.5.3 amino acids and deiminases (e.g., belonging to EC 3.5.3.1 arginase activity, belonging to EC 3.5.3.6 arginine deiminase activity, belonging to EC 3.5.3.10 D-arginase activity, belonging to EC 3.5.3.15) and / or a deaminase activity belonging to EC 3.5.4 (e.g., a cytosine deaminase activity belonging to EC 3.5.4.1, an adenine deaminase activity belonging to EC 3.5.4.2, a guanine deaminase activity belonging to EC 3.5.4.3, an adenosine deaminase activity belonging to EC 3.5.4.4), and optionally comprising a polypeptide as described herein in SEQ ID 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, or consisting essentially of, one or more of the amino acid sequences set forth in NOs:89-90.

[0543] In some embodiments, the protein is selected from the group consisting of:

[0544] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 89-90;

[0545] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 89-90;

[0546] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 180-181 or a cDNA sequence thereof;

[0547] d) a polypeptide derived from any one of SEQ ID NOs: 89-90 by substitution, deletion or insertion of one or more amino acids;

[0548] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 89-90 by substitution, deletion or insertion of one or more amino acids;

[0549] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0550] g) A fragment of the polypeptide of any one of a) to f)

[0551] Wherein the polypeptide has asparaginase activity belonging to EC 3.5.1.1. Examples of proteins exhibiting asparaginase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NOs: 89-90 are set forth herein as SEQ ID NOs: 71904-72141.

[0552] In some embodiments, the protein is derived from Aspergillus. For example, in some embodiments, the protein is a native Aspergillus asparaginase, or a fragment / mutant / variant of a native Aspergillus asparaginase.

[0553] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more hydrolase activities belonging to EC 3.5. See, for example, CN 109486689-A; EP 2295582-A2; US7504490-B1; WO 2004032648-A1; WO 2008110513-A1; WO 2008128974-A1; WO 2008128975-A1; WO 2011134916-A1; WO 2012068047-A2; WO 2014027062-A1; WO 2014027063-A1; WO2014147189-A1.

[0554] In some embodiments, the proteins of the disclosure exhibit one or more lytic enzyme activities belonging to Enzyme Commission Classification Number 4 (EC4). For example, in some embodiments, the proteins of the present disclosure exhibit lytic enzyme activity and can be used to a) prevent / treat / inhibit / eliminate / reduce the harmful effects of various pests / infestations / infections caused by them, including but not limited to plant pathogenic pests, such as mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; b) reduce one or more aspects of disease severity in plants affected by one or more plant pathogenic pests; c) pre-treat surfaces / materials susceptible to infestation / infection by pests; d) clean surfaces / materials infested / infected by pests; e) improve the environment in which plants grow; f) increase nutrient availability in plant growth media; g) reduce the amount of exogenous fertilizer required to achieve desired results; h) improve plant growth, development and yield characteristics; i) extend the storage life of harvested plants and plant parts; j) delay / accelerate the maturity of plants or plant parts; k) improve the efficacy of chemical pesticides; and / or l) reduce chemical pesticide-induced resistance / phytotoxicity.

[0555] In some embodiments, the proteins of the present disclosure exhibit one or more carbon-carbon lyase activities belonging to EC 4.1, such as a carboxyl lyase activity belonging to EC 4.1.1 (e.g., aspartate 1-decarboxylase activity belonging to EC 4.1.1.11, aspartate 4-decarboxylase activity belonging to EC 4.1.1.12, valine decarboxylase activity belonging to EC 4.1.1.14, glutamate decarboxylase activity belonging to EC 4.1.1.15, lysine decarboxylase activity belonging to EC 4.1.1.18, arginine decarboxylase activity belonging to EC 4.1.1.19, histidine decarboxylase activity belonging to EC 4.1.1.22, tyrosine decarboxylase activity belonging to EC 4.1.1.25, phenylalanine decarboxylase activity belonging to EC 4.1.1.53, methionine decarboxylase activity belonging to EC 4.1.1.57, 4.1.1.105) and / or a carbon-carbon lyase activity belonging to EC 4.1.99 (e.g., a tryptophanase activity belonging to EC 4.1.99.1, a tyrosine phenol lyase activity belonging to EC 4.1.99.2).

[0556] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more carbon-carbon lyase activities belonging to EC 4.1.

[0557] In some embodiments, the proteins of the present disclosure exhibit one or more carbon-oxygen lyase activities belonging to EC 4.2, such as polysaccharide lyase activities belonging to EC 4.2.2 (e.g., pectate lyase activity belonging to EC 4.2.2.2, pectin lyase activity belonging to EC 4.2.2.10, glucan lyase activity belonging to EC 4.2.2.13, gellan gum lyase activity belonging to EC 4.2.2.25, oligo-alginase lyase activity belonging to EC 4.2.2.26, pectin monosaccharide-lyase activity belonging to EC 4.2.2.27), and optionally comprise the same as described herein as SEQ ID The amino acid sequences shown in NO:91 and 55 are about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to, consist essentially of, or consist of the amino acid sequences.

[0558] In some embodiments, the protein is selected from the group consisting of:

[0559] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:91;

[0560] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:91;

[0561] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 182 or its cDNA sequence;

[0562] d) a polypeptide derived from any one of SEQ ID NO: 91 by substitution, deletion or insertion of one or more amino acids;

[0563] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 91 by substitution, deletion or insertion of one or more amino acids;

[0564] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0565] g) A fragment of the polypeptide of any one of a) to f)

[0566] Wherein the polypeptide has pectate lyase activity belonging to EC 4.2.2.2. Examples of proteins exhibiting pectate lyase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 91 are set forth herein as SEQ ID NOs: 72142-72143.

[0567] In some embodiments, the protein is derived from Bacillus. For example, in some embodiments, the protein is a native Bacillus pectate lyase, or a fragment / mutant / variant of a native Bacillus pectate lyase.

[0568] In some embodiments, the protein is selected from the group consisting of:

[0569] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO:55;

[0570] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NO:55;

[0571] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 146 or its cDNA sequence;

[0572] d) a polypeptide derived from any one of SEQ ID NO: 55 by substitution, deletion or insertion of one or more amino acids;

[0573] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NO: 55 by substitution, deletion or insertion of one or more amino acids;

[0574] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0575] g) A fragment of the polypeptide of any one of a) to f)

[0576] Wherein the polypeptide has pectin lyase activity belonging to EC 4.2.2.10. Examples of proteins exhibiting pectin lyase activity and having an amino acid sequence at least 70% identical to one or more of SEQ ID NO: 55 are set forth herein as SEQ ID NOs: 45409-45436.

[0577] In some embodiments, the protein is derived from Aspergillus, Botrytis, Neosartorya, Penicillium, or Pseudomyllocerus. For example, in some embodiments, the protein is a native Aspergillus, Botrytis, Neosartorya, Penicillium, or Pseudomyllocerus pectate lyase, or a fragment / mutant / variant of a native Aspergillus, Botrytis, Neosartorya, Penicillium, or Pseudomyllocerus pectate lyase.

[0578] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more carbon-oxygen lyase activities belonging to EC 4.2. See, for example, US 2015045535-A1; WO 9927083-A1.

[0579] In some embodiments, the proteins of the present disclosure exhibit one or more carbon-nitrogen lyase activities belonging to EC 4.3, such as an ammonia lyase activity belonging to EC 4.3.1 (e.g., an aspartate ammonia lyase activity belonging to EC 4.3.1.1, a histidine ammonia lyase activity belonging to EC 4.3.1.3, an L-serine ammonia lyase activity belonging to EC 4.3.1.17, a D-serine ammonia lyase activity belonging to EC 4.3.1.18, a threonine ammonia lyase activity belonging to EC 4.3.1.19, a tyrosine ammonia lyase activity belonging to EC 4.3.1.23, a phenylalanine ammonia lyase activity belonging to EC 4.3.1.24, a phenylalanine / tyrosine ammonia lyase activity belonging to EC 4.3.1.25, an L-lysine cyclodeaminase activity belonging to EC 4.3.1.28, an L-tryptophan ammonia lyase activity belonging to EC 4.3.1.31).

[0580] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more carbon-nitrogen lyase activities belonging to EC 4.3.

[0581] In some embodiments, the proteins of the present disclosure exhibit one or more carbon-sulfur lyase activities belonging to EC 4.4, such as a carbon-sulfur lyase activity belonging to EC 4.4.1 (e.g., a cysteine ​​lyase activity belonging to EC 4.4.1.10, a methionine γ-lyase activity belonging to EC 4.4.1.11, an L-cysteine ​​desulfidase activity belonging to EC 4.4.1.28, an L-cysteine ​​β-lyase activity belonging to EC 4.4.1.35).

[0582] Those skilled in the art will understand how to identify, isolate, characterize, produce, recover and formulate proteins having one or more carbon-sulfur lyase activities belonging to EC 4.4.

[0583] In some embodiments, the protein comprises, consists essentially of, or consists of a wild-type polypeptide. For example, in some embodiments, the protein comprises, consists essentially of, or consists of a wild-type polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0584] In some embodiments, the protein comprises, consists essentially of, or consists of a variant polypeptide. For example, in some embodiments, the protein comprises, consists essentially of, or consists of a variant polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0585] In some embodiments, a protein comprises, consists essentially of, or consists of a catalytic domain, a binding moiety, and a linker between the catalytic domain and the binding moiety.

[0586] The present disclosure extends to proteins capable of exhibiting two, three, four, five or more different catalytic activities, including but not limited to proteins that inherently exhibit two or more different catalytic activities and fusion proteins comprising two or more polypeptides exhibiting different catalytic activities.

[0587] In some embodiments, the protein is a hybrid protein.

[0588] In some embodiments, the protein comprises two or more catalytic domains.

[0589] In some embodiments, the protein comprises two or more binding modules.

[0590] In some embodiments, the protein is a fusion protein (eg, a fusion protein comprising a first polypeptide having a first enzymatic activity and a second polypeptide having a second enzymatic activity).

[0591] In some embodiments, the protein is a fusion protein comprising a first polypeptide and a second polypeptide, the second polypeptide being different from the first polypeptide, wherein the first polypeptide is selected from the group consisting of:

[0592] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149;

[0593] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0594] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof;

[0595] d) a polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0596] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0597] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0598] g) a fragment of the polypeptide of any one of a) to f), and optionally

[0599] Wherein the second polypeptide is selected from the group consisting of:

[0600] h) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0601] i) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0602] j) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof;

[0603] k) a polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0604] 1) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0605] m) a polypeptide derived from the polypeptide of any one of h) to l), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and

[0606] n) A fragment of the polypeptide of any one of h) to m).

[0607] In preferred embodiments, the protein of the present disclosure comprises, consists essentially of, or consists of the amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0608] In preferred embodiments, the protein of the present disclosure is encoded by a polynucleotide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 92-182, 72145-72146, 72148, and 72150, or a cDNA thereof.

[0609] In some embodiments, the proteins of the present disclosure comprise, consist essentially of, or consist of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide. For example, the protein can be a fragment of any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide, said fragment comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0610] As described above, in some embodiments, the protein of the present disclosure comprises any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or an N-terminal extension thereof having one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). , 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0611] Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the catalytic activity of the resulting molecule is evaluated to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The active site of an enzyme or other biological interaction can also be determined by physical analysis of the structure, such as by techniques such as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, together with mutations to putative contact site amino acids. See, e.g., de Vos et al., 1992, Science 255:306-312; Smith et al., 1992, J. Mol. Biol. 224:899-904; Wlodaver et al., 1992, FEBS Lett. 309:59-64. The identity of essential amino acids can also be inferred from alignments with related polypeptides, and / or from sequence homology and conserved catalytic mechanisms with related polypeptides or polypeptides / proteins from a common ancestor (typically having similar three-dimensional structures, functions, and significant sequence similarity) within a family of polypeptides or proteins. Additionally or alternatively, protein structure prediction tools can be used for protein structure modeling to identify essential amino acids and / or active sites of a polypeptide. See, e.g., Jumper et al., 2021, “Highly accurate protein structure prediction with AlphaFold,” Nature 596:583-589.

[0612] Single or multiple amino acid substitutions, deletions and / or insertions can be made and tested using known mutagenesis, recombination and / or shuffling methods followed by relevant screening procedures, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241:53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86:2152-2156; WO 95 / 17413; or WO 95 / 22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30:10832-10837; US 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46:145; Ner et al., 1988, DNA 7:127).

[0613] Mutagenesis / shuffling methods can be combined with high-throughput, automated screening methods to detect the activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17:893-896). Mutagenized DNA molecules encoding active polypeptides can be recovered from host cells and rapidly sequenced using standard methods in the art. These methods allow the importance of individual amino acid residues in a polypeptide to be rapidly determined.

[0614] Table 1 provides a non-exhaustive list of proteins that can be used in the compositions and methods of the present disclosure.

[0615] Table 1. Exemplary proteins of the present disclosure

[0616]

[0617]

[0618]

[0619]

[0620]

[0621] The proteins disclosed herein may be derived from microorganisms of any genus.

[0622] In some embodiments, the protein is derived from and / or obtained from a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Dictyoglossum (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0623] In some embodiments, the protein is derived from a Gram-positive bacterium, such as A. akibai (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus ), Bacillus subtilis, Bacillus thuringiensis), Clostridium, Bacillus polymorpha (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neosporium Bacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus), or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sackliffe (e.g., S. halmapala).

[0624] In some embodiments, the protein is derived from a fungus, such as Acremonium, A. fusispora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. shewanella, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. snow-white-gray green, A. oryzae, A. tubingensis ), B. adusta, B. fumosa (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis rubrum subrufa), C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. g raminicola), Coprinus (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryptococcus (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F.graminearum), F.graminum, F.heterosporum, F.longipes, F.negundi, F.oxysporum, F.reticulatum, F.roseum, F.sambucinum, F.sarcochroum, F.solani, F.sporotrichioides, F.sulphureum, F.toru Losum), F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microspora (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), crassa), Thicktoplasma (e.g., O. barbara), Penicillium, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, Penicillium viridifolium), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), eryngii), Pseudomonas (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Cylindrospermum (e.g., S. maydis), Talaromyces (e.g., T. eryngii), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. aurantiacus),thermophila), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavioides (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa), versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium).

[0625] In some embodiments, the protein is derived from a yeast such as Candida, Hansenula, Kluyveromyces (e.g., K. phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica).

[0626] It will be understood that for the aforementioned species, the present disclosure encompasses both perfect and imperfect states, as well as other taxonomic equivalents, such as anamorphs, regardless of the species name by which they are known. Those skilled in the art will readily recognize the identity of appropriate equivalents.

[0627] The above-mentioned probes can be used to identify and obtain proteins from other sources (including microorganisms separated from nature (e.g., soil, compost, water, etc.) or DNA samples directly obtained from natural materials (e.g., soil, compost, water, etc.). The technology for directly isolating microorganisms and DNA from natural living environments is well known in the art. The polynucleotides encoding the protein can then be obtained by similarly screening the genomic DNA or cDNA library of another microorganism or a mixed DNA sample. Once the polynucleotide encoding the protein has been detected with one or more probes, the polynucleotides can be isolated or cloned by utilizing techniques known to those of ordinary skill in the art (see, for example, Davis et al., 2012, Basic Methods in Molecular Biology [Basic Methods of Molecular Biology], Elsevier [Elsevier]).

[0628] The proteins disclosed herein may also be derived from plants of any genus.

[0629] In some embodiments, the protein is derived from a plant selected from the following families: Amaranthaceae (e.g., Swiss chard, spinach, beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, echinacea, goldenrod, guayule, lettuce, marigold, safflower, sunflower, zinnia), Cruciferae (e.g., arugula, broccoli, cabbage, Brussels sprouts, cabbage, cauliflower, canola, kale, radish, Lepidium, horseradish, kale, mustard, radish, rapeseed, kohlrabi, turnip, horseradish, watercress, Arabidopsis), Caricapae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, zucchini, pumpkin (e.g., acorn squash, winter squash, summer squash), watermelon, zucchini), Leguminosae (e.g., alfalfa,

[0013] The present invention relates to plants and animals of the family Cyperaceae, such as beans, carob, clover, guar, lentil, mesquite, pea, peanut, soybean, tamarind, tragacanth, vetch), Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, turf grasses (e.g., bahia grass, bermudagrass, bluegrass, buffalo grass, centipede, fescue, or zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, citrus, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, capsicum, eggplant, petunia, potato, tobacco, tomato), and Vitaceae (e.g., grape).

[0630] The proteins of the present disclosure can be produced and obtained using any one or more suitable methods, including but not limited to shake flask culture and large-scale fermentation (including continuous, batch, fed-batch, solid-state and / or microcarrier-based fermentation) methods.

[0631] The disclosure extends to methods of producing a protein of the disclosure, the methods comprising (a) cultivating a cell under conditions conducive for production of the protein, the cell producing the protein in its wild-type form; and optionally (b) recovering the protein.

[0632] The disclosure also extends to methods of producing a protein of the disclosure, comprising (a) cultivating a recombinant host cell of the disclosure under conditions conducive for production of the protein; and optionally (b) recovering the protein.

[0633] In some embodiments, the protein is produced by and obtained from a Gram-negative bacterium such as Campylobacter, Chryseobacterium (e.g., Chryseobacterium viscerae), Dictyoglobulus (e.g., Dictyoglobulus thermophilus), Escherichia (e.g., Escherichia coli), Flavobacterium, Fusobacterium, Helicobacter, Gluebacter, Lysobacter (e.g., Lysobacter colloidus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0634] In some embodiments, the protein is produced by and obtained from Gram-positive bacteria such as: Halobacterium spp. (e.g., Halobacterium akiba, Halobacter clausii), Bacillus spp. (e.g., Bacillus agaricus, Bacillus alkaliphilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus delamifie, Bacillus firmus, Bacillus radiata, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus brevis, Bacillus stearothermophilus, Bacillus subtilis, Bacillus thuringiensis), Clostridium spp., Bacillus variabilis (e.g., Bacillus variabilis Bacillus), Enterococcus, Geobacillus (e.g., Geobacillus stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., Lederbergia slow), Neobacillus (e.g., Neobacillus novalis), Nocardiopsis, Oceanobacillus (e.g., Oceanobacillus barbara), Staphylococcus, Streptococcus (e.g., Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi zooepidemicus), or Streptomyces (e.g., Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, Streptomyces lividans), Sackliffia (e.g., Sackliffia hamachia).

[0635] In some embodiments, the protein is produced by and obtained from fungal cells such as: Acremonium, Endocerium (e.g., Endocerium fuscipenser), Aspergillus (e.g., A. aculeatus, A. awamori, A. shewani, A. foetidum, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. snow-white-gray green, A. oryzae, A. tubingensis), A. pullulans, A. fumonis (e.g., A. fumonis, A. fumochrome), A. cereus (e.g., A. cymosum, A. fumochrome), A. cymosporum (e.g., A. cymosporum ..., A. cymosporum, A. cymosporum, A. cymosporum, A. cymosporum, A. cymosporum, ), Coprinus (e.g., Coprinus griseus), Coprinus (e.g., Coprinus cinerea), Coprinus (e.g., Coprinus cinerea), Coriolus (e.g., Coriolus furciferus), Cryptococcus (e.g., Cryptococcus parasiticus), Cryptococcus, Evansstolkia (e.g., E. leycettana), Ustilago, Fusarium (e.g., Fusarium rod-shaped, Fusarium grain, Fusarium graminearum, Fusarium graminearum, Fusarium heterosporum, Fusarium longipes, Fusarium albizia, Fusarium oxysporum, Fusarium multibranched, Fusarium pink, Fusarium graminearum, Fusarium graminearum, Fusarium heterosporum, Fusarium longipes, Fusarium albizia, Fusarium oxysporum, Fusarium multibranched, Fusarium pink, Fusarium serrata, Fusarium graminearum, Fusarium graminearum, Fusarium graminearum, Fusarium heterosporum, Fusarium longipes, Fusarium albizia, Fusarium oxysporum, Fusarium multibranched, Fusarium pink, Fusarium serrata ... Fusarium spp., ... abalone), Pseudomonas (e.g., Pseudomonas glaucosa), Schizophyllum, Sodiomyces (e.g., S.alcalophilus), Cylindrospermum (e.g., Cylindrospermum zeae), Talaromyces (e.g., Talaromyces spp., Talaromyces emersonii, Talaromyces rufipogon), Thermoascus (e.g., Thermoascus aureus), Themochaetoides (e.g., T.thermophila), Thermomyces (e.g., Thermomyces lanuginosus), Thermothielavioides (e.g., T.terrestris), Thermothelomyces (e.g., T.thermophilus), Thielavia (e.g., Thielavia terrestris), Tolypocladium, Trametes (e.g., Trametes tricholoma, Trametes villosa, Trametes versicolor), Trichoderma (e.g., Trichoderma amurensis, Trichoderma harzianum, Trichoderma koningii, Trichoderma longipes, Trichoderma reesei, Trichoderma viride), Trichopanax (e.g., Trichopanax vesicularis), or Phialopsora (e.g., Phialopsora annularis).

[0636] In some embodiments, the protein is produced by and obtained from a yeast cell such as Candida, Hansenula, Klebsiella (e.g., Klebsiella phaffii), Kluyveromyces (e.g., K. lactis), Pichia (e.g., Pichia pastoris), Saccharomyces (e.g., Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces novonis, Saccharomyces oviformis), Schizosaccharomyces, or Yarrowia (e.g., Y. lipolytica).

[0637] In some embodiments, the protein is produced by and obtained from a plant cell selected from the following families: Amaranthaceae (e.g., Swiss chard, spinach, beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, echinacea, goldenrod, guayule, lettuce, marigold, safflower, sunflower, zinnia), Cruciferae (e.g., arugula, broccoli, cabbage, Brussels sprouts, cabbage, cauliflower, canola, kale, radish, Lepidium, horseradish, kale, mustard, radish, rapeseed, kohlrabi, turnip, horseradish, watercress, Arabidopsis), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, zucchini, pumpkin (e.g., acorn squash, winter squash, summer squash), watermelon, zucchini), Leguminosae and oats. The family includes, for example, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops. The family includes, for example, alfalfa, beans, carob, clover, guar, lentil, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch, Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, crabgrass, turf grasses (e.g., bahia grass, bermudagrass, bluegrass, buffalo grass, centipede grass, fescue, or zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, citrus, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, capsicum, eggplant, petunia, potato, tobacco, tomato), and Vitaceae (e.g., grapes).

[0638] Cells can be cultured in a nutrient medium suitable for producing proteins using methods known in the art. For example, cells can be cultured in a suitable medium and under conditions that allow expression and / or separation of proteins by shaking flask culture or in a laboratory or industrial fermentor on a small or large scale (including continuous, batch, fed-batch or solid-state and / or based on microcarrier fermentation). Suitable culture medium can be obtained from commercial suppliers, or can be prepared according to disclosed composition (for example, in the catalog of the American Type Culture Collection). If protein is secreted into the nutrient medium, protein can be directly recovered from the medium. If protein is not secreted, it can be recovered from cell lysates.

[0639] The protein can be detected using methods known in the art that are specific for the protein, including but not limited to assays using specific antibodies, enzyme product formation, disappearance of enzyme substrate, or determining the relative or specific activity of the protein.

[0640] The protein can be recovered from the culture medium using methods known in the art, including but not limited to collection, centrifugation, filtration, extraction, spray drying, evaporation or precipitation. In one aspect, the entire fermentation broth containing the protein is recovered. In another aspect, the cell-free fermentation broth containing the protein is recovered.

[0641] In some embodiments, the protein is secreted extracellularly.

[0642] In some embodiments, the protein is isolated.

[0643] In some embodiments, the protein is purified.

[0644] Proteins can be purified by a variety of procedures known in the art to obtain substantially pure proteins and / or protein fragments (see, e.g., Wingfield, 2015, Current Protocols in Protein Science; 80(1):6.1.1-6.1.35; Labrou, 2014, Protein Downstream Processing, 1129:3-10).

[0645] In an alternative aspect, the protein is not recovered.

[0646] The present disclosure also provides cells that naturally express the native proteins of the present disclosure and cells that have been engineered to express the heterologous proteins of the present disclosure (e.g., recombinant host cells comprising a polynucleotide of the present disclosure, which polynucleotide is operably linked to one or more control sequences that direct the production of the proteins of the present disclosure), as well as tools and methods for producing such recombinant host cells, including polynucleotides encoding the proteins of the present disclosure and nucleic acid constructs comprising such polynucleotides.

[0647] In some embodiments, the cell is a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., Chryseobacterium viscerae), Dictyoglobulus (e.g., Dictyoglobulus thermophilus), Escherichia (e.g., Escherichia coli), Flavobacterium, Fusobacterium, Helicobacter, Gluebacter, Lysobacter (e.g., Lysobacter colloidus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0648] In some embodiments, the cell is a gram-positive bacterium, such as Halobacter spp. (e.g., Halobacter akibae, Halobacter clausii), Bacillus spp. (e.g., Bacillus agaricus, Bacillus alkaliphilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus delamifie, Bacillus firmus, Bacillus radiata, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus brevis, Bacillus stearothermophilus, Bacillus subtilis, Bacillus thuringiensis), Clostridium, Bacillus variabilis (e.g., Bacillus variabilis), Enterococcus, Geobacillus (e.g., Geobacillus stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., Lederbergia slow), Neobacillus (e.g., Neobacillus novalis), Nocardiopsis, Oceanobacillus (e.g., Oceanobacillus barbara), Staphylococcus, Streptococcus (e.g., Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi zooepidemicus), or Streptomyces (e.g., Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, Streptomyces lividans), Sackliffia (e.g., Sackliffia hamachia).

[0649] In some embodiments, the cell is a fungal cell, such as Acremonium, Endocerium (e.g., Endocerium fuscipenser), Aspergillus (e.g., A. aculeatus, A. awamori, A. shewani, A. foetidum, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. snow-white-gray green, A. oryzae, A. tubingensis), A. pullulans, A. fumonis (e.g., A. fumonis, A. fumochrome), A. cereus (e.g., A. cymosum, A. cymosum stylosum, A. fumochrome), A. cymosporum (e.g., A. cymosporum, A. cymosporum stylosum, A. cymosporum stylosum, A. cymosporum pannohita, A. cymosporum annulare, A. rubrum, A. worm), Chaetomium (e.g., Chaetomium irregulare, Chaetomium globosum), Chrysosporium (e.g., Chrysosporium stenomarginatum, Chrysosporium keratinophilum, Chrysosporium lukenovens , Chrysosporium, Chrysosporium dungarum, Chrysosporium quinslandensis, Chrysosporium tropicalis, Chrysosporium tassels), Colletotrichum spp. (e.g., Colletotrichum graminicum), Coprinus spp. (e.g., Coprinus cinereus), Coprinus spp. (e.g., Coprinus cinereus), Coriolus spp. (e.g., Coriolus furfuricus), Cryptococcus spp. (e.g., Cryptococcus parasiticus), Cryptococcus spp., Evansstolkia (e.g., E. leycettana), Ustilago, Fusarium spp. (e.g., Fusarium rod-shaped, Fusarium grain, Fusarium graminicum, Fusarium graminicum, Fusarium heterosporum, Fusarium longipes, Fusarium albizia, Fusarium oxysporum, Fusarium multibranched, Fusarium pink, Fusarium elderberry, Fusarium complexion Fusarium, Fusarium solani, Fusarium pseudocladosporium, Fusarium sulphureus, Fusarium circumflexus, Fusarium pseudohypodermis, Fusarium embellishment), Humicola (e.g., Humicola insolens, Humicola lanuginosa), Macrocystis, Microcystis (e.g., Microcystis nivalis), Mucor (e.g., Mucor miehei), Myceliophthora (e.g., Myceliophthora thermophila), Neotrichia, Neurospora (e.g., Neurospora crassa), Thicktopterus (e.g., Thicktopterus barbarum), Penicillium, Penicillium (e.g., Penicillium emersonii, Penicillium purpurogenum, Penicillium thommii, Penicillium viridiflorum), Phanerochaete (e.g., Phanerochaete chrysosporium), Radialis (e.g., Radialis), Pyrimethamine, Pleurotus (e.g., Pleurotus eryngii) , Pseudomonas (e.g., Pseudomonas glaucosa), Schizophyllum, Sodiomyces (e.g., S.alcalophilus), Cylindrospermum (e.g., Cylindrospermum zeae), Talaromyces (e.g., Talaromyces spp., Talaromyces emersonii, Talaromyces rufipogon), Thermoascus (e.g., Thermoascus aureus), Themochaetoides (e.g., T.thermophila), Thermomyces (e.g., Thermomyces lanuginosus), Thermothielavioides (e.g., T.terrestris), Thermothelomyces (e.g., T.thermophilus), Thielavia (e.g., Thielavia terrestris), Tolypocladium, Trametes (e.g., Trametes tricholoma, Trametes villosa, Trametes versicolor), Trichoderma (e.g., Trichoderma amurensis, Trichoderma harzianum, Trichoderma koningii, Trichoderma longipes, Trichoderma reesei, Trichoderma viride), Trichopanax (e.g., Trichopanax vesicularis), or Phialopsora (e.g., Phialopsora annularis).

[0650] In some embodiments, the cell is a yeast cell, such as a Candida, Hansenula, Saccharomyces cerevisiae (e.g., Saccharomyces cerevisiae), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., Pichia pastoris), Saccharomyces (e.g., Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces nobensis, Saccharomyces oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica).

[0651] In some embodiments, the cell is a plant cell, optionally selected from the family Amaranthaceae (e.g., chard, spinach, beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, echinacea, goldenrod, guayule, lettuce, marigold, safflower, sunflower, zinnia), Cruciferae (e.g., arugula, broccoli, cabbage, Brussels sprouts, cabbage, cauliflower, canola, kale, radish, Lepidium, horseradish, kale, mustard, radish, rapeseed, kohlrabi, turnip, wasabi, watercress, Arabidopsis), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, zucchini, pumpkin (e.g., acorn squash, winter squash, summer squash), watermelon, zucchini), Leguminosae and oats. The family includes, for example, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops. The family includes, for example, alfalfa, beans, carob, clover, guar, lentil, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch, Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, crabgrass, turf grasses (e.g., bahia grass, bermudagrass, bluegrass, buffalo grass, centipede grass, fescue, or zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, citrus, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, capsicum, eggplant, petunia, potato, tobacco, tomato), and Vitaceae (e.g., grapes).

[0652] In some embodiments, the cells express:

[0653] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149;

[0654] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0655] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof;

[0656] d) a polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0657] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0658] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and / or

[0659] g) A fragment of the polypeptide of any one of a) to f).

[0660] In preferred embodiments, the cells express a polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0661] In some embodiments, the cell expresses a polypeptide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide. For example, the microorganism can express any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide, comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0662] In some embodiments, the cell expresses an amino acid sequence comprising any of SEQ ID NOS: 1-91, 45906, 72144, 72147, and 72149 or an N-terminal extension thereof having one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). 14,15,16,17,18,19,20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide, consisting essentially of, or consisting of, any of them or their mature polypeptides. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0663] In some embodiments, the cells comprise a homologous or heterologous nucleic acid sequence that is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the nucleic acid sequences set forth herein as SEQ ID NOs:92-182, 72145-72146, 72148, and 72150, or a cDNA sequence thereof.

[0664] In preferred embodiments, the cell comprises a polynucleotide encoding a polypeptide comprising, consisting essentially of, or consisting of an amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0665] In some embodiments, the cells comprise a polynucleotide comprising, consisting essentially of, or consisting of a nucleic acid sequence encoding a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0666] In some embodiments, the cells comprise a polynucleotide comprising, consisting essentially of, or consisting of a nucleic acid sequence encoding a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0667] In preferred embodiments, the cell comprises a polynucleotide comprising, consisting essentially of, or consisting of a nucleic acid sequence of any one of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof.

[0668] In some embodiments, the cell comprises a polynucleotide encoding a polypeptide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof. For example, the microorganism comprises a polynucleotide encoding any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof, said fragment comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0669] In some embodiments, the cell comprises a polynucleotide encoding any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 or an N-terminal extension thereof having one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). 14,15,16,17,18,19,20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide, consisting essentially of, or consisting of, any of them or their mature polypeptides. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0670] Thus, the present disclosure encompasses plants and plant parts expressing one or more proteins of the present disclosure, including plants and plant parts that have been engineered to (over) express one or more proteins of the present disclosure; and methods of producing proteins of the present disclosure, comprising cultivating (transgenic) plants or plant parts comprising polynucleotides encoding proteins under conditions conducive to the production of proteins, and optionally recovering the proteins. In alternative embodiments, such plants can be used as is to enhance one or more food / feed characteristics (e.g., to improve nutritional value, palatability and / or rheological properties, to destroy anti-nutritional factors, etc.).

[0671] In some embodiments, the plant expresses:

[0672] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149;

[0673] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0674] c) a polypeptide encoded by a polynucleotide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof;

[0675] d) a polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0676] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0677] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and / or

[0678] g) A fragment of the polypeptide of any one of a) to f).

[0679] In preferred embodiments, the plant expresses a polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0680] In some embodiments, the plant expresses a polypeptide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof. For example, the microorganism can express any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof, comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0681] In some embodiments, the plant expresses a polypeptide comprising any of SEQ ID NOS: 1-91, 45906, 72144, 72147, and 72149 or a polypeptide having an N-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). 14,15,16,17,18,19,20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide, consisting essentially of, or consisting of, any of them or their mature polypeptides. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0682] In some embodiments, the plant comprises a homologous or heterologous nucleic acid sequence that is at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to one or more of the nucleic acid sequences set forth herein as SEQ ID NOs:92-182, 72145-72146, 72148, and 72150, or a cDNA sequence thereof.

[0683] In a preferred embodiment, the plant comprises a polynucleotide encoding a polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0684] In some embodiments, the plant comprises, consists essentially of, or consists of a nucleic acid sequence encoding a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0685] In some embodiments, the plant comprises, consists essentially of, or consists of a nucleic acid sequence encoding a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0686] In a preferred embodiment, the plant comprises a polynucleotide comprising, consisting essentially of, or consisting of a nucleic acid sequence of any one of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof.

[0687] In some embodiments, the plant comprises a polynucleotide encoding a polypeptide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof. For example, the microorganism comprises a polynucleotide encoding any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of a mature peptide thereof, said fragment comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0688] In some embodiments, the plant comprises a polynucleotide encoding any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 or an N-terminal extension thereof having one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). 14,15,16,17,18,19,20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide, consisting essentially of, or consisting of, any of them or their mature polypeptides. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0689] Also included within the scope of the present disclosure are the progeny of such plants, plant parts, and plant cells.

[0690] As noted above, the disclosure extends to tools and methods for producing such recombinant host cells that express one or more proteins of the disclosure, including polynucleotides encoding the proteins of the disclosure and nucleic acid constructs comprising such polynucleotides.

[0691] The present disclosure provides polynucleotides encoding the proteins of the present disclosure, including but not limited to nucleic acid constructs and recombinant expression vectors encoding one or more enzymes of the present disclosure; and methods of producing such polynucleotides.

[0692] The polynucleotide can be genomic DNA, cDNA, synthetic DNA, synthetic RNA, mRNA, or a combination thereof.

[0693] The polynucleotides may be cloned from any suitable genus, species or strain.

[0694] In some embodiments, the protein is cloned from a Gram-negative bacterium such as Campylobacter, Chryseobacterium (e.g., Chryseobacterium viscerae), Dictyoglobulus (e.g., Dictyoglobulus thermophilus), Escherichia (e.g., Escherichia coli), Flavobacterium, Fusobacterium, Helicobacter, Gluebacter, Lysobacter (e.g., Lysobacter colloidus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0695] In some embodiments, the polynucleotides are cloned from Gram-positive bacteria such as Halobacter spp. (e.g., Halobacter akiba, Halobacter clausii), Bacillus spp. (e.g., Bacillus agaricus, Bacillus alkaliphilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus delamifie, Bacillus firmus, Bacillus radiata, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus brevis, Bacillus stearothermophilus, Bacillus subtilis, Bacillus thuringiensis), Clostridium spp., Bacillus variabilis (e.g., Bacillus variabilis, Bacillus thuringiensis), Bacillus), Enterococcus, Geobacillus (e.g., Geobacillus stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., Lederbergia slow), Neobacillus (e.g., Neobacillus novalis), Nocardiopsis, Oceanobacillus (e.g., Oceanobacillus barbara), Staphylococcus, Streptococcus (e.g., Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi zooepidemicus subsp.) or Streptomyces (e.g., Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, Streptomyces lividans), Sackliffia (e.g., Sackliffia hamachia).

[0696] In some embodiments, the polynucleotides are cloned from fungi such as Acremonium, Endocerium (e.g., Endocerium fuscipenser), Aspergillus (e.g., A. aculeatus, A. awamori, A. shewani, A. foetidum, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. snow-white-gray green, A. oryzae, A. tubingensis), A. pullulans, A. fumonis (e.g., A. fumonis, A. fumochrome), A. cereus (e.g., A. cymosum, A. cymosum stylosum, A. fumochrome), A. cymosporum (e.g., A. cymosporum, A. cymosporum stylosum, A. cymosporum stylosum, A. cymosporum pannohita, A. cymosporum annulare, A. rubrum, A. worm), Chaetomium (e.g., Chaetomium irregulare, Chaetomium globosum), Chrysosporium (e.g., Chrysosporium stenosporum, Chrysosporium keratinum, A. lucinosporum Chrysosporium venus, Chrysosporium dungarum, Chrysosporium quenslandensis, Chrysosporium tropicalis, Chrysosporium tassels), Colletotrichum spp. (e.g., Colletotrichum graminicum), Coprinus spp. (e.g., Coprinus cinereus), Coprinus spp. (e.g., Coprinus cinereus), Coriolus spp. (e.g., Coriolus furfuricus), Cryptococcus spp. (e.g., Cryptococcus parasiticus), Cryptococcus spp., Evansstolkia (e.g., E. leycettana), Ustilago, Fusarium spp. (e.g., Fusarium rod-shaped, Fusarium grain, Fusarium kedii, Fusarium yellow, Fusarium graminearum, Fusarium graminearum, Fusarium heterosporum, Fusarium longipes, Fusarium albizia, Fusarium oxysporum, Fusarium multibranched, Fusarium pink, Fusarium elder , Fusarium spp., Fusarium solani, Fusarium spp. ... Mushroom), Pseudomonas (e.g., Pseudomonas glaucosa), Schizophyllum, Sodiomyces (e.g., S.alcalophilus), Cylindrospermum (e.g., Cylindrospermum zeae), Talaromyces (e.g., Talaromyces spp., Talaromyces emersonii, Talaromyces rufipogon), Thermoascus (e.g., Thermoascus aureus), Themochaetoides (e.g., T.thermophila), Thermomyces (e.g., Thermomyces lanuginosus), Thermothielavioides (e.g., T.terrestris), Thermothelomyces (e.g., T.thermophilus), Thielavia (e.g., Thielavia terrestris), Tolypocladium, Trametes (e.g., Trametes tricholoma, Trametes villosa, Trametes versicolor), Trichoderma (e.g., Trichoderma amurensis, Trichoderma harzianum, Trichoderma koningii, Trichoderma longipes, Trichoderma reesei, Trichoderma viride), Trichopanax (e.g., Trichopanax vesicularis), or Phialopsora (e.g., Phialopsora annularis).

[0697] In some embodiments, the polynucleotide is cloned from a yeast such as Candida, Hansenula, Komagata (e.g., Komagata phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., Pichia pastoris), Saccharomyces (e.g., Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces novonis, Saccharomyces oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica).

[0698] In some embodiments, the polynucleotide is cloned from a plant cell selected from the following families: Amaranthaceae (e.g., chard, spinach, beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, echinacea, goldenrod, guayule, lettuce, marigold, safflower, sunflower, zinnia), Cruciferae (e.g., arugula, broccoli, cabbage, Brussels sprouts, cabbage, cauliflower, canola, kale, radish, Lepidium, horseradish, kale, mustard, radish, rapeseed, kohlrabi, turnip, horseradish, watercress, Arabidopsis), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, zucchini, pumpkin (e.g., acorn squash, winter squash, summer squash), watermelon, zucchini), Leguminosae (e.g., For example, alfalfa, beans, carob, clover, guar, lentil, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, crabgrass, turf grasses (e.g., bahia grass, bermudagrass, bluegrass, buffalo grass, centipede grass, fescue, or zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, citrus, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, capsicum, eggplant, petunia, potato, tobacco, tomato), and Vitaceae (e.g., grape).

[0699] In some embodiments, the polynucleotide encodes:

[0700] a) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149;

[0701] b) a polypeptide having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149;

[0702] c) a polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0703] e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids;

[0704] f) a polypeptide derived from the polypeptide of any one of a) to e), wherein the N-terminus and / or the C-terminus has been extended by the addition of one or more amino acids; and / or

[0705] g) A fragment of the polypeptide of any one of a) to f).

[0706] In a preferred embodiment, the polynucleotide encodes a polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature polypeptide thereof.

[0707] In some embodiments, the polynucleotide comprises, consists essentially of, or consists of a nucleic acid sequence having about / at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148, and 72150, or a cDNA sequence thereof;

[0708] In preferred embodiments, the polynucleotide comprises, consists essentially of, or consists of the nucleic acid sequence of any one of SEQ ID NOs: 92-182, 72145-72146, 72148, and 72150, or a cDNA sequence thereof.

[0709] In some embodiments, the polynucleotide encodes a polypeptide comprising, consisting essentially of, or consisting of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide. For example, the polynucleotide can encode any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a fragment of its mature peptide, said fragment comprising at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the amino acids found in the original protein.

[0710] In some embodiments, the polynucleotides of the present disclosure encode any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or an N-terminal extension thereof having one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids). 14,15,16,17,18,19,20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and / or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions) of the mature polypeptide, consisting essentially of, or consisting of, any of them or their mature polypeptides. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino-terminal or carboxyl-terminal extensions, such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering the net charge or another function, such as a polyhistidine stretch, an antigenic epitope, or a binding module.

[0711] The polynucleotides of the present disclosure can be mutated by introducing nucleotide substitutions that do not result in changes in the amino acid sequence of the protein but correspond to the codon usage of the host organism intended to produce the enzyme or by introducing nucleotide substitutions that can produce a different amino acid sequence. For a general description of nucleotide substitutions, see, for example, Ford et al., 1991, Protein Expression and Purification 2:95-107.

[0712] In one aspect, the polynucleotide is isolated.

[0713] In another aspect, the polynucleotide is purified.

[0714] The disclosure also provides nucleic acid constructs comprising a polynucleotide of the disclosure, wherein the polynucleotide is operably linked to one or more control sequences that direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences.

[0715] Polynucleotides can be manipulated in a variety of ways to provide expression of proteins. Depending on the expression vector, manipulation of the polynucleotide prior to its insertion into the vector may be desirable or necessary. Techniques for modifying polynucleotides using recombinant DNA methods are well known in the art.

[0716] The control sequence can be a promoter, i.e., a polynucleotide that is recognized by the host cell for expressing a polynucleotide encoding a protein of the present disclosure. The promoter contains a transcriptional control sequence that mediates the expression of the protein. The promoter can be any polynucleotide that exhibits transcriptional activity in the host cell, including mutant, truncated, and hybrid promoters, and can be obtained from genes encoding extracellular or intracellular proteins that are homologous or heterologous to the host cell.

[0717] Examples of suitable promoters for directing transcription of the polynucleotides of the present disclosure in bacterial host cells are described in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Lab., New York, Davis et al., 2012, supra, and Song et al., 2016, PLOS One 11(7):e0158447.

[0718] Examples of suitable promoters for directing transcription of the polynucleotides of the present disclosure in filamentous fungal host cells are promoters obtained from Aspergillus, Fusarium, Rhizomucor, and Trichoderma cells, as described in Mukherjee et al., 2013, “Trichoderma: Biology and Applications” and in Schmoll et al., 2014. 2016. Promoters described in “Gene Expression Systems in Fungi: Advancements and Applications.” Fungal Biology.

[0719] For expression in yeast hosts, examples of useful promoters are provided by Smolke et al., 2018, “Synthetic Biology: Parts, Devices and Applications” (Chapter 6: Constitutive and Regulated Promoters in Yeast: How to Design and Make Use of Promoters in S. cerevisiae) and Schmoll et al., 2018, “Synthetic Biology: Parts, Devices and Applications” (Chapter 6: Constitutive and Regulated Promoters in Yeast: How to Design and Make Use of Promoters in S. cerevisiae). 2016. “Gene Expression Systems in Fungi: Advancements and Applications.” Fungal Biology. Description.

[0720] The control sequence may also be a transcription terminator that is recognized by the host cell to terminate transcription. The terminator is operably linked to the 3' end of the polynucleotide encoding the protein. Any terminator that is functional in the host cell may be used in the present disclosure.

[0721] Preferred terminators for bacterial host cells can be obtained from the genes for Bacillus clausii alkaline protease (aprH), Bacillus licheniformis alpha-amylase (amyL), and Escherichia coli ribosomal RNA (rrnB).

[0722] Preferred terminators for filamentous fungal host cells can be obtained from Aspergillus or Trichoderma species, such as from the genes for Aspergillus niger glucoamylase, Trichoderma reesei β-glucosidase, Trichoderma reesei cellobiohydrolase I, and Trichoderma reesei endoglucanase I as described in Mukherjee et al., 2013, “Trichoderma: Biology and Applications” and in Schmoll et al. 2016. “Gene Expression Systems in Fungi: Advancements and Applications.” Terminators described in Fungal Biology.

[0723] Preferred terminators for yeast host cells can be obtained from the genes for Saccharomyces cerevisiae enolase, Saccharomyces cerevisiae cytochrome C (CYC1), and Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Other useful terminators for yeast host cells are described by Romanos et al., 1992, Yeast 8:423-488.

[0724] The control sequence may also be an mRNA stabilizer region downstream of the promoter and upstream of the coding sequence of a gene, which increases the expression of the gene.

[0725] Examples of suitable mRNA stabilizer regions are obtained from the Bacillus thuringiensis cryIIIA gene (WO 94 / 25612) and the Bacillus subtilis SP82 gene (Hue et al., 1995, J. Bacteriol. 177:3465-3471).

[0726] Examples of mRNA stabilizer regions of fungal cells are described in Geisberg et al., 2014, Cell 156(4):812-824 and Morozov et al., 2006, Eukaryotic Cell 5(11):1838-1846.

[0727] The control sequence may also be a leader sequence, i.e., an untranslated region of an mRNA that is important for translation by the host cell. The leader sequence is operably linked to the 5' end of the polynucleotide encoding the protein. Any leader sequence that is functional in the host cell may be used.

[0728] Suitable leader sequences for bacterial host cells are provided by Hambraeus et al., 2000, Microbiology 146(12):3051-3059 and Kaberdin and 2006, FEMS Microbiol. Rev. [FEMS Microbiology Review] 30(6): 967-979 description.

[0729] Preferred leaders for filamentous fungal host cells can be obtained from the genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase.

[0730] Suitable leaders for yeast host cells can be obtained from the genes for Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase, Saccharomyces cerevisiae alpha-factor, and Saccharomyces cerevisiae alcohol dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH2 / GAP).

[0731] The control sequence may also be a polyadenylation sequence, a sequence operably linked to the 3' terminus of the polynucleotide which, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to transcribed mRNA. Any polyadenylation sequence functional in the host cell may be used.

[0732] Preferred polyadenylation sequences for filamentous fungal host cells are obtained from the genes for Aspergillus nidulans anthranilate synthase, Aspergillus niger glucoamylase, Aspergillus niger alpha-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-like protease.

[0733] Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, 1995, Mol. Cellular Biol. 15: 5983-5990.

[0734] The control sequence can also be a signal peptide coding region that encodes a signal peptide connected to the N-terminus of a protein and directs the protein to enter the secretory pathway of a cell. The 5' end of the coding sequence of a polynucleotide may inherently contain a signal peptide coding sequence, which is naturally connected to the segment of the coding sequence of the encoded protein in the translation reading frame. Alternatively, the 5' end of the coding sequence may contain a signal peptide coding sequence that is heterologous to the coding sequence. In the case where the coding sequence does not naturally contain a signal peptide coding sequence, a heterologous signal peptide coding sequence may be required. Alternatively, a heterologous signal peptide coding sequence may simply replace a natural signal peptide coding sequence to enhance the secretion of a protein. Any signal peptide coding sequence that directs the expressed protein to enter the secretory pathway of a host cell may be used.

[0735] Effective signal peptide coding sequences for bacterial host cells are those obtained from the following genes: Bacillus NCIB 11837 maltogenic amylase, Bacillus licheniformis subtilisin, Bacillus licheniformis β-lactamase, Bacillus stearothermophilus α-amylase, Bacillus stearothermophilus neutral protease (nprT, nprS, nprM) and Bacillus subtilis prsA. Other signal peptides are described by Freudl, 2018, Microbial Cell Factories [Microbial Cell Factory] 17:52.

[0736] An effective signal peptide coding sequence for a filamentous fungal host cell is the signal peptide coding sequence obtained from the genes for Aspergillus niger neutral amylase, Aspergillus niger glucoamylase, Aspergillus oryzae TAKA amylase, Humicola insolens cellulase, Humicola insolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucor miehei aspartic proteinase, such as the signal peptide described by Xu et al., 2018, Biotechnology Letters 40:949-955.

[0737] Useful signal peptides for yeast host cells are obtained from the genes for Saccharomyces cerevisiae α-factor and Saccharomyces cerevisiae invertase. Other useful signal peptide coding sequences are described by Romanos et al., 1992, supra.

[0738] The control sequence can also be a propeptide coding sequence encoding a propeptide located at the N-terminal end of a protein. The resulting protein is referred to as a proenzyme or proprotein (or in some cases as a zymogen). Proprotein is usually inactive and can be converted into an active protein by catalytic or autocatalytic cleavage of the propeptide from the proprotein. The propeptide coding sequence can be obtained from the following genes: Bacillus subtilis alkaline protease (aprE), Bacillus subtilis neutral protease (nprT), Myceliophthora thermophila laccase (WO 95 / 33836), Rhizomucor miehei aspartic protease and Saccharomyces cerevisiae α-factor.

[0739] In the case where both the signal peptide and the propeptide sequence are present, the propeptide sequence is located next to the N-terminus of the protein, and the signal peptide sequence is located next to the N-terminus of the propeptide sequence. Additionally or alternatively, when both the signal peptide and the propeptide sequence are present, the protein may comprise only a portion of the signal peptide sequence and / or only a portion of the propeptide sequence. Alternatively, the final or separated protein may comprise a mixture of a mature protein and a partial or full-length protein comprising a propeptide sequence and / or a signal peptide sequence.

[0740] It may also be desirable to add regulatory sequences that regulate the expression of proteins associated with host cell growth. Examples of regulatory sequences are regulatory sequences that cause gene expression to open or close in response to chemical or physical stimuli (including the presence of regulatory compounds). Regulatory sequences in prokaryotic systems include lac, tac, and trp operator systems. In yeast, the ADH2 system or the GAL1 system can be used. In filamentous fungi, Aspergillus niger glucoamylase promoter, Aspergillus oryzae TAKA α-amylase promoter and Aspergillus oryzae glucoamylase promoter, Trichoderma reesei cellobiohydrolase I promoter and Trichoderma reesei cellobiohydrolase II promoter can be used. Other examples of regulatory sequences are regulatory sequences that allow gene amplification. In fungal systems, these regulatory sequences include dihydrofolate reductase genes amplified in the presence of methotrexate and metallothionein genes amplified with heavy metals.

[0741] The control sequence can also be a transcription factor, i.e., a polynucleotide encoding a polynucleotide-specific DNA binding protein, which controls the rate at which genetic information is transcribed from DNA to mRNA by binding to a specific polynucleotide sequence. Transcription factors can act alone and / or together with one or more other proteins or transcription factors in a complex by promoting or blocking the recruitment of RNA polymerase. Transcription factors are characterized by comprising at least one DNA binding domain, which is generally attached to a specific DNA sequence adjacent to a genetic element regulated by a transcription factor. Transcription factors can directly (i.e., by binding to its promoter to activate the transcription of a gene encoding a target protein) or indirectly (i.e., such as by binding to the promoter of other transcription factors (which regulate the transcription of a gene encoding a target protein) to activate the transcription of other transcription factors) to regulate the expression of the target protein. Suitable transcription factors for fungal host cells are described in WO 2017 / 144177. Suitable transcription factors for prokaryotic host cells are described in Seshasayee et al., 2011, Subcellular Biochemistry 52:7-23 and Balleza et al., 2009, FEMS Microbiol. Rev. 33(1):133-151.

[0742] The disclosure also provides a recombinant expression vector comprising the polynucleotides of the disclosure, promoters, and transcription and translation termination signals. Various nucleotides and control sequences can be linked together to produce a recombinant expression vector, which can include one or more convenient restriction sites to allow insertion or replacement of the polynucleotides encoding proteins at such sites. Alternatively, the polynucleotides can be expressed by inserting a polynucleotide or a nucleic acid construct comprising the polynucleotide into a suitable vector for expression. When producing an expression vector, the coding sequence is located in the vector so that the coding sequence is operably connected to the suitable control sequence for expression.

[0743] The recombinant expression vector can be any vector (e.g., plasmid or virus) that can be easily subjected to recombinant DNA procedures and can cause expression of the polynucleotide. The choice of vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector can be a linear or closed circular plasmid.

[0744] The vector can be an autonomously replicating vector, i.e. a vector existing as an extrachromosomal entity, which replicates independently of chromosomal replication, such as a plasmid, an extrachromosomal element, a minichromosome or an artificial chromosome. The vector can contain any means for ensuring self-replication. Alternatively, the vector can be a vector that is integrated into the genome and replicates with one or more chromosomes into which it has been integrated when it is introduced into the host cell. In addition, a single vector or plasmid or two or more vectors or plasmids can be used, which contain the total DNA to be introduced into the host cell genome together, or a transposon can be used.

[0745] The vector preferably contains one or more selectable markers that permit easy selection of transformed cells, transfected cells, transduced cells, etc. Selectable markers are genes whose products provide biocide or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like.

[0746] The vector preferably contains at least one element that permits integration of the vector into the host cell's genome or autonomous replication of the vector in the cell independent of the genome.

[0747] For integration into the host cell genome, the vector may rely on the polynucleotide sequence encoding the protein or any other element of the vector for integration into the genome by homologous recombination, such as homology directed repair (HDR), or non-homologous recombination, such as non-homologous end joining (NHEJ).

[0748] For autonomous replication, the vector may further comprise an origin of replication, enabling the vector to replicate autonomously in the host cell in question. The origin of replication may be any plasmid replicon that mediates autonomous replication that functions in the cell. The term "origin of replication" or "plasmid replicon" means a polynucleotide that enables a plasmid or vector to replicate in vivo.

[0749] More than one copy of the polynucleotides disclosed herein can be inserted into a host cell to increase the production of the protein. For example, 2 or 3 or 4 or 5 or more copies are inserted into a host cell. The increased copy number of the polynucleotides can be obtained by integrating at least one other copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene together with the polynucleotides, wherein cells containing amplified copies of the selectable marker gene and thus other copies of the polynucleotides can be selected by culturing cells in the presence of an appropriate selective agent.

[0750] The disclosure also provides methods for producing a recombinant host cell comprising a polynucleotide of the disclosure operably linked to one or more control sequences that direct the production of a protein of the disclosure.

[0751] The construct or vector comprising the polynucleotide is introduced into the host cell so that the construct or vector is maintained as a chromosomal integrant or as an autonomously replicating extrachromosomal vector, as described earlier. The selection of the host cell will depend to a large extent on the gene encoding the protein and its source. The protein can be native or heterologous to the recombinant host cell. In addition, at least one of the one or more control sequences can be heterologous to the polynucleotide encoding the protein. The recombinant host cell can contain a single copy or at least two copies of the polynucleotide of the present disclosure, such as three, four, five or more copies.

[0752] The host cell can be any cell that can be used to recombinantly produce a protein of the disclosure, including but not limited to prokaryotic cells, fungal cells, and plant cells, as described above.

[0753] In one aspect, the host cell is isolated.

[0754] In another aspect, the host cell is purified.

[0755] In some embodiments, the host cell is a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., Chryseobacterium viscerae), Dictyoglobulus (e.g., Dictyoglobulus thermophilus), Escherichia (e.g., Escherichia coli), Flavobacterium, Fusobacterium, Helicobacter, Gluebacter, Lysobacter (e.g., Lysobacter colloidus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0756] In some embodiments, the host cell is a Gram-positive bacterium, such as Halobacter spp. (e.g., Halobacter akibae, Halobacter clausii), Bacillus spp. (e.g., Bacillus agaricus, Bacillus alkaliphilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus delamifie, Bacillus firmus, Bacillus radiata, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus brevis, Bacillus stearothermophilus, Bacillus subtilis, Bacillus thuringiensis), Clostridium, Bacillus variabilis (e.g., Bacillus variabilis of phytohormone) , Enterococcus, Geobacillus (e.g., Geobacillus stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., Lederbergia slow), Neobacillus (e.g., Neobacillus novalis), Nocardiopsis, Oceanobacillus (e.g., Oceanobacillus barbara), Staphylococcus, Streptococcus (e.g., Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi zooepidemicus subsp.) or Streptomyces (e.g., Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, Streptomyces lividans), Sackliffia (e.g., Sackliffia hamachia).

[0757] Methods for introducing DNA into prokaryotic host cells are well known in the art, and any suitable method can be used, including but not limited to protoplast transformation, competent cell transformation, electroporation, conjugation, transduction, and DNA is introduced as linearized or circular polynucleotides. Those skilled in the art will be able to easily determine the appropriate method for introducing DNA into a given prokaryotic cell according to, for example, the genus. Methods for introducing DNA into prokaryotic host cells are described, for example, in Heinze et al., 2018, BMC Microbiology [BMC Microbiology] 18: 56, Burke et al., 2001, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences of the United States] 98: 6289-6294, Choi et al., 2006, J. Microbiol. Methods [Microbiological Methods Magazine] 64: 391-397 and Donald et al., 2013, J. Bacteriol. [Bacteriology Magazine] 195 (11): 2612-2620.

[0758] In some embodiments, the host cell is a fungal cell, such as Acremonium, Endocerium (e.g., Endocerium fuscipenser), Aspergillus (e.g., A. aculeatus, A. awamori, A. shevarii, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. snow-white-gray green, A. oryzae, A. tubingensis), A. pullulans, A. fumonis (e.g., A. fumonis, A. fumochrome), A. cereus (e.g., A. cymosum, A. fumochrome), A. cymosum (e.g., A. cymosum, A. cymosum, A. fumochrome), A. cymosum (e.g., A. cymosum, A. cymosum, A. cymosum, A. cymosum, A. cymosum), A. cymosum (e.g. ... spores, such as chrysosporium, chrysosporium dungarum, chrysosporium quinslandensis, chrysosporium tropicalis, chrysosporium with stripes), spores (e.g., spores of graminaceous spores), pseudocoprinus (e.g., pseudocoprinus cinereus), coprinus (e.g., pseudocoprinus cinereus), coriolus (e.g., coriolus furfuricus), cryptoglobulus (e.g., cryptoglobulus parasiticus), Cryptococcus, Evansstolkia (e.g., E. leycettana), smut powder, Fusarium (e.g., rod-shaped fusarium, fusarium grain, fusarium graminearum, fusarium graminearum, fusarium graminearum, fusarium heterosporum, long-stalked fusarium, Fusarium albizia, fusarium oxysporum, fusarium multibranched, pink fusarium, fusarium elderberry, skin Fusarium spp., Fusarium solani, Fusarium pseudocladosporium, Fusarium sulphureum, Fusarium rotundifolium, Fusarium pseudotricholonis, Fusarium embellishment), Humicola spp. (e.g., Humicola insolens, Humicola lanuginosus), Macrocystis spp., Microcystis spp. (e.g., Microcystis nivalis), Mucor spp. (e.g., Mucor miehei), Myceliophthora spp. (e.g., Myceliophthora thermophila), Neotrichia spp., Neurospora spp. (e.g., Neurospora crassa), Thicktopterygium spp. (e.g., Thicktopterygium barbarum), Penicillium spp., Penicillium spp. (e.g., Penicillium emersonii, Penicillium purpurogenum, Penicillium thommii, Penicillium viridiflorum), Phanerochaete spp. (e.g., Phanerochaete chrysosporium), Radialis spp. (e.g., Radialis), Pyrimethamine spp., Pleurotus spp. (e.g., Pleurotus eryngii ), Pseudomonas (e.g., Pseudomonas glaucosa), Schizophyllum, Sodiomyces (e.g., S.alcalophilus), Cylindrospermum (e.g., Cylindrospermum zeae), Talaromyces (e.g., Talaromyces spp., Talaromyces emersonii, Talaromyces rufipogon), Thermoascus (e.g., Thermoascus aureus), Themochaetoides (e.g., T.thermophila), Thermomyces (e.g., Thermomyces lanuginosus), Thermothielavioides (e.g., T.terrestris), Thermothelomyces (e.g., T.thermophilus), Thielavia (e.g., Thielavia terrestris), Tolypocladium, Trametes (e.g., Trametes tricholoma, Trametes villosa, Trametes versicolor), Trichoderma (e.g., Trichoderma amurensis, Trichoderma harzianum, Trichoderma koningii, Trichoderma longipes, Trichoderma reesei, Trichoderma viride), Trichopanax (e.g., Trichopanax vesicularis), or Phialopsora (e.g., Phialopsora annularis).

[0759] In some embodiments, the host cell is a yeast cell, such as a Candida, Hansenula, Komagata (e.g., Komagata phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., Pichia pastoris), Saccharomyces (e.g., Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces nobensis, Saccharomyces oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica).

[0760] Fungal cells can be transformed by processes involving protoplast-mediated transformation, Agrobacterium-mediated transformation, electroporation, gene gun methods, and shock wave-mediated transformation (reviewed in Li et al., 2017, Microbial Cell Factories [microbial cell factory] 16: 168) and EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences of the United States] 81: 1470-1474, Christensen et al., 1988, Bio / Technology [biological / technology] 6: 1419-1422 and Lubertozzi and Keasling, 2009, Biotechn. Advances [biotechnological progress] 27: 53-75. However, any method known in the art for introducing DNA into fungal host cells may be used, and the DNA may be introduced as a linearized or circular polynucleotide.

[0761] In some embodiments, the host cell is a plant cell, optionally selected from the following families: Amaranthaceae (e.g., chard, spinach, beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, echinacea, goldenrod, guayule, lettuce, marigold, safflower, sunflower, zinnia), Cruciferae (e.g., arugula, broccoli, cabbage, Brussels sprouts, cabbage, cauliflower, canola, kale, radish, Lepidium, horseradish, kale, mustard, radish, rapeseed, kohlrabi, turnip, horseradish, watercress, Arabidopsis), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, zucchini, pumpkin (e.g., acorn squash, winter squash, summer squash), watermelon, zucchini), and oats, ornamental grasses, rice, rye, sorghum, sugarcane, triticale, wheat, and other cereal crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, citrus, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, capsicum, eggplant, petunia, potato, tobacco, tomato), and Vitaceae (e.g., grape).

[0762] Transgenic plants and plant cells expressing proteins can be constructed according to methods known in the art. In short, plants or plant cells are constructed by incorporating one or more expression constructs encoding proteins into a plant host genome or chloroplast genome and propagating the resulting modified plants or plant cells into transgenic plants or plant cells. In one embodiment, the plant cell does not belong to a plant variety.

[0763] An expression construct is conveniently a nucleic acid construct comprising a polynucleotide encoding a protein, wherein the polynucleotide is operably linked to appropriate regulatory sequences required for expression of the polynucleotide in a selected plant or plant part. In addition, the expression construct may comprise a selectable marker that can be used to identify plant cells that have integrated the expression construct and a DNA seq...

Claims

1. Use of an enzyme-active protein, a preparation comprising an enzyme-active protein, a polynucleotide encoding an enzyme-active protein, or an organism expressing an enzyme-active protein for: a. Treating surfaces / materials susceptible to infestation / infection by one or more pests, optionally one or more mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa and / or viruses; b. Cleaning surfaces / materials infested / infected by one or more pests, optionally one or more mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa and / or viruses; c. treating (e.g., coating, dipping, impregnating, atomizing, spraying, immersing, spraying) plants or plant parts; d. treating (e.g., soaking, atomizing, misting, spraying) plant growth media; e. Treating (e.g., coating, dipping, impregnating, atomizing, irrigating, spraying, immersing, spraying) agronomic / floristry / horticultural / forestry equipment / facilities, optionally for planting, irrigating, fertilizing, growing, monitoring, testing, pruning, harvesting, processing, packaging and / or storing plants or plant parts; f. preventing, treating, inhibiting and / or eliminating infestation / infection of / caused by one or more pests of / on a surface / substance, the one or more pests being optionally one or more mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa and / or viruses; g. preventing, treating, suppressing and / or eliminating infestation / infection of / caused by / from one or more phytopathogenic pests of plants, plant parts, plant growth media or agronomic / floristry / horticultural / forestry equipment / facilities, the one or more phytopathogenic pests optionally being one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and / or weeds; h. reducing one or more aspects of disease severity in plants or plant parts affected by one or more phytopathogenic pests, optionally one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and / or weeds; i. reducing one or more aspects of disease severity in plants or plant parts grown in a plant growth medium infested / infected by one or more phytopathogenic pests, optionally one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and / or weeds; ... j. reducing one or more aspects of disease severity in plants or plant parts grown in or in contact with agronomic / floristry / horticultural / forestry equipment / facility infested / infected by one or more phytopathogenic pests, optionally one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and / or weeds; k. improving one or more soil characteristics, optionally soil structure and / or drainage; 1. Improve nutrient availability / uptake / accumulation, optionally boron, calcium, carbon, copper, iron, magnesium, manganese, molybdenum, nitrogen, phosphorus, potassium, sulfur and / or zinc availability / uptake / accumulation; m. improving one or more plant growth and / or development characteristics; n. Reduce the need for external fertilizers; o. reducing one or more amounts of exogenous fertilizer required to achieve the desired result; p. improving one or more plant yield characteristics; q. Prolonging the storage period of harvested plants or plant parts; r. Delaying the maturity of harvested plants or plant parts; s. Accelerate the maturation of harvested plants or plant parts; t. improving the efficacy of a chemical pesticide, which is optionally a miticide, bactericide, fungicide, gastropodicide, herbicide, insecticide, nematicide, oomycete, protozoicide or viricide; u. Improving the efficacy of a biopesticide, which is optionally a miticide, bactericide, fungicide, gastropodicide, herbicide, insecticide, nematicide, oomycicide, protozoicide or virucide: v. Improve the efficacy of pre-harvest treatment agents; w. Improve the efficacy of post-harvest treatment agents; x. Prevent, treat, suppress and / or eliminate chemical pesticide-induced pest resistance and / or phytotoxicity; y. preventing, treating, suppressing and / or eliminating biopesticide-induced pest resistance and / or phytotoxicity; and / or z. included as part of an integrated pest management plan / strategy, optionally an integrated pest management plan / strategy that includes one or more chemical pesticides, The enzymatically active protein is selected from the group consisting of: i. a polypeptide having glucose oxidase activity; ii. a polypeptide having glucose oxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 1-5 and 183-2205; iii. a polypeptide having glucose oxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 1-5 and 183-2205; iv. a polypeptide having glucose oxidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 92-96 or a cDNA sequence thereof; v. A polypeptide having cellobiose oxidase activity; vi. a polypeptide having cellobiose oxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 6-8 and 2206-2217; vii. a polypeptide having cellobiose oxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 6-8 and 2206-2217; viii. a polypeptide having cellobiose oxidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 97-99, or a cDNA sequence thereof; ix. A polypeptide having laccase activity; x. a polypeptide having laccase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 9 and 2218-2251; xi. a polypeptide having laccase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 9 and 2218-2251; xii. a polypeptide having laccase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 100 or its cDNA sequence; xiii. A polypeptide having catalase activity; xiv. a polypeptide having catalase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 10-12 and 2252-2296; xv. a polypeptide having catalase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 10-12 and 2252-2296; xvi. a polypeptide having catalase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 101-103, or a cDNA sequence thereof; xvii. A polypeptide having peroxidase activity; xviii. a polypeptide having peroxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 13 and 2297-2381; xix. a polypeptide having peroxidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 13 and 2297-2381; xkx. A polypeptide having peroxidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 104 or its cDNA sequence; xxi. A polypeptide having lytic cellulose monooxygenase activity; xxii. a polypeptide having lytic cellulose monooxygenase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 800%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 14-15 and 2382-2755; xxiii. a polypeptide having lytic cellulose monooxygenase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 14-15 and 2382-2755; xxiv. a polypeptide having lytic cellulose monooxygenase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 105-106, or a cDNA sequence thereof; xxv. A polypeptide having γ-glutamyl transferase activity; xxvi. a polypeptide having gamma-glutamyl transferase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 16 and 2756-2769; xxvii. a polypeptide having gamma-glutamyl transferase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 16 and 2756-2769; xxviii. a polypeptide having gamma-glutamyl transferase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NO: 107 or a cDNA sequence thereof; xxix. A polypeptide having triglyceride lipase activity; xxx. a polypeptide having triacylglycerol lipase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 17-22 and 2778-10223; xxxi. A polypeptide having triacylglycerol lipase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 17-22 and 2778-10223; xxxii. a polypeptide having triacylglycerol lipase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 108-113 or a cDNA sequence thereof; xxxiii. A polypeptide having triglyceride lipase and / or phospholipase A1 activity; xxxiv. a polypeptide having triacylglycerol lipase and / or phospholipase A1 activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 23 and 10243-15978; xxxv. a polypeptide having triacylglycerol lipase and / or phospholipase A1 activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 23 and 10243-15978; xxxvi. A polypeptide having triacylglycerol lipase and / or phospholipase A1 activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NO: 114 or a cDNA sequence thereof; xxxvii. A polypeptide having lysophospholipase activity; xxxviii. a polypeptide having lysophospholipase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 24 and 15979-15981; xxxix. A polypeptide having lysophospholipase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 24 and 15979-15981; xl. a polypeptide having lysophospholipase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 115 or its cDNA sequence; xli. A polypeptide having pectinesterase activity; xlii. A polypeptide having pectinesterase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 25 and 2770-2777; xliii. a polypeptide having pectinesterase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 25 and 2770-2777; xliv. A polypeptide having pectinesterase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 116 or its cDNA sequence; xlv. A polypeptide having phospholipase A1 activity; xlvi. a polypeptide having phospholipase A1 activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 26 and 10224-10242; xlvii. A polypeptide having phospholipase A1 activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 26 and 10224-10242; xlviii. A polypeptide having phospholipase A1 activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 117 or its cDNA sequence; xlix. A polypeptide having cutinase activity; 1. A polypeptide having cutinase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 27-31 and 15982-16004; li. a polypeptide having cutinase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 27-31 and 15982-16004; lii. A polypeptide having cutinase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 118-122 or a cDNA sequence thereof; liii. A polypeptide having phospholipase C activity; liv. A polypeptide having phospholipase C activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 32 and 16396-16412; lv. a polypeptide having phospholipase C activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 32 and 16396-16412; lvi. a polypeptide having phospholipase C activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NQ: 123 or its cDNA sequence; lvii. A polypeptide having phosphoinositide phospholipase C activity; lviii. a polypeptide having phosphoinositide phospholipase C activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 33 and 16005-16395; lix. a polypeptide having phosphoinositide phospholipase C activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 33 and 16005-16395; 1x. a polypeptide having phosphoinositide phospholipase C activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NO: 124 or a cDNA sequence thereof; lxi. A polypeptide having amylase activity; lxii. A polypeptide having α-amylase activity; 1xiii. a polypeptide having alpha-amylase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 34-40 and 16413-45041; lxiv. A polypeptide having alpha-amylase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 34-40 and 16413-45041; 1xv. A polypeptide having alpha-amylase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 125-131 or a cDNA sequence thereof; lxvi. A polypeptide having β-amylase activity; lxvii. A polypeptide having glucanase activity; lxviii. A polypeptide having α-glucanase activity; lxix. A polypeptide having β-glucanase activity; lxx. A polypeptide having glucan 1,4-α-glucosidase activity; lxxi. A polypeptide having glucan 1,4-alpha-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:41-42 and 45756-45904; lxxii. a polypeptide having glucan 1,4-alpha-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 41-42 and 45756-45904; 1xxiii. a polypeptide having glucan 1,4-alpha-glucosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 132-133 or a cDNA sequence thereof; lxxiv. A polypeptide having cellulase activity; lxxv. a polypeptide having cellulase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 43-45 and 45913-48750; lxxvi. a polypeptide having cellulase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 43-45 and 45913-48750; lxxvii. A polypeptide having cellulase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 134-136 or a cDNA sequence thereof; lxxviii. A polypeptide having endo-1,3(4)-β-glucanase activity; lxxix. A polypeptide having endo-1,3(4)-β-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs:46 and 49229-49346; lxxx. A polypeptide having endo-1,3(4)-β-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:46 and 49229-49346; 1xxxi. A polypeptide having endo-1,3(4)-β-glucanase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 137 or its cDNA sequence; lxxxii. A polypeptide having inulinase activity; lxxxiii. a polypeptide having inulinase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:47 and 49347-49419; lxxxiv. a polypeptide having inulinase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:47 and 49347-49419; 1xxxv. A polypeptide having inulinase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 138 or a cDNA sequence thereof; lxxxvi. A polypeptide having endo-1,4-β-xylanase activity; lxxxvii. A polypeptide having endo-1,4-beta-xylanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:48-53 and 49453-49912; lxxxviii. a polypeptide having endo-1,4-beta-xylanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs:48-53 and 49453-49912; lxxxix. A polypeptide having endo-1,4-beta-xylanase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 139-144, or a cDNA sequence thereof; xc. A polypeptide having dextranase activity; xci. A polypeptide having dextranase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 54 and 45063-45071; xcii. A polypeptide having dextranase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 54 and 45063-45071; xciii. a polypeptide having dextranase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 145 or its cDNA sequence; xciv. A polypeptide having chitinase activity; xcv. A polypeptide having endo-polygalacturonase (pectinase) activity; xcvi. A polypeptide having lysozyme activity; xcvii. A polypeptide having lysozyme activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 56 and 45443-45456; xcviii. a polypeptide having lysozyme activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 56 and 45443-45456; xcix. A polypeptide having lysozyme activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 147 or its cDNA sequence; c. a polypeptide having α-glucosidase activity; ci. A polypeptide having β-glucosidase activity; cii. a polypeptide having beta-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 57 and 45457-45754; ciii. a polypeptide having beta-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 57 and 45457-45754; civ. having beta-glucosidase activity and consisting of a polypeptide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100%, 101%, 102%, 103%, 104%, 105%, 106%, 107%, 108%, 109%, 110%, 111%, 112%, 113%, 114%, 115%, 116%, 117%, 118%, 119%, 120%, 121%, 122%, 123%, 124%, 125%, 126%, 127%, 128%, 129%, 130%, 131%, 132%, 133%, 134%, 135%, 136%, 137%, 138%, 139%, 140%, 141%, 142%, 143%, 144%, 145%, 146%, 147%, 148%, 149%, 150%, 151%, 152%, 153%, 154%, 155%, 156%, 157%, 158%, 159%, 160%, 8 polypeptides encoded by polynucleotides having 7%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity; cv. A polypeptide having α-galactosidase activity; cvi. A polypeptide having β-galactosidase activity; cvii. A polypeptide having α-mannosidase activity; cviii. a polypeptide having alpha-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 58 and 45755; cix. a polypeptide having alpha-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 58 and 45755; cx. a polypeptide having alpha-mannosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 149 or its cDNA sequence; cxi. A polypeptide having β-mannosidase activity; cxii. A polypeptide having endo-1,3-β-xylanase activity; cxiii. A polypeptide having endoglucanase-1,3-β-D-glucosidase activity; cxiv. A polypeptide having endo-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 59-60 and 45905-45912; cxv. a polypeptide having glucan endo-1,3-beta-D-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 59-60 and 45905-45912; cxvi. A polypeptide having endo-glucanase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 150-151 or a cDNA sequence thereof; cxvii. A polypeptide having pullulanase activity; cxviii. A polypeptide having pullulanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 61 and 48751-49148; cxix. A polypeptide having pullulanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 61 and 48751-49148; cxx. A polypeptide having pullulanase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 152 or its cDNA sequence; cxxi. A polypeptide having α-L-arabinofuranosidase activity; cxxii. A polypeptide having alpha-L-arabinofuranosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 62 and 49149-49209; cxxiii. a polypeptide having alpha-L-arabinofuranosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 62 and 49149-49209; cxxiv. a polypeptide having α-L-arabinofuranosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 153 or its cDNA sequence; cxxv. A polypeptide having glucan 1,3-β-glucosidase activity; cxxvi. A polypeptide having endoglucanase-1,3-α-glucosidase activity; cxxvii. A polypeptide having endo-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 63-64 and 49210-49228; cxxviii. A polypeptide having glucan endo-1,3-alpha-glucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 63-64 and 49210-49228; cxxix. A polypeptide having endo-1,3-alpha-glucosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 154-155 or a cDNA sequence thereof; cxxx. A polypeptide having glucan 1,4-ɑ-glucosidase activity; cxxxi. A polypeptide having glucan 1,6-ɑ-glucosidase activity; cxxxii. A polypeptide having endoglucanase-1,2-β-glucosidase activity; cxxxiii. A polypeptide having xylanase activity; cxxxiv. A polypeptide having lichenase activity; cxxxv. A polypeptide having lichenase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOS: 65 and 49420-49446; cxxxvi. A polypeptide having lichenase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 65 and 49420-49446; cxxxvii. A polypeptide having lichenase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 156 or its cDNA sequence; cxxxviii. A polypeptide having glucan 1,4-β-glucosidase activity; cxxxix. A polypeptide having endo-1,6-β-glucosidase activity; cxl. a polypeptide having endo-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 66-67 and 49447-49451; cxli. A polypeptide having endo-glucanase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 66-67 and 49447-49451; cxlii. A polypeptide having endo-glucanase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 157-158 or a cDNA sequence thereof; cxliii. A polypeptide having mannan 1,2-(1,3)-α-mannosidase activity; cxliv. A polypeptide having mannan endo-1,4-β-mannosidase activity; cxlv. A polypeptide having endomannan-1,4-beta-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 68, 72144, and 49452; cxlvi. A polypeptide having mannan endo-1,4-beta-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 68, 72144, and 49452; cxlvii. A polypeptide having mannan endo-1,4-beta-mannosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 159 and 72145 or a cDNA sequence thereof; cxlviii. A polypeptide having glucan 1,3-α-glucosidase activity; cxlix. A polypeptide having cellulose 1,4-β-cellobiosidase activity; cl. A polypeptide having mannan endo-1,6-α-mannosidase activity; cli. A polypeptide having mannan endo-1,6-α-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 69 and 45042; clii. A polypeptide having mannan endo-1,6-α-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 69 and 45042; cliii. A polypeptide having mannan endo-1,6-α-mannosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 160 or its cDNA sequence; cliv. A polypeptide having endoglucosidase activity; clv. a polypeptide having endoglucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 70-75 and 45043-45062; clvi. A polypeptide having endoglucosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 70-75 and 45043-45062; clvii. A polypeptide having endoglucosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 161-166 or a cDNA sequence thereof; clviii. A polypeptide having glycoprotein endo-α-1,2-mannosidase activity; clix. A polypeptide having glycoprotein endo-alpha-1,2-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs:76-77; clx. A polypeptide having glycoprotein endo-alpha-1,2-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 76-77; clxi. A polypeptide having glycoprotein endo-alpha-1,2-mannosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 167-168 or a cDNA sequence thereof; clxii. A polypeptide having chitosanase activity; clxiii. A polypeptide having glucan 1,4-αa-maltose hydratase activity; clxiv. A polypeptide having glucan 1,4-alpha-maltose hydratase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 78 and 45072-45408; clxv. A polypeptide having glucan 1,4-α-maltose hydratase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 78 and 45072-45408; clxvi. A polypeptide having glucan 1,4-α-maltose hydratase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 169 or its cDNA sequence; clxvii. A polypeptide having 1,6-α-D-mannosidase activity; clxviii. A polypeptide having 1,6-alpha-D-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 79 and 45437-45442; clxix. A polypeptide having 1,6-alpha-D-mannosidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 79 and 45437-45442; clxx. A polypeptide having 1,6-alpha-D-mannosidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 170 or its cDNA sequence; clxxi. A polypeptide having β-1,2-mannosidase activity; clxxii. A polypeptide having aminopeptidase activity; clxxiii. A polypeptide having leucyl aminopeptidase activity; clxxiv. A polypeptide having alanyl aminopeptidase activity; clxxv. A polypeptide having cysteinyl aminopeptidase activity; clxxvi. A polypeptide having tripeptide aminopeptidase activity; clxxvii. A polypeptide having prolyl aminopeptidase activity; clxxviii. A polypeptide having glutamyl aminopeptidase activity; clxxix. A polypeptide having cytoplasmic aminopeptidase activity; clxxx. A polypeptide having tryptophanyl aminopeptidase activity; clxxxi. A polypeptide having methionyl aminopeptidase activity; clxxxii. A polypeptide having aspartyl aminopeptidase activity; clxxxiii. Polypeptide having carboxypeptidase activity; clxxxiv. A polypeptide having endopeptidase activity; clxxxv. A polypeptide having serine endopeptidase activity; clxxxvi. A polypeptide having serine endopeptidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 80-81 and 49913-50777; clxxxvii. A polypeptide having serine endopeptidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 80-81 and 49913-50777; clxxxviii. A polypeptide having serine endopeptidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 171-172, or a cDNA sequence thereof; clxxxix. A polypeptide having glutamyl endopeptidase activity; cxc. a polypeptide having glutamyl endopeptidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 82 and 50778-50953; cxci. A polypeptide having glutamyl endopeptidase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 82 and 50778-50953; cxcii. A polypeptide having glutamyl endopeptidase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 173 or its cDNA sequence; cxciii. A polypeptide having subtilisin activity; cxciv. A polypeptide having subtilisin activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 83-87 and 50954-70838; cxcv. A polypeptide having subtilisin activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 83-87 and 50954-70838; cxcvi. A polypeptide having subtilisin activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SQ ID NOs: 174-178 or a cDNA sequence thereof; cxcvii. A polypeptide having bacillus lysin activity; cxcviii. A polypeptide having bacillus lysin activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 88 and 70839-71903; cxcix. A polypeptide having bacillus lysin activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 88 and 70839-71903; cc. a polypeptide having bacitracin activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 179 or its cDNA sequence; cci. A polypeptide having asparaginase activity; ccii. A polypeptide having asparaginase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 89-90 and 71904-72141; cciii. a polypeptide having asparaginase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 89-90 and 71904-72141; cciv. A polypeptide having asparaginase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NOs: 180-181 or a cDNA sequence thereof; ccv. A polypeptide having glutaminase activity; ccvi. A polypeptide having amidase activity; ccvii. A polypeptide having urease activity; ccviii. A polypeptide having hydrolase activity; ccix. A polypeptide having deacetylase activity; ccx. A polypeptide having deaminase activity; ccxi. A polypeptide having pectate lyase activity; ccxii. A polypeptide having pectate lyase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 91 and 72142-72143; ccxiii. a polypeptide having pectate lyase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 91 and 72142-72143; ccxiv. A polypeptide having pectate lyase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 182 or its cDNA sequence; ccxv. A polypeptide having pectin lyase activity; ccxvi. A polypeptide having pectin lyase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one or more of SEQ ID NOs: 55 and 45409-45436; ccxvii. A polypeptide having pectin lyase activity and having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to the mature polypeptide of any one of SEQ ID NOs: 55 and 45409-45436; ccxviii. A polypeptide having pectin lyase activity and encoded by a polynucleotide having at least 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one or more of SEQ ID NO: 146 or a cDNA sequence thereof; ccxix. A polypeptide having glucan lyase activity; ccxx. A polypeptide having α-1,4-glucan lyase activity: ccxxi. any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 and 183-72143 or an enzymatically active fragment / mutant / variant thereof of the mature polypeptide; ccxxii. An enzymatically active polypeptide derived from any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, 72149 and 183-72143 by substitution, deletion or insertion of one or more amino acids; ccxxiii. An enzymatically active polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 and 183-72143 by substitution, deletion or insertion of one or more amino acids; ccxxiv. An enzymatically active polypeptide derived from any one of the polypeptides of i) to ccxxiii), wherein the N-terminus and / or the C-terminus has been extended by adding one or more amino acids; An enzymatically active fragment of the polypeptide of any one of ccxxv.i) to ccxxiv); and ccxxvi. A fusion protein comprising a first polypeptide having a first enzyme activity and a second polypeptide having a second enzyme activity, wherein at least one of the first polypeptide and the second polypeptide optionally comprises the polypeptide of any one of i) to ccxxv).

2. A method comprising applying an enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above to plants, plant parts, plant growth media and / or agronomic / floristry / horticultural / forestry equipment / facilities.

3. A formulation comprising an enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above in an agriculturally acceptable carrier.

4. A method comprising applying a formulation as claimed in claim 3 to plants, plant parts, plant growth media and / or agronomic / floristry / horticultural / forestry equipment / facilities.

5. A method comprising applying a cell, optionally a recombinant host cell, expressing an enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above to a plant, a plant part, a plant growth medium and / or agronomic / floristry / horticultural / forestry equipment / facilities.

6. A plant or plant part comprising a heterologous polynucleotide encoding an enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above.

7. A plant or plant part expressing a heterologous enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above.

8. A method comprising introducing into a plant growth medium a plant or plant part comprising a heterologous polynucleotide encoding an enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above.

9. A method comprising introducing into a plant growth medium a plant or plant part expressing a heterologous enzymatically active protein selected from the group consisting of i) to ccxxvi) as defined in claim 1 above.

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