Compositions and methods for preventing, treating, suppressing and / or eliminating parasitism and infection by phytopathogens

JP2025518489A5Pending Publication Date: 2026-05-20NOVO NORDISK AS +1
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Patent Information

Authority / Receiving Office
JP · JP
Patent Type
Applications
Current Assignee / Owner
NOVO NORDISK AS
Filing Date
2023-05-12
Publication Date
2026-05-20

AI Technical Summary

Technical Problem

Current agricultural treatments for plant diseases, particularly those caused by fungi and bacteria, often rely on chemical pesticides that can be harmful to the environment and may lead to pesticide resistance in pathogens.

Method used

Development of enzyme treatment agents that target specific plant pathogens, such as Blumeria graminis, Botrytis cinerea, Fusarium graminearum, and others, to control disease severity and promote plant health.

Benefits of technology

The enzyme treatment agents demonstrate significant disease control efficacy, as shown in various efficacy tests, reducing disease severity and promoting healthy plant growth with minimal environmental impact.

✦ Generated by Eureka AI based on patent content.

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Abstract

The present disclosure provides proteins useful for preventing, treating, suppressing and / or eliminating plant parasitism and infection by various phytopathogenic pests, as well as formulations containing such proteins, polynucleotides encoding such proteins, organisms expressing such proteins, and methods of using such proteins, formulations, polynucleotides and organisms in agriculture and other fields of endeavor.
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Description

Background Art

[0001] Related Applications This application claims priority to International Patent Application Publication No. PCT / US2022 / 073761, filed on July 15, 2022 and published as International Publication No. 2023 / 288,294 on January 19, 2023, and to U.S. Provisional Patent Application No. 63 / 342,064, filed on May 14, 2022, and to U.S. Provisional Patent Application No. 63 / 476,590, filed on December 21, 2022, the entire disclosures of each of which are hereby incorporated by reference in their entirety.

[0002] Reference to Sequence Listing This application contains a sequence listing in computer-readable form. The file name containing the sequence listing is SQ.XML. This was created on May 12, 2023 and contains 89,744,839 bytes. This computer-readable form is hereby incorporated by reference in its entirety.

Brief Description of the Drawings

[0003]

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Mode for Carrying Out the Invention

[0004] This description is not intended to be an exhaustive list of all the various ways in which the inventive concepts disclosed herein may be implemented or of all the features that may be added to the invention. For example, features shown with respect to one embodiment may be incorporated into other embodiments, and features shown with respect to a particular embodiment may be deleted from that embodiment. Further, many modifications and additions to the various embodiments proposed herein that do not depart from the invention will be apparent to those skilled in the art in light of this disclosure. Accordingly, the following specification is intended to illustrate some embodiments of the invention and is not intended to specifically identify all changes, combinations, and variations thereof.

[0005] The terms used herein are for the purpose of describing particular embodiments only and are not intended to limit the invention.

[0006] Unless otherwise defined, all terms (including technical and scientific terms) used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Further, terms such as those defined in commonly used dictionaries are to be interpreted as having a meaning that coincides with their meaning in the context of the relevant art and this specification and are not to be interpreted in an idealized or overly formal sense unless expressly so defined herein. For brevity and / or clarity, well-known functions or structures may not be described in detail.

[0007] 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.

[0008] As used herein, “additive,” when referring to the effect of a combination in a composition, means that the effect of the combination is generally approximately the same as the sum of the effects of the individual components of the combination. The combination of individual components that produces this effect may be referred to as an additive combination.

[0009] As used herein, the terms "agricultural equipment / facilities, flower cultivation equipment / facilities, horticultural equipment / facilities and / or forestry planting equipment / facilities" and "agricultural / flower cultivation / horticultural / forestry planting equipment / facilities" refer to devices or facilities used in one or more aspects of plant and plant part breeding, planting, irrigation, fertilization, growth, monitoring, testing, pruning, harvesting, processing, packaging and / or storage, including but not limited to these. Exemplary devices and facilities include tillage tractors, seed containers, seeders, planting pots, hydroponic systems, plant cultivation boxes, greenhouses, sprayers, fertilizer drills, fertilizer spreaders, irrigation systems, harvesting devices, post-harvest storage containers, post-harvest treatment chambers, and post-harvest transport containers.

[0010] 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 environment (e.g., soil) without causing / having an excessive adverse effect on plant growth, development, and / or yield. As used herein, the term "foliar compatibility carrier" refers to a substance that can be applied to the leaves of a plant or plant part without causing / having an excessive adverse effect on the plant, plant part, plant growth, plant health, etc. As used herein, the term "seed compatibility carrier" refers to a substance that can be applied to a seed without causing / having an excessive adverse effect on the seed, the plant growing from the seed, seed germination, etc. As used herein, the term "soil compatibility carrier" refers to a substance that can be applied to soil without causing / having an excessive adverse effect on plant growth, soil structure, soil drainage, etc.

[0011] As used herein, the term "and / or" is intended to include any combination of one or more of the associated listed items, as well as the absence of a combination when interpreted in the 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 and C, or C".

[0012] As used herein, when referring to the effect of a combination in a composition, “antagonistic” means that the effect of the combination is generally less than the sum of the effects of the individual components of the combination. These compositions may be referred to as antagonistic combinations.

[0013] As used herein, the term “aqueous” refers to a composition that contains more than a trace amount of water (i.e., more than 0.5% by weight of water based on the total weight of the composition).

[0014] As used herein, the terms “associated with,” “in association with,” and “associated therewith,” when used with reference to the relationship between the compositions of the present disclosure and a plant or plant part, refer to at least juxtaposition, or proximity, of the composition with the plant or plant part. Such juxtaposition or proximity can be achieved by directly contacting or applying the composition to the plant or plant part and / or by applying the composition to the plant growth environment (e.g., soil) in which the plant or plant part grows. According to some embodiments, the composition is applied as a coating to the outer surface of the plant or plant part. According to some embodiments, the composition is applied to the soil near, at, or surrounding the site where the plant or plant part grows (or is currently growing).

[0015] As used herein, the term “beneficial agent” can refer to any agent having at least one agriculturally / horticulturally / forestry-beneficial property (e.g., the ability to fix atmospheric nitrogen, solubilize phosphates, produce one or more agriculturally / horticulturally / forestry-beneficial small molecules such as plant signaling molecules, stimulate one or more plant defense systems, and produce one or more plant defense agents such as insecticidal toxins).

[0016] As used herein, the term "biostimulant" refers to an agent or combination of agents whose application promotes one or more metabolic processes, and / or physiological processes (e.g., carbohydrate biosynthesis, ion uptake, nucleic acid uptake, nutrient delivery, photosynthesis and / or respiration) in a plant or plant part.

[0017] As used herein, the term "binding module" refers to an enzyme region that mediates the binding of an enzyme to a substrate.

[0018] As used herein, the term "catalytic domain" refers to an enzyme region that contains the catalytic mechanism of an enzyme.

[0019] As used herein, the term "cDNA" means a DNA molecule that can be prepared by reverse transcription from a mature, spliced mRNA molecule obtained from a eukaryotic or prokaryotic cell. 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 before it results in the spliced mature mRNA.

[0020] As used herein, the term "coding sequence" means a polynucleotide that directly specifies the amino acid sequence of a polypeptide. The boundaries of the coding sequence are generally 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 combinations thereof.

[0021] As used herein, the terms "colony forming unit" and "cfu" refer to microbial cells / spores that are capable of growing 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.

[0022] As used herein, the term "consists essentially of", when used in reference to the compositions and methods of the present disclosure, means that the composition / method may contain additional components / steps, provided that the additional components / steps do not substantially alter the composition / method. The term "substantially alter" when applied to the compositions / methods of the present disclosure refers to an increase or decrease in the effectiveness of the composition / method of at least about 20% or more. For example, a component added to a composition of the present disclosure may be considered to "substantially alter" the composition if it increases or decreases the ability of the composition to inhibit the growth of a target plant pathogen by at least 20%.

[0023] As used herein, the term "control sequence" refers to a nucleic acid sequence involved in regulating the expression of a polynucleotide in a particular organism or in vitro. Each control sequence may be native (i.e., derived from the same gene) or heterologous (i.e., derived from a different gene) to the polynucleotide encoding the polypeptide, and may be native or heterologous to each other. Such control sequences include, but are not limited to, leader, polyadenylation, prepropeptide, propeptide, signal peptide, promoter, terminator, enhancer and transcription or translation initiator, and terminator sequences. At a minimum, the control sequences include a promoter, as well as transcription and translation termination signals. The control sequences may be provided together with a linker to introduce specific restriction sites that facilitate ligation of the control sequences with the coding region of the polynucleotide encoding the polypeptide.

[0024] 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 is naturally present in the organism.

[0025] As used herein, the term "diazotroph" refers to an organism capable of converting atmospheric nitrogen (N2) into a form (e.g., ammonia (NH3), ammonium (NH4+), etc.) that can be utilized by a plant or a plant part.

[0026] As used herein, the term "dispersant" refers to an agent or combination of agents, the application of which reduces the cohesiveness 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.

[0027] 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., inhibition of a plant disease, improvement of plant yield). The absolute value of the amount / concentration sufficient to cause a desired effect can be affected by factors such as the type and scale of the desired effect, the type, size, and volume of the substance to which the composition is to be applied, the type of enzyme in the composition, the amount of enzyme in the composition, the stability of the enzyme in the composition, and storage conditions (e.g., temperature, relative humidity, duration). One of ordinary skill in the art will understand how to select an effective amount / concentration using routine 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.

[0028] As used herein, the term "endogenous gene" refers to a gene consisting of an endogenous polynucleotide.

[0029] As used herein, the term "endogenous polynucleotide" refers to a polynucleotide that is native to the host cell being referenced.

[0030] As used herein, the terms "improved growth" and "improved plant growth" refer to an improvement in one or more characteristics of plant growth and / or development when compared to one or more control plants (e.g., plants germinated from untreated seeds or untreated plants). Exemplary plant growth / development 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., uptake of calcium, magnesium, nitrogen, phosphorus, and / or potassium), photosynthesis rate, root area, root diameter, root length, root mass, root nodulation (e.g., root nodule mass, root nodule number, root nodule volume), root number, root surface area, root volume, salt tolerance, seed germination, seedling emergence, shoot diameter, shoot length, shoot mass, shoot number, shoot surface area, shoot volume, spread, stomatal conductance, and survival rate.

[0031] As used herein, the terms "improved stability" and "improved enzyme stability" refer to an improvement in one or more characteristics of enzyme stability when compared to one or more controls (e.g., control compositions identical to the compositions of the present disclosure except lacking one or more of the components found in the compositions 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 over a defined period of time, and the ability to cause a desired effect (e.g., reduction in the phytopathogenicity of a target pest) after application to a plant or plant part and / or storage over a defined period of time.

[0032] As used herein, the terms "improved yield" and "improved plant yield" refer to an improvement in one or more characteristics of plant yield as compared to one or more control plants (e.g., control plants germinated from untreated seeds). Exemplary plant yield characteristics include biomass; bushels per acre; crop weight per plot (GWTPP); nutrient content; percentage of plants in a given area (e.g., plot) that are unable to produce a crop; yield at a standard moisture percentage (YSMP), e.g., crop yield at a standard moisture percentage (GYSMP); yield per plot (YPP), e.g., crop weight per plot (GWTPP); and yield reduction (YRED), but are not limited to these.

[0033] 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, for example, measurement of the level of mRNA and / or translated polypeptide to detect an increase in expression.

[0034] As used herein, the term "expression vector" refers to a linear or circular DNA construct that contains a DNA sequence encoding a polypeptide, wherein the coding sequence is operably linked to suitable control sequences capable of causing DNA expression in a suitable host. Such control sequences can include a promoter that causes transcription, an optional operator sequence that controls transcription, a sequence encoding a suitable ribosome binding site on the mRNA, an enhancer, and sequences that control the termination of transcription and translation.

[0035] As used herein, the term "extension" refers to the addition of one or more amino acids to the amino terminus and / or carboxy terminus of a polypeptide.

[0036] As used herein, the term "foliage" refers to the parts of a plant that normally grow above ground, including but not limited to leaves, stalks, stems, flowers, fruiting bodies, and fruits.

[0037] As used herein, the terms "foliar application" and "foliarly applied" refer to the application of one or more active ingredients to the foliage of a plant (e.g., the leaves of a plant). The application can be effected by any suitable means including, but not limited to, spraying / fogging a composition containing the active ingredient onto the plant. In some embodiments, the active ingredient is applied to the leaves, stems, and / or stalks of the plant and not to the flowers, fruiting bodies, or fruits of the plant.

[0038] As used herein, the term "fragment" refers to a polypeptide having one or more amino acids that are not present at the amino- and / or carboxy-terminus of the mature polypeptide.

[0039] As used herein, the term "fusion protein" refers to a polypeptide in which a polypeptide is fused at the N-terminus and / or C-terminus of a polypeptide of the present disclosure. Fusion proteins are produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present disclosure, or by fusing two or more polynucleotides of the present disclosure together. Techniques for producing fusion proteins are known in the art and include ligating the coding sequences encoding the polypeptides such that they are in-frame and the expression of the fusion protein is under the control of the same promoter and terminator. Fusion proteins may also be constructed using intein technology in which the fusion protein is formed after translation (Cooper et al., 1993, EMBO J. 12:2575-2583; Dawson et al., 1994, Science 266:776-779). Fusion proteins can further include a cleavage site between the two polypeptides. Upon secretion of the fusion protein, this site is cleaved and the two polypeptides are released. 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., 1995, 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.

[0040] As used herein, when used to describe the relationship between a polynucleotide or polypeptide and a host cell, the term "heterologous" refers to a polynucleotide or polypeptide that is not naturally present in the host cell. For the purposes of the present disclosure, an exogenous copy of a polynucleotide that is unmodified with respect to a reference host cell is considered a heterologous polynucleotide.

[0041] As used herein, when used to describe the relationship between a polynucleotide or polypeptide and a control sequence (e.g., a promoter sequence), the term "heterologous" refers to a polynucleotide or polypeptide that is not naturally associated with the control sequence (i.e., the control sequence is derived from a gene other than the gene encoding the mature polypeptide).

[0042] As used herein, the terms "host strain" or "host cell" refer to an organism into which an expression vector, phage, virus, or other DNA construct containing 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 that are capable of expressing the protein of interest. The term "host cell" includes protoplasts generated from the cells.

[0043] As used herein, the terms "inoculum composition" and "inoculum material" refer to a composition containing microbial cells and / or spores that are capable of growing / 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.

[0044] As used herein, when used to describe inserting a nucleic acid sequence into a cell, the term "introduced" encompasses "transfection", "transformation", or "transduction" as known in the art.

[0045] As used herein, the term "isolated" means a polypeptide, nucleic acid, cell, or other specific material or component that is separated from at least one other material or component, including but not limited to other proteins, nucleic acids, cells, etc. Thus, an isolated polypeptide, nucleic acid, cell, or other material is in a form that does not exist naturally. Examples of isolated polypeptides include, but are not limited to, culture broths containing polypeptides expressed and secreted in host cells.

[0046] As used herein, the term "isomer" includes all stereoisomers of the compound and / or molecule it refers to, including enantiomers and diastereomers, as well as all conformational isomers, rotational isomers, and tautomers, unless otherwise specified. The compounds and / or molecules disclosed herein include all enantiomers in substantially pure levorotatory or dextrorotatory forms, or in racemic mixtures, or in any ratio of enantiomers. If an embodiment discloses a (D)-enantiomer, that embodiment also includes the (L)-enantiomer; if an embodiment discloses an (L)-enantiomer, that embodiment also includes the (D)-enantiomer. If an embodiment discloses a (+)-enantiomer, that embodiment also includes the (-)-enantiomer; if an embodiment discloses a (-)-enantiomer, that embodiment also includes the (+)-enantiomer. If an embodiment discloses an (S)-enantiomer, that embodiment also includes the (R)-enantiomer; if an embodiment discloses an (R)-enantiomer, that embodiment also includes the (S)-enantiomer. Embodiments are intended to include any diastereomers of the compounds and / or molecules referred to herein in diastereomerically pure form and in the form of mixtures in any ratio. Unless stereochemistry is explicitly indicated in the chemical structure or chemical name, the chemical structure or chemical name is intended to encompass all possible stereoisomers, conformational isomers, rotational isomers, and tautomers of the compound and / or molecule shown.

[0047] As used herein, the term "mature polypeptide" means the polypeptide in its mature form after N-terminal and / or C-terminal processing (e.g., removal of the signal peptide).

[0048] As used herein, the term "mature polypeptide coding sequence" means a polynucleotide that encodes a mature polypeptide.

[0049] As used herein, the term "modified microbial strain" refers to a microbial strain modified from a strain isolated from nature. Modified microbial strains include chemical or other forms of induced mutations to polynucleotides within any genome within the strain; insertions or deletions of one or more nucleotides within any genome within the strain, or combinations thereof; inversion of at least one segment of DNA within any genome within the strain; translocation of any genome within the strain; generalized or specific transduction of homozygous or heterozygous polynucleotide segments into any genome within the strain; introduction of one or more phages into any genome of the strain; transformation of any strain resulting in the introduction of stably replicating extrachromosomal DNA into the strain; any change to any genome or total DNA composition within a strain isolated from nature as a result of combination with any different microbial strain; and can be produced by any suitable method including, but not limited to, any combination of the above. The term modified microbial strain includes (a) one or more heterologous nucleotide sequences, (b) one or more non-natural copies of a nucleotide sequence isolated from nature (i.e., additional copies of a gene that is naturally present in the microbial strain from which the modified microbial strain is derived), (c) the absence of one or more nucleotide sequences that would be present in a natural reference strain, for example by deletion of the nucleotide sequence, and (d) strains having additional extrachromosomal DNA. In some embodiments, the modified microbial strain comprises a combination of two or more nucleotide sequences (e.g., two or more native genes not naturally present in the same microbial strain) or comprises a nucleotide sequence isolated from nature at a locus different from the native locus.

[0050] As used herein, the term "native" refers to a polynucleotide or polypeptide that is naturally present in a host cell.

[0051] As used herein, the term "naturally occurring" refers to something found in nature (e.g., a protein, amino acid, or nucleic acid sequence). In contrast, the term "non-naturally occurring" refers to something not found in nature (e.g., recombinant nucleic acid and protein sequences produced in the laboratory, modifications of wild-type sequences, formulations containing one or more synthetic components, formulations containing artificial combinations of other naturally occurring components).

[0052] As used herein, the term "non-aqueous" refers to a composition containing less than trace amounts of water (i.e., 0.5% by weight or less water based on the total weight of the composition).

[0053] As used herein, the term "nutrient" refers to a compound or element useful for providing nutrients to a plant (e.g., vitamins, macronutrients, micronutrients, trace elements, organic acids, etc., that are necessary for plant growth and / or development).

[0054] As used herein, when the term "obtained from" is used in reference to the relationship between an organism and a protein, it means that the protein is expressed in the organism, whether it is derived from a polynucleotide naturally present therein or from a heterologous polynucleotide introduced into the organism.

[0055] As used herein, the term "polynucleotide" includes DNA, RNA, heteroduplexes, and synthetic molecules that can encode polypeptides. The polynucleotide may be single-stranded or double-stranded and may contain chemical modifications. The terms "nucleic acid" and "polynucleotide" are used interchangeably. Since the genetic code is degenerate, two or more codons can be used to encode a particular amino acid, and the present compositions and methods include nucleotide sequences that encode a particular amino acid sequence. Unless otherwise specified, nucleic acid sequences are shown in the 5' to 3' direction.

[0056] As used herein, the term "nucleic acid construct" refers to a polynucleotide, either single-stranded or double-stranded, that is isolated from a naturally occurring gene, or modified to contain segments of nucleic acids in a manner that does not normally occur in nature, or is synthetic, and contains one or more control sequences operably linked to a nucleic acid sequence.

[0057] As used herein, the term "operably linked" means that the designated components are in a relationship (including, but not limited to, juxtaposition) that enables them to function in the intended manner. For example, a regulatory sequence is operably linked to a coding sequence if the expression of the coding sequence is under the control of the regulatory sequence.

[0058] As used herein, the term "phosphate solubilizing microorganism" refers to a microorganism capable of converting insoluble phosphate into a soluble form of phosphate.

[0059] As used herein, the term "phytopathogenic pest" includes, but is not limited to, any organism or virus that has an adverse effect on plants, including organisms and viruses that spread disease, damage host plants, and / or compete for soil nutrients. The term "phytopathogenic pest" encompasses organisms or viruses that are associated with plants and are known to cause harmful effects on the health and / or vitality of plants. Phytopathogenic 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., aphids, thrips, beetles, 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.).

[0060] As used herein, the term "plant" includes, but is not limited to, all plant groups including agricultural, floricultural, horticultural, and forestry plants. The term "plant" encompasses plants obtained by genetic recombination, including plants obtained by conventional plant breeding and optimization methods (e.g., marker-assisted selection), and cultivars that may or may not be protectable by plant breeder's rights.

[0061] As used herein, the term "plant cell" refers to cells of intact plants, cells taken from plants, or cells derived from cells taken from plants. Thus, the term "plant cell" includes cells within seeds, suspension cultures, embryos, meristematic regions, callus tissue, leaves, shoots, gametophytes, sporophytes, pollen, and microspores.

[0062] As used herein, the term "plant growth regulator" refers to an agent or combination of agents that, through its direct physiological action on plants, accelerates or delays the growth / maturation rate of plants or, in other cases, changes the behavior of plants through its direct physiological action on plants. "Plant growth regulator" should not be construed to include any agent or combination of agents that is excluded from the definition of "plant regulator" set forth in section 2(v) of the Federal Insecticide, Fungicide, and Rodenticide Act (7 U.S.C. § 136(v)). Thus, "plant growth regulator" does not include microorganisms applied to plants, plant parts, or the plant growth environment for the purpose of enhancing the availability and / or uptake of nutrients, nutrients necessary for normal plant growth, or soil amendments applied for the purpose of improving soil properties favorable for plant growth or vitamin hormone products as defined by 40 C.F.R. § 152.6(f).

[0063] As used herein, the term "plant part" refers to any part of a plant, including cells and tissues derived from the plant. Thus, the term "plant part" can refer to any of a plant component or organ (e.g., leaf, 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, leaves, ovules, pollen, rhizomes, roots, seeds, shoots, stems, and tubers, as well as young branches, rootstocks, protoplasts, callus, etc.

[0064] As used herein, the term "plant propagule" refers to a plant part from which an entire plant can be generated. Examples of plant propagules include, but are not limited to, cuttings of plants (e.g., leaves, stems), rhizomes, seeds, tubers, and cells / tissues that can be cultivated into an entire plant.

[0065] As used herein, the term "protein" does not mean to refer to a specific amino acid chain length and includes peptides, oligopeptides, and polypeptides. It should be understood that the term "protein" also includes two or more polypeptides combined to form an encoded product, as well as hybrid polypeptides and fusion proteins.

[0066] As used herein, the term "purified" refers to a polynucleotide, protein, or cell that is substantially free of other components as determined by analytical techniques well known in the art (e.g., a purified polynucleotide or protein can form distinct bands in an electrophoretic gel, a chromatographic eluate, and / or a medium subjected to density gradient ultracentrifugation). A purified polynucleotide or protein is at least about 50% pure and is usually 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., by weight or molar concentration percent). In a related sense, a composition is concentrated with respect to a molecule if there is a substantial increase in the concentration of the molecule after application of purification or concentration techniques. The term "concentrated" refers to a compound, polynucleotide, protein, cell, nucleic acid, amino acid, or other designated material or component present in a composition at a higher relative or absolute concentration compared to the starting composition.

[0067] In one aspect, as used herein, the term "purified" refers to a protein or cell that is essentially free of components derived from the production organism (in particular, insoluble components). In other aspects, the term "purified" refers to a protein that is essentially free of insoluble components (in particular, insoluble components) derived from the natural organism from which the protein is obtained. In one aspect, the protein is separated from a portion of the soluble components of the organism and the culture medium in which the protein is recovered. The protein can be purified (i.e., separated) by one or more of the unit operations of filtration, precipitation, or chromatography.

[0068] Accordingly, the protein can be purified such that other proteins present (specifically, other proteins) are present in only trace amounts. The term "purified," as used herein, can refer to the removal of other components present in the cells of origin of the protein (specifically, other proteins, most specifically other enzymes). The protein can be "substantially pure," i.e., it can contain no other components derived from the organism that produces the protein (e.g., the host organism in the case of a recombinantly produced protein). In one aspect, the protein is at least 40% pure by weight of the total protein material present in the preparation. In one aspect, the protein is at least 50%, 60%, 70%, 80%, or 90% pure by weight of the total protein material present in the preparation. As used herein, a "substantially pure protein" can mean a protein preparation that contains, 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 other protein material that the protein is naturally or recombinantly associated with.

[0069] Accordingly, a substantially pure protein is preferably at least 92% pure by weight of the total protein material present in the preparation, 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, and most preferably at least 99.5% pure. The proteins of the present disclosure are preferably in substantially pure form (i.e., the preparation is essentially free of other protein materials). This can be achieved, for example, by preparing the protein by well-known recombinant methods or classical purification methods.

[0070] As used herein, the term "recombinant" is used in its conventional sense to refer to the manipulation of nucleic acid sequences, such as cleavage and recombination, to form a constellation different from that found in nature. The term recombinant refers to a cell, nucleic acid, protein, or vector that has been modified from its natural state. Thus, for example, a recombinant cell expresses a gene not found within the natural (non-recombinant) form of the cell, or expresses a native gene at a different level or under different conditions than found in nature. The term "recombinant" is synonymous with "genetically modified" and "transgenic".

[0071] As used herein, the terms "recover" and "recovery" refer to the extraction of a protein from at least one fermentation broth component selected from a list of cells, nucleic acids, or other specific materials, e.g., the recovery of a protein from the whole fermentation broth or from a cell-free fermentation broth, by polypeptide crystal collection, by filtration, e.g., depth filtration (using a filter aid or packed filter media, chamber filter cloth filtration, rotary drum filtration, drum filtration, rotary vacuum drum filter, candle filter, horizontal leaf filter or the like, using seed or pad filtration in a framed or modular setting), or membrane filtration (using sheet filtration, module filtration, candle filtration, microfiltration, ultrafiltration in any of crossflow, dynamic crossflow or dead-end operation), or by centrifugation (using a decanter centrifuge, disc centrifuge, liquid cyclone or the like), or by precipitating the protein and using an appropriate solid-liquid separation method and using classification separation by particle size to collect the protein from the broth medium. Recovery encompasses the isolation and / or purification of the protein.

[0072] As used herein, the relatedness between two amino acid sequences or between two nucleotide sequences is represented by the parameter "sequence identity".

[0073] For the purposes of the present disclosure, sequence identity between two amino acid sequences is determined as the output of "maximum identity" using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277) (preferably version 6.6.0 or later). The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The -nobrief option must be specified on the command line in order for the Needle program to report the longest identity. The output of Needle labeled "longest identity" is calculated as follows: (Number of identical residues × 100) / (Length of alignment - Total number of gaps in alignment).

[0074] For the purposes of the present disclosure, sequence identity between two polynucleotide sequences is preferably determined as the output of "longest identity" using the Needleman-Bunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS; The European Molecular Biology Open Software Suite, Rice et al., 2000, supra) (version 6.6.0 or later). The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The nobrief option must be specified on the command line so that the Needle program reports the longest identity. The output of Needle labeled "longest identity" is calculated as follows: (Same deoxyribonucleotide × 100) / (Length of alignment - Total number of gaps in the alignment).

[0075] As used herein, the term "signal peptide" refers to the sequence of amino acids attached to the N-terminal portion of a protein, which promotes the secretion of the protein outside the cell. The mature form of an extracellular protein lacks the signal peptide, which is cleaved during the secretion process.

[0076] As used herein, the terms "stabilizing compound" and "stabilizer" refer to an agent or combination of agents, the application of which enhances the stability of an enzyme.

[0077] As used herein, the term "subsequence" refers to a polynucleotide having one or more proteins missing at the 5' end and / or 3' end of the mature protein coding sequence, and the subsequence encodes a fragment having enzyme activity.

[0078] As used herein, the term "variant" refers to a protein that contains artificial mutations (i.e., substitutions, insertions (including extensions), and / or deletions (e.g., truncations)) at one or more positions. Substitution means replacement of an amino acid occupying a position with a different amino acid; deletion means removal of the amino acid occupying a position; insertion means addition of 1 to 5 amino acids (e.g., 1 to 3 amino acids, particularly 1 amino acid) adjacent to and immediately following the amino acid occupying a position.

[0079] As used herein, the term "wild-type" with respect to an amino acid sequence or nucleic acid sequence means that the amino acid sequence or nucleic acid sequence is a natural or naturally occurring sequence.

[0080] Hereinafter, some aspects of the present disclosure will be described with respect to its embodiments, but it will be understood by those skilled in the art that various modifications of form and detail can be made without departing from the spirit and scope of the present disclosure as defined by the claims.

[0081] All publications, patent applications, patents, and other references cited herein are hereby incorporated by reference in their entirety, unless they conflict with the disclosure explicitly described herein.

[0082] The present disclosure provides a protein useful for: a) preventing, treating, suppressing, and / or eliminating infestation and / or infection by a variety of pests, including but not limited to phytopathogenic pests such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses, and weeds; b) treating surfaces / substances susceptible to infestation / infection; c) cleaning infested / infected surfaces / substances; d) reducing disease severity in plants and plant parts affected directly or indirectly by phytopathogenic pests; e) enhancing the plant growth environment; f) improving nutrient availability in the plant growth environment; g) reducing the amount of exogenous chemical fertilizers required to achieve desired results; h) improving plant growth, development, and yield characteristics; i) extending the storage life of harvested plants and plant parts; j) delaying the ripening of plants and plant parts; k) promoting the ripening of plants and plant parts; l) improving the efficacy of biological / chemical pesticides; m) preventing, treating, suppressing, and / or eliminating pesticide-induced tolerance / phytotoxicity, and polynucleotides encoding such proteins, organisms expressing such proteins, formulations containing such proteins, polynucleotides, and organisms, and methods of using such proteins, polynucleotides, organisms, and formulations in agriculture and other fields of endeavor.

[0083] Those skilled in the art will understand that the proteins, polynucleotides and organisms of the present disclosure may be used (and may be formulated for use) at any point throughout agricultural, floricultural, horticultural and forestry processes, such as before planting, at the time of planting, after planting, before germination, at the time of germination, after germination, before seedling emergence, at the time of seedling emergence, after seedling 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 the time of flowering, after flowering, before fruiting, at the time of fruiting, after fruiting, before ripening, at the time of ripening, after ripening, before harvest, at the time of harvest, after harvest, before transport / storage, at the time of transport / storage and / or after transport / storage. Accordingly, the proteins of the present disclosure may be formulated for any suitable application method, including but not limited to on-seed application, inter-row application, foliar application, pre-harvest application and post-harvest application.

[0084] As will be further understood by those skilled in the art, the proteins, polynucleotides, organisms and formulations of the present disclosure can affect the desired results, including the prevention, treatment, suppression and / or elimination of parasitism / infection, without being toxic. As will be explained in more detail below, the compositions of the present disclosure can exert their effects through various non-lethal means, such as reducing the attraction of pests to the treated surface by decomposing a food source. In addition, in many cases, other toxic proteins of the present disclosure can be used at non-lethal doses to enhance the effectiveness of various chemical and biological pesticides and / or to expand the range of their target pests.

[0085] Finally, those skilled in the art will understand that the proteins, polynucleotides, organisms and formulations of the present disclosure can be used in combination to achieve the desired results. The present disclosure thus extends to formulations containing two or more proteins of the present disclosure, hybrid proteins containing two or more distinct catalytic domains, fusion proteins containing two or more enzyme polypeptides, and the like. Although certain combinations are described in detail below, the present disclosure is not limited to these combinations, but should be understood to extend to all possible combinations of the proteins, formulations, polynucleotides and organisms described herein.

[0086] In some embodiments, the proteins of the present disclosure exhibit one or more catalytic activities belonging to Enzyme Classification Number 1 (EC1). For example, in some embodiments, the proteins of the present disclosure are capable of a) preventing / treating / suppressing / eliminating / reducing the harmful effects of parasitism / infection by various pests including, but not limited to, phytopathogenic pests such as spider mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses, and weeds; b) reducing one or more aspects of disease severity in plants infested with one or more phytopathogenic pests; c) pretreating surfaces / substances susceptible to parasitism / infection by pests; d) cleaning surfaces / substances parasitized / infested by pests; e) enhancing the environment in which plants grow; f) improving nutrient availability in the plant growth environment; g) reducing the amount of exogenous chemical fertilizers required to obtain a desired result; h) improving the growth, development, and yield characteristics of plants; i) extending the storage life of harvested plants and plant parts; j) delaying / promoting the maturation of plants or plant parts; k) improving the efficacy of chemical pesticides and / or reducing the tolerance / plant toxicity of resistance induced by chemical pesticides, and are useful for exhibiting glucose oxidase, cellobiose dehydrogenase, amino acid oxidase, laccase, catalase, peroxidase, and / or oxygenase activity.

[0087] In some embodiments, the proteins of the present disclosure exhibit one or more oxidoreductase activities belonging to EC1 and optionally comprise, consist essentially of, or consist of an amino acid sequence having an identity 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% with one or more of the amino acid sequences described herein as SEQ ID NOs: 1-15 and 183-2755.

[0088] In some embodiments, the protein of the present disclosure exhibits one or more oxidoreductase activities belonging to EC1.1, such as oxidase activities belonging to EC1.1.3 (for example, glucose oxidase activity belonging to EC1.1.3.4, hexose oxidase activity belonging to EC3.1.1.5, galactose oxidase activity belonging to EC1.1.3.9) and / or EC1.1.99 (for example, cellobiose oxidase activity belonging to EC1.1.99.18), and optionally comprises, consists essentially of, or consists of an amino 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% identity to one, two, three, four, five or more of the amino acid sequences described herein as SEQ ID NOs: 1-8.

[0089] In some embodiments, the protein is 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; 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; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with one or more of SEQ ID NOs: 92-96 and their cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 1-5 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide has glucose oxidase activity belonging to EC 1.1.3.4 and is selected from the group consisting of fragments. Examples of proteins having glucose oxidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 1-5 are described herein as SEQ ID NOs: 183-2205.

[0090] In some such embodiments, the protein is derived from the genus Aspergillus (e.g., A. chevalieri, A. cristatus, A. flavus, A. niger, A. niveoglaucus, A. nomiae, A. oryzae, A. terreus, A. tubingensis), the genus Beauveria (e.g., B. bassiana), the genus Escherichia (e.g., E. coli), the genus Komagataella (e.g., K. pastoris), the genus Penicillium (e.g., P. adametzii, P. amagasakiense, P. chrysogenum, P. decumbens, P. expansum, P. polonicum, P. viridicatum) or the genus Talaromyces (e.g., T. bacillisporus, T. flavus, T. stipitatus, T. variabilis). For example, in some embodiments, the protein is a natural genus Aspergillus (e.g., A. chevalieri, A. cristatus, A. flavus, A. niger, A. niveoglaucus, A. nomiae, A. oryzae, A. terreus, A. tubingensis), the genus Beauveria (e.g., B. bassiana), the genus 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) glucose oxidase, or a natural 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.a functional fragment / mutant / variant of glucose oxidase from T. stipitatus or T. variabilis).

[0091] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 6-8; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 6-8; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 97-99 and their cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 6-8 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), The polypeptide is selected from the group consisting of fragments having cellobiose oxidase activity belonging to EC 1.1.99.18. Examples of proteins having an amino acid sequence that exhibits cellobiose oxidase activity and is at least 70% identical to one or more of SEQ ID NOs: 6 to 8 are described herein as SEQ ID NOs: 2206 to 2217.

[0092] In some such embodiments, the protein is derived from the genus Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora or Remersonia. For example, in some embodiments, the protein is a natural Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora or Remersonia, or a functional fragment / mutant / variant of cellobiose oxidase of natural Chaetomium, Humicola, Microdochium, Myceliophthora, Myriococcum, Neurospora or Remersonia.

[0093] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more oxidoreductase activities belonging to EC 1.1. For example, Chinese Patent No. 101348794A; No. 101348795A; No. 102517304A; No. 103275942A; No. 103525778A; No. 103614350A; No. 103981159A; No. 104312989A; No. 104711273A; No. 104711274A; No. 105002147A; No. 105420252A; No. 105746635A; No. 105950577A; No. 105950578A; No. 106119219A; No. 107012130A; No. 107988177A; No. 108003244A; No. 108004256A; No. 108118036A; No. 108118037A; No. 108118038A; No. 108251389A; No. 108251390A; No. 108251391A; No. 108251392A; No. 108374001A; No. 108893453A; No. 109207446A; No. 109321586A; No. 109423483A; No. 109666657A; No. 110577939A; No. 110592034A; No. 110628738A; No. 110885801A; No. 111004786A; No. 112143717A; No. 112760299A; No. 112877306A; No. 113061189A; No. 113403290A; No. 113528476A; No. 113862233A; No. 114058637A; No. 114181916A; No. 114395540A; No. 114395541A; No. 114736879A; No. 114736880A; No. 114736881A; No. 115029327A;Refer to Japanese Patent No. 115029328A; Japanese Patent No. 115612628A; Japanese Patent No. 1229139A; European Patent No. 1892529A1; Japanese Patent No. 2415863A1; Japanese Patent No. 2562250A1; Japanese Patent No. 2796547A1; Japanese Patent No. 3572503A1; Japanese Patent No. 3984368A1; French Patent No. 2979918A1; Japanese Unexamined Patent Application Publication No. 2011139677; Japanese Unexamined Patent Application Publication No. 2012157315; Japanese Unexamined Patent Application Publication No. 2015002686; Japanese Unexamined Patent Application Publication No. 2018198581; US Patent No. 10233430B1; US Patent Application Publication No. 2004053425A1; US Patent Application Publication No. 2022283151A1; International Publication No. 2010039840A1 Pamphlet; International Publication No. 2010053161A1 Pamphlet; International Publication No. 2010121933A1 Pamphlet; International Publication No. 2010135499A1 Pamphlet; International Publication No. 2011068050A1 Pamphlet; International Publication No. 2012068236A2 Pamphlet; International Publication No. 2013026575A2 Pamphlet; International Publication No. 2013159005A2 Pamphlet; International Publication No. 2013181760A1 Pamphlet; International Publication No. 2014000746A1 Pamphlet; International Publication No. 2014013073A1 Pamphlet; International Publication No. 2014081700A1 Pamphlet; International Publication No. 2014114810A1 Pamphlet; Japanese Unexamined Patent Application Publication No. 2014173822; International Publication No. 2015109405A1 Pamphlet; International Publication No. 2016026842A1 Pamphlet; International Publication No. 2016031611A1 Pamphlet; International Publication No. 2016090472A1 Pamphlet; International Publication No. 2016090473A1 Pamphlet; International Publication No. 2016050905A1 Pamphlet; International Publication No. 2018039802A1 Pamphlet; International Publication No. 2019110497A1 Pamphlet; International Publication No. 2020125700A1 Pamphlet; International Publication No. 2020239064A1 Pamphlet; International Publication No. 2020254336A1 Pamphlet; International Publication No. 2022138668A1 Pamphlet; International Publication No. 2022256274A1 Pamphlet; International Publication No. 2023004432A2 Pamphlet; International Publication No. 2023288294A1 Pamphlet; Japanese Patent No. 8912675A; Japanese Patent No. 9521924A1.;

[0094] In some embodiments, the protein of the present disclosure exhibits one or more oxidoreductase activities belonging to EC1.4, such as D-aspartate oxidase activity belonging to EC1.4.3 (e.g., EC1.4.3.1), L-amino acid oxidase activity belonging to EC1.4.3.2, D-amino acid oxidase activity belonging to EC1.4.3.3, D-glutamate oxidase activity belonging to EC1.4.3.7, L-glutamate oxidase activity belonging to EC1.4.3.11, cyclohexylamine oxidase activity belonging to EC1.4.3.12, protein-lysine-6-oxidase activity belonging to EC1.4.3.13, L-lysine-oxidase activity belonging to EC1.4.3.14, D-glutamate (D-aspartate) oxidase activity belonging to EC1.4.3.15, L-aspartate oxidase activity belonging to EC1.4.3.16, glycine oxidase activity belonging to EC1.4.3.19, L-lysine-6-oxidase activity belonging to EC1.4.3.20, L-arginine oxidase activity belonging to EC1.4.3.25, etc.

[0095] In some embodiments, the protein of the present disclosure exhibits one or more oxidase activities belonging to EC1.10, such as laccase activity belonging to EC1.10.3 (e.g., EC1.10.3.2), and optionally, comprises, consists essentially of, or consists of an amino 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% identity to the amino acid sequence described herein as SEQ ID NO: 9.

[0096] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 9; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 9; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 100 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 9 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 9 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein The polypeptide is selected from the group consisting of fragments having laccase activity belonging to EC 1.10.3.2. Examples of proteins having an amino acid sequence that exhibits laccase activity and is at least 70% identical to SEQ ID NO: 9 are described herein as SEQ ID NOs: 2218 to 2251.

[0097] In some such embodiments, the protein is derived from the genus Chaetomium, Chrysocorona, Melanocarpus, Myceliophthoora, Myriococcum or Thermothelomyces. For example, in some embodiments, the protein is a native Chaetomium, Chrysocorona, Melanocarpus, Myceliophthoora, Myriococcum or Thermothelomyces laccase, or a functional fragment / mutant / variant of a native Chaetomium, Chrysocorona, Melanocarpus, Myceliophthoora, Myriococcum or Thermothelomyces laccase.

[0098] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more oxidase activities belonging to EC 1.10. See, for example, European Patent No. 3444323A1; Indian Patent No. 9601521I4; US Patent Application Publication No. 2008 / 148432A1; No. 2009 / 155415A1; No. 2012 / 227131A1; No. 2022 / 298533A1; US Patent No. 6060442A1; International Publication No. 2009 / 075860A2; No. 2012 / 068236A2; No. 2013 / 181760A1; No. 2014 / 081700A1; No. 2015 / 109405A1; No. 2016 / 029107A1; No. 2016 / 090059A1; No. 2016 / 090474A1; No. 2017 / 089304A1; No. 2022 / 029293A1; No. 2022 / 270590A1; No. 2023 / 288294A1; No. 9838286A1.

[0099] 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, 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 described herein as SEQ ID NOs: 10-13.

[0100] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 10-12; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 10-12; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 101-103 or the cDNA sequence thereof; d) a polypeptide derived from any one of SEQ ID NOs: 10-12 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide is selected from the group consisting of fragments having catalase activity belonging to EC 1.11.1.6. Examples of proteins having an amino acid sequence that exhibits catalase activity and is at least 70% identical to one or more of SEQ ID NOs: 10 to 12 are described herein as SEQ ID NOs: 2252 to 2296.

[0101] In some such embodiments, the protein is derived from the genus 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.

[0102] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 13; b) A polypeptide having at least 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 with any one of the mature polypeptides of SEQ ID NO: 13; c) A polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 104 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 13 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 13 by substitution, deletion or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide has peroxidase activity belonging to EC 1.11.1.7 and is selected from the group consisting of fragments. Examples of proteins having peroxidase activity and having an amino acid sequence that is at least 70% identical to SEQ ID NO: 13 are described herein as SEQ ID NOs: 2297 to 2381.

[0103] In some such embodiments, the protein is derived from the genus Arthromyces or Coprinopsis. For example, in some embodiments, the protein is a native Arthromyces or Coprinopsis peroxidase, or a functional fragment / mutant / variant peroxidase of native Arthromyces or Coprinopsis peroxidase.

[0104] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more peroxidase activities belonging to EC 1.11. For example, refer to the specifications of Chinese Patent No. 105441400-A; No. 108070574-A; No. 112522227-A; European Patent No. 2295582A2; No. 486067A2; Japanese Patent Laid-Open No. 2007143405A; No. 2010044058A; Korean Patent No. 2011013726A; US Patent Application Publication No. 2005108791A1; No. 2007118916A1; No. 2008148432A1; No. 2013074202A1; No. 2020306342A1; International Publication No. 2004108765A2 pamphlet; No. 2006114616A1 pamphlet; No. 2007020428A1 pamphlet; No. 2007044043A2 pamphlet; No. 2009104622A1 pamphlet; No. 2010027755A1 pamphlet; No. 2011068297A1 pamphlet; No. 2012068236A2 pamphlet; No. 2012072777A1 pamphlet; No. 2012130120A1 pamphlet; No. 2013091547A1 pamphlet; No. 2014018368A2 pamphlet; No. 2014081700A1 pamphlet; No. 2014202616A2 pamphlet; No. 2015048332A2 pamphlet; No. 2015182941A1 pamphlet; No. 2017040907A1 pamphlet; No. 2018089391A1 pamphlet; No. 2020200321A1 pamphlet; No. 2020200322A1 pamphlet; No. 2022074170A1 pamphlet; No. 2022251056A1 pamphlet; No. 2023002065A2 pamphlet; No. 2023019266A2 pamphlet; No. 9317721A1 pamphlet; No. 9318166A2 pamphlet; No. 9510602A1 pamphlet; No. 9515391A2 pamphlet; No. 9810060A1 pamphlet; No. 9835026A1 pamphlet.

[0105] In some embodiments, the protein of the present disclosure exhibits one or more oxygenase activities belonging to EC1.14, such as oxygenase activities belonging to EC1.14.16 (for example, phenylalanine 4-monooxygenase activity belonging to EC.1.14.16.1, tyrosine 3-monooxygenase activity belonging to EC1.14.16.2, tryptophan 5-monooxygenase activity belonging to EC1.14.16.4, phenylalanine 3-monooxygenase activity belonging to EC1.14.16.7), EC1.14.18 (for example, tyrosinase activity belonging to EC1.14.18.1), and / or EC1.14.99 (for example, soluble chitin monooxygenase activity belonging to EC1.14.99.53, soluble cellulose monooxygenase activity belonging to EC1.14.99.54, soluble starch monooxygenase activity belonging to EC1.14.99.55, soluble cellulose monooxygenase activity belonging to EC1.14.99.56, soluble cellulose monooxygenase activity belonging to EC1.14.99.56), and optionally, has an identity 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% with one or more of the amino acid sequences described herein as SEQ ID NOs: 14-15, and comprises, consists essentially of, or consists of an amino acid sequence having such identity.

[0106] In some embodiments, the protein is a) a polypeptide having at least 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 with one or more of SEQ ID NOs: 14-15; b) a polypeptide having at least 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 with the mature polypeptide of any one of SEQ ID NOs: 14-15; c) a polypeptide encoded by a polynucleotide having at least 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 with one or more of SEQ ID NOs: 105-106 or the cDNA sequence thereof; d) a polypeptide derived from any one of SEQ ID NOs: 14-15 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a)-f), wherein The polypeptide is selected from the group consisting of fragments having soluble cellulose monooxygenase activity belonging to EC 1.14.99.56. Examples of proteins having an amino acid sequence that exhibits soluble cellulose monooxygenase activity and is at least 70% identical to one or more of SEQ ID NOs: 14-15 are described herein as SEQ ID NOs: 2382-2755.

[0107] In some such embodiments, the protein is derived from the genus Penicillium, the genus Rasamsonia, or the genus Thermoascus. For example, in some embodiments, the protein is a native Penicillium, Rasamsonia, or Thermoascus monooxygenase, or a functional fragment / mutant / variant of a native Penicillium, Rasamsonia, or Thermoascus monooxygenase.

[0108] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more oxygenase activities belonging to EC 1.14. For example, Chinese Patent No. 103232949A1; No. 103255072A; No. 106544329A; No. 109554355A; No. 110093326A; Japanese Patent Application Laid-Open No. 2016039821A; US Patent Application Publication No. 2008299613A1; No. 2011099671A1; No. 2014075603A1; No. 2018019412A1; No. 2019153414A1; International Publication No. 2011080267A2 Pamphlet; International Publication No. 2011121768A1 Pamphlet; International Publication No. 2011153516A2 Pamphlet; International Publication No. 2012000892A1 Pamphlet; International Publication No. 2012021394A1 Pamphlet; International Publication No. 2012021395A1 Pamphlet; International Publication No. 2012044835A1 Pamphlet; International Publication No. 2012044836A1 Pamphlet; International Publication No. 2012068509A1 Pamphlet; International Publication No. 2012089023A1 Pamphlet; International Publication No. 2013028915A2 Pamphlet; International Publication No. 2013036898A2 Pamphlet; International Publication No. 2013110242A1 Pamphlet; International Publication No. 2013119302A2 Pamphlet; International Publication No. 2014085251A1 Pamphlet; International Publication No. 2014093835A1 Pamphlet; International Publication No. 2014138983A1 Pamphlet; International Publication No. 2014140165A1 Pamphlet; International Publication No. 2014202616A2 Pamphlet; International Publication No. 2014202711A1 Pamphlet; International Publication No. 2015105835A1 Pamphlet; International Publication No. 2015187935A1 Pamphlet; International Publication No. 2016045569A1 Pamphlet; International Publication No. 2016090473A1 Pamphlet; International Publication No. 2016145358A1 Pamphlet; International Publication No. 2017070219A1 Pamphlet; International Publication No. 2018019948A1 Pamphlet; International Publication No. 2018106656A1 Pamphlet;Please refer to International Publication No. WO 2018 / 142002 A1; International Publication No. WO 2019 / 005755 A1; International Publication No. WO 2019 / 083831 A1; International Publication No. WO 2019 / 229228 A1;

[0109] In some embodiments, the proteins of the present disclosure exhibit one or more catalytic activities belonging to Enzyme Classification Number 2 (EC2). For example, in some embodiments, the proteins of the present disclosure are capable of: a) preventing / treating / suppressing / eliminating / reducing the deleterious effects of parasitism / infection by various pests, including but not limited to phytopathogenic pests such as mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses, and weeds; b) reducing one or more aspects of disease severity in plants infested with one or more phytopathogenic pests; c) pretreating surfaces / substances susceptible to parasitism / infection by pests; d) cleaning surfaces / substances parasitized / infected by pests; e) enhancing the environment in which plants grow; f) improving nutrient availability in the plant growth environment; g) reducing the amount of exogenous chemical fertilizers required to obtain a desired result; h) improving the growth, development, and yield characteristics of plants; 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 reducing the tolerance / phytotoxicity induced by chemical pesticides.

[0110] In some embodiments, the protein of the present disclosure exhibits one or more transferase activities belonging to EC2 and, optionally, has an amino acid sequence identity 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% with one or more of the amino acid sequences described herein as SEQ ID NO: 16 and 2756 - 2769, and includes, consists essentially of, or consists of such amino acid sequences.

[0111] In some embodiments, the protein of the present disclosure exhibits one or more acyltransferase activities belonging to EC2.3, such as aminoacyltransferase activities belonging to EC2.3.2 (for example, D - glutamyltransferase activity belonging to EC2.3.2.1, gamma - glutamyltransferase activity belonging to EC2.3.2.2, aspartyltransferase activity belonging to EC2.3.2.7, protein - glutamine - gamma - glutamyltransferase activity belonging to EC2.3.2.13, D - alanine gamma - glutamyltransferase activity belonging to EC2.3.2.14), and, optionally, has an amino acid sequence identity 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% with one or more of the amino acid sequences described herein as SEQ ID NO: 16, and includes, consists essentially of, or consists of such amino acid sequences.

[0112] In some embodiments, the protein is a) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 16; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NO: 16; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 107 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 16 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having gamma-glutamyltransferase activity belonging to EC 2.3.2.2. Examples of proteins having an amino acid sequence that exhibits gamma-glutamyltransferase activity and is at least 70% identical to SEQ ID NO: 16 are described herein as SEQ ID NOs: 2756-2769.

[0113] In some such embodiments, the protein is derived from Bacillus. For example, in some embodiments, the protein is a native Bacillus gamma-glutamyltransferase or a fragment / mutant / variant of a native Bacillus gamma-glutamyltransferase.

[0114] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more acyltransferase activities belonging to EC 2.3. See, for example, Chinese Patent No. 107828754A; No. 108611333A; No. 108929866A; No. 112111468A; No. 114806988A; European Patent No. 441353A; Republic of Korea Patent No. 1814024B1; International Publication No. 2003087149A2; No. 2005075652A1; No. 2014081884A1; No. 2015048332A2; No. 2018234382A1.

[0115] In some embodiments, the proteins of the present disclosure exhibit one or more catalytic activities belonging to Enzyme Classification Number 3 (EC3). For example, in some embodiments, the proteins of the present disclosure are useful for: a) preventing / treating / suppressing / eliminating / reducing the harmful effects of parasitism / infection by various pests including, but not limited to, phytopathogenic pests such as spider mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses, and weeds; b) reducing one or more aspects of disease severity in plants infested with one or more phytopathogenic pests; c) pretreating surfaces / substances susceptible to parasitism / infection by pests; d) cleaning surfaces / substances parasitized / infected by pests; e) enhancing the environment in which plants grow; f) improving nutrient availability in the plant growth environment; g) reducing the amount of exogenous chemical fertilizers required to obtain a desired result; h) improving the growth, development, and yield characteristics of plants; i) extending the storage life of harvested plants and plant parts; j) delaying / promoting the maturation of plants or plant parts; k) improving the efficacy of chemical pesticides and / or reducing the resistance / phytoxicity induced by chemical pesticides. The proteins may exhibit lipase, triacylglycerol lipase, pectin esterase, phospholipase, lysophospholipase, cutinase, amylase, glucosidase, galactosidase, cellulase, glucanase, xylanase, ceramidase, dextranase, chitinase, chitosanase, galacturonase, fucosidase, lysozyme, xylosidase, rhamnosidase, pullulanase, mannosidase, amidase, aminidase, maltohydrolase, cellobiosidase, pectinase, mannanase, aminopeptidase, serine peptidase, and / or metallopeptidase, asparaginase and / or glutaminase activity.

[0116] In some embodiments, the protein of the present disclosure exhibits esterase activity belonging to EC3 and, optionally, has 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 described herein as SEQ ID NOs: 17-90 and 2770-72141, or consists essentially of or consists of these amino acid sequences.

[0117] In some embodiments, the protein of the present disclosure has one or more esterase activities belonging to EC3.1, such as lipase activity belonging to EC3.1.1 (for example, triacylglycerol lipase activity belonging to EC3.1.1.3, phospholipase A2 activity belonging to EC3.1.1.4, lysophospholipase activity belonging to 3.1.1.5, pectin esterase activity belonging to 3.1.1.11, phospholipase A1 activity belonging to 3.1.1.32, lipoprotein lipase activity belonging to EC3.1.1.34, cutinase activity belonging to 3.1.1.74), phosphatase activity belonging to EC3.1.3 (for example, alkaline phosphatase activity belonging to EC3.1.3.1, acid phosphatase activity belonging to EC3.1.3.2, 3-phytase activity belonging to EC3.1.3.8, glucose-6-phosphatase activity belonging to EC3.1.3.9, glucose-1-phosphatase activity belonging to EC3.1.3.10, fructose-bisphosphatase activity belonging to EC3.1.3.11, sugar-phosphatase activity belonging to EC3.1.3.23, 4-phytase activity belonging to EC3.1.3.26, fructose-2,6-bisphosphate 2-phosphatase activity belonging to EC3.1.3.46, fructose-2,6-bisphosphate 6-phosphatase activity belonging to EC3.1.3.54, 5-phytase activity belonging to EC3.1.3.72, lipid-phosphate phosphatase activity belonging to EC3.1.3.76), and / or hydrolase activity belonging to EC3.1.4 (for example, phospholipase C activity belonging to 3.1.4.3, phospholipase D activity belonging to EC3.1.4.4, 3.1.4.exhibits phosphatidylinositol phospholipase C activity belonging to 11, and optionally comprises, consists essentially of, or consists of an amino acid sequence having an identity 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% with one or more of the amino acid sequences described herein as SEQ ID NOs: 17-33, 72147 and 72149.

[0118] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NOs: 17-22; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NOs: 17-22; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 108-113 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 17-22 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide has triacylglycerol lipase activity belonging to EC 3.1.1.3 and is selected from the group consisting of fragments. Examples of proteins having triacylglycerol lipase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 17-22 are described herein as SEQ ID NOs: 2778-10223.

[0119] 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 natural protein that is an Aspergillus, Bacillus, Cryphonectria, Fusarium, Haloquadratum, Humicola, Penicillium, Scytalidium, Talaromyces, Thermomyces or Thermus triacylglycerol lipase, or a fragment / mutant / variant of a natural Aspergillus, Bacillus, Cryphonectria, Fusarium, Haloquadratum, Humicola, Penicillium, Scytalidium, Talaromyces, Thermomyces or Thermus triacylglycerol lipase.

[0120] In some embodiments, the protein is, a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 23; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 23; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 114 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 23 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 23 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having triacylglycerol lipase activity belonging to EC3.1.1.3 and / or phospholipase A1 activity belonging to EC3.1.1.32. Examples of proteins having triacylglycerol lipase activity and / or phospholipase A1 activity and having an amino acid sequence that is at least 70% identical to SEQ ID NO: 23 are described herein as SEQ ID NOs: 10243 to 15978.

[0121] In some embodiments, the protein is derived from the genus 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.

[0122] 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 phospholipase A1, or a fragment / mutant / variant of a native Aspergillus, Bacillus, Fusarium, Struthio, Talaromyces or Thermomyces phospholipase A1.

[0123] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 24; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NO: 24; 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 with SEQ ID NO: 115 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 24 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide has lysophospholipase activity belonging to EC 3.1.1.5 and is selected from the group consisting of fragments. Examples of proteins having lysophospholipase activity and having an amino acid sequence that is at least 70% identical to SEQ ID NO: 24 are described herein as SEQ ID NOs: 15979 - 15981.

[0124] In some embodiments, the protein is derived from the genus Aspergillus. For example, in some embodiments, the protein is a native Aspergillus lysophospholipase or a fragment / mutant / variant of a native Aspergillus lysophospholipase.

[0125] In some embodiments, the protein is a) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 25; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NO: 25; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 116 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 25 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having pectin esterase activity belonging to EC3.1.1.11. Examples of proteins having pectin esterase activity and having an amino acid sequence that is at least 70% identical to SEQ ID NO: 25 are described herein as SEQ ID NOs: 2770 to 2777.

[0126] In some embodiments, the protein is derived from the genus Aspergillus. For example, in some embodiments, the protein is a native Aspergillus pectin esterase or a fragment / mutant / variant of a native Aspergillus pectin esterase.

[0127] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 26; b) a polypeptide having a sequence identity 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% with any one mature polypeptide of SEQ ID NO: 26; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 117 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 26 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide has phospholipase A1 activity belonging to EC 3.1.1.32 and is selected from the group consisting of fragments. Examples of proteins having phospholipase A1 activity and having an amino acid sequence at least 70% identical to SEQ ID NO: 26 are described herein as SEQ ID NOs: 10224 - 10242.

[0128] In some embodiments, the protein is derived from the genus Evansstolkia. For example, in some embodiments, the protein is the native Evansstolkia phospholipase A1 or a fragment / mutant / variant of the native Evansstolkia phospholipase A1.

[0129] In some embodiments, the protein is a) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 27 - 31, 72147 and 72149; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 27 - 31, 72147 and 72149; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 118 - 122, 72148 and 72150, or the cDNA sequences thereof; 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; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by addition of one or more amino acids; g) A fragment of any one of polypeptides a) to f), wherein the polypeptide is selected from the group consisting of fragments having cutinase activity belonging to EC 3.1.1.74. Examples of proteins having an amino acid sequence that exhibits cutinase activity and is at least 70% identical to one or more of SEQ ID NOs: 27 to 31, 72147, and 72149 are described herein as SEQ ID NOs: 15982 to 16004.

[0130] In some embodiments, the protein is derived from Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Myriococcum, Pyrenophora, Thermochaetoides, or Trichoderma. For example, in some embodiments, the protein is a native Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Myriococcum, Pyrenophora, Thermochaetoides, or Trichoderma cutinase, or a fragment / mutant / variant of a native Acrophialophora, Ascomycota, Chaetomium, Humicola, Hypocrea, Myceliophthora, Myriococcum, Pyrenophora, Thermochaetoides, or Trichoderma cutinase.

[0131] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 32; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NO: 32; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 123 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 32 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of a) to f), wherein the polypeptide is selected from the group consisting of fragments having phospholipase C activity belonging to EC 3.1.4.3. Examples of proteins having an amino acid sequence that exhibits phospholipase C activity and is at least 70% identical to SEQ ID NO: 32 are described herein as SEQ ID NOs: 16396 to 16412.

[0132] In some embodiments, the protein is derived from the genus Pseudomonas. For example, in some embodiments, the protein is a native Pseudomonas phospholipase C or a fragment / mutant / variant of native Pseudomonas phospholipase C.

[0133] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 33; b) a polypeptide having a sequence identity 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% with any one mature polypeptide of SEQ ID NO: 33; c) a polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 124 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 33 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide has inositol phospholipid phospholipase C activity belonging to EC 3.1.4.11 and is selected from the group consisting of fragments. Examples of proteins having inositol phospholipid phospholipase C activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 33 are described herein as SEQ ID NOs: 16005 to 16395.

[0134] In some embodiments, the protein is derived from Bacillus, Komagataella, or Lysinibacillus. For example, in some embodiments, the protein is a native Bacillus, Komagataella, or Lysinibacillus inositol lipid phospholipase C, or a fragment / mutant / variant of a native Bacillus, Komagataella, or Lysinibacillus inositol lipid phospholipase C.

[0135] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more esterase activities belonging to EC 3.1. For example, Canadian Patent No. 2715086A1; Chinese Patent No. 102604913A; No. 103045559A; No. 103243038A; No. 103555600A; No. 103865896A; No. 103981160A; No. 104293744A; No. 104878033A; No. 105087614A; No. 106591258A; No. 106632683A; No. 106635846A; No. 106676084A; No. 106884030A; No. 107151660A; No. 107488644A; No. 107488645A; No. 107488646A; No. 107488647A; No. 107488648A; No. 107815460A; No. 108118039A; No. 108239626A; No. 108239627A; No. 108277212A; No. 108315312A; No. 108359655A; No. 108913675A; No. 109321546A; No. 109468301A; No. 109776686A; No. 109929821A; No. 110129301A; No. 110760531A; No. 111378583A; No. 112175976A; No. 112574974A; No. 112592907A; No. 112608912A; No. 113025595A; No. 113025596A; No. 113122520A; No. 113215130A; No. 113338044A; No. 113736817A; No. 113755509A; No. 113846074A; No. 114317490A; No. 114621941A; No. 115521925A; No. 115717134A; German Patent Application Publication No. 102016204813A1;European Patent No. 2145904 A1; No. 2623586; 2; No. 305216 A; No. 3091080 A1; No. 3101108 A1; No. 3101109 A1; No. 3284811 A1; No. 3287513 A1; No. 3301145 A1; No. 3301147 A1; No. 3301156 A1; No. 3301161 A1; No. 3301162 A1; No. 3301163 A1; No. 3301165 A1; No. 3301166 A1; No. 3301169 A1; Japanese Unexamined Patent Application Publication No. 09-249891; No. 09-249893; Japanese Unexamined Patent Application Publication No. 2019-165727; US Patent Application Publication No. 2005287250 A1; No. 2007173430 A1; No. 2009162480 A1; No. 2009217463 A1; No. 2009217464 A1; No. 2009221033 A1; No. 2009221034 A1; No. 2011312057 A1; No. 2013316458 A1; No. 2018094228 A1; No. 2019093054 A1; No. 2020306342 A1; No. 2021015105 A1; No. 2022177812 A1; No. 9102933 B1; International Publication No. 2000060063 A1 Pamphlet; No. 200011211 A1 Pamphlet; No. 200034450 A1 Pamphlet; No. 200127251 A1 Pamphlet; No. 200192502 A1 Pamphlet; No. 200255679 A2 Pamphlet; No. 200262973 A2 Pamphlet; No. 200266622 A2 Pamphlet; No. 200295127 A2 Pamphlet; No. 2003060112 A1 Pamphlet; No. 2003089620 A2 Pamphlet; No. 2004099400 A2 Pamphlet; No. 2004111216 A2 Pamphlet; No. 2005032496 A2 Pamphlet; No. 2005086900 A2 Pamphlet; No. 2006084470 A2 Pamphlet; No. 2006136159 A2 Pamphlet; No. 2006136160 A2 Pamphlet;Same as Pamphlet No. 2007080197A2; Same as Pamphlet No. 2007087243A2; Same as Pamphlet No. 2007087318A2; Same as Pamphlet No. 2007087319A2; Same as Pamphlet No. 2007087508A2; Same as Pamphlet No. 2008073169A2; Same as Pamphlet No. 2008079685A2; Same as Pamphlet No. 2008122640A2; Same as Pamphlet No. 2009071550A1; Same as Pamphlet No. 2009083607A1; Same as Pamphlet No. 2009108941A2; Same as Pamphlet No. 2009133177A1; Same as Pamphlet No. 2011046812A1; Same as Pamphlet No. 2011046815A1; Same as Pamphlet No. 2012027282A2; Same as Pamphlet No. 2012078741A2; Same as Pamphlet No. 2012129548A2; Same as Pamphlet No. 2012173658A1; Same as Pamphlet No. 2013098205A2; Same as Pamphlet No. 2013113622A1; Same as Pamphlet No. 2013149858A1; Same as Pamphlet No. 2013171072A1; Same as Pamphlet No. 2013181760A1; Same as Pamphlet No. 2014055778A2; Same as Pamphlet No. 2014059360A1; Same as Pamphlet No. 2014059541A1; Same as Pamphlet No. 2014081700A1; Same as Pamphlet No. 2014081884A1; Same as Pamphlet No. 2014147219A1; Same as Pamphlet No. 2014162001A1; Same as Pamphlet No. 2014184164A1; Same as Pamphlet No. 2014186464A1; Same as Pamphlet No. 2015010009A2; Same as Pamphlet No. 2015017045A1; Same as Pamphlet No. 2015048332A2; Same as Pamphlet No. 2015067161A1; Same as Pamphlet No. 2015085920A1; Same as Pamphlet No. 2015109405A1; Same as Pamphlet No. 2015110058A1; Same as Pamphlet No. 2015110562A1; Same as Pamphlet No. 2015140275A1; Same as Pamphlet No. 2015144780A2; Same as Pamphlet No. 2015173426A1; Same as Pamphlet No. 2016050661A1; Same as Pamphlet No. 2016087401A1;Same as Pamphlet No. 2016090472A1; Same as Pamphlet No. 2016090473A1; Same as Pamphlet No. 2016090474A1; Same as Pamphlet No. 2016091870A1; Same as Pamphlet No. 2016102356A1; Same as Pamphlet No. 2016107567A1; Same as Pamphlet No. 2016109758A2; Same as Pamphlet No. 2016164596A2; Same as Pamphlet No. 2017001673A1; Same as Pamphlet No. 2017005640A1; Same as Pamphlet No. 2017015233A1; Same as Pamphlet No. 2017093318A1; Same as Pamphlet No. 2017101801A1; Same as Pamphlet No. 2017161091A1; Same as Pamphlet No. 2017182666A1; Same as Pamphlet No. 2018001959A1; Same as Pamphlet No. 2018015295A1; Same as Pamphlet No. 2018127486A1; Same as Pamphlet No. 2018171552A1; Same as Pamphlet No. 2018188667A1; Same as Pamphlet No. 2019014118A1; Same as Pamphlet No. 2019060574A1; Same as Pamphlet No. 2019063499A1; Same as Pamphlet No. 2019110462A1; Same as Pamphlet No. 2019137289A1; Same as Pamphlet No. 2019154951A1; Same as Pamphlet No. 2019154952A1; Same as Pamphlet No. 2019154954A1; Same as Pamphlet No. 2019154955A1; Same as Pamphlet No. 2019215078A1; Same as Pamphlet No. 2019236717A1; Same as Pamphlet No. 2020014407A1; Same as Pamphlet No. 2020046613A1; Same as Pamphlet No. 2020076697A1; Same as Pamphlet No. 2020088393A1; Same as Pamphlet No. 2020103861A1; Same as Pamphlet No. 2020135657A1; Same as Pamphlet No. 2020135658A1; Same as Pamphlet No. 2020173817A1; Same as Pamphlet No. 2020190782A1; Same as Pamphlet No. 2021037878A1; Same as Pamphlet No. 2021119304A1; Same as Pamphlet No. 2021170799A1; Same as Pamphlet No. 2021239267A1; Same as Pamphlet No. 2022063699A1;Refer to Pamphlet No. 2022090361A2; Pamphlet No. 2022103725A1; Pamphlet No. 2022173694A1; Pamphlet No. 2023032952A1; Pamphlet No. 2023288294A1; Specification No. 9205249A; Pamphlet No. 9219726A1; Pamphlet No. 9425575A1; Pamphlet No. 9425577A1; Pamphlet No. 9522615A1; Pamphlet No. 9613580A1; Pamphlet No. 9704079A1; Pamphlet No. 9707202A1; Pamphlet No. 9707205A1; Pamphlet No. 9707206A1.;

[0136] In some embodiments, the proteins of the present disclosure have glycosidase activity belonging to EC3.2.1 (e.g., α-amylase activity belonging to EC3.2.1.1, β-amylase activity belonging to EC3.2.1.2, glucan 1,4-α-glucosidase activity belonging to 3.2.1.3, cellulase activity belonging to EC3.2.1.4, endo-1,3(4)-β-glucanase activity belonging to EC3.2.1.6, 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 belonging to 3.2.1.10, 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, 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, amyloglucosidase activity belonging to EC3.2.1.33, xylan 1,4-β-xylosidase activity belonging to 3.2.1.37, glucan 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, glucan 1,3-β-glucosidase activity belonging to 3.2.1.58, glucan endo-1,3-α-glucosidase activity belonging to 3.2.1.59, glucan 1,6-α-glucosidase activity belonging to EC3.2.1.70, glucan endo-1,2-β-glucosidase activity belonging to EC3.2.1.71, xylan 1,3-β-xylosidase activity belonging to 3.2.1.72, licheninase activity belonging to 3.2.1.73, glucan 1,4-β-glucosidase activity belonging to EC3.2.1.74, 3.2.1.Glucan endo-1,6-β-glucosidase activity belonging to 75, mannan 1,2-(1,3)-α-mannosidase activity belonging to EC3.2.1.77, mannan endo-1,4-β-mannosidase activity belonging to 3.2.1.78, glucan 1,3-α-glucosidase activity belonging to EC3.2.1.84, cellulose 1,4-β-cellobiosidase activity belonging to 3.2.1.91, peptidoglycan β-N-acetylmuramidase activity belonging to EC3.2.1.92, endo-α-N-acetylgalactosaminidase activity belonging to EC3.2.1.97, mannan 1,4-mannobiosidase activity belonging to EC3.2.1.100, mannan endo-1,6-α-mannosidase activity belonging to 3.2.1.101, endogalactosaminidase activity belonging to 3.2.1.109, 1,3-α-L-fucosidase activity belonging to 3.2.1.111, 2-deoxyglucosidase activity belonging to 3.2.1.112, glycoprotein endo-α-1,2-mannosidase activity belonging to EC3.2.1.130, chitosanase activity belonging to EC3.2.1.132, glucan 1,4-α-maltohydrolase activity belonging to 3.2.1.133, mannan exo-1,2-1,6-α-mannosidase activity belonging to EC3.2.1.137, 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-galactonase activity belonging to EC3.2.1.181, α-mannan endo-1,2-α-mannanase activity belonging to EC3.2.1.198, exo-chitinase activity belonging to EC3.2.1.200, exo-chitinase activity belonging to EC3.2.1.201), etc., EC3.Exhibits one or more glucosidase activities belonging to 2, and optionally has an identity 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% with one or more of the amino acid sequences described herein as SEQ ID NOs: 34-80, 45906 and 72144, and includes, consists essentially of, or consists of such amino acid sequences.

[0137] In some embodiments, the protein is a) a polypeptide having an identity 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% with one or more of SEQ ID NOs: 34-40; b) a polypeptide having an identity 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% with the mature polypeptide of any one of SEQ ID NOs: 34-40; 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 of SEQ ID NOs: 125 to 131 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 34 to 40 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 34 to 40 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide has α-amylase activity belonging to EC 3.2.1.1 and is selected from the group consisting of fragments. Examples of proteins having α-amylase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 34 to 40 are described herein as SEQ ID NOs: 16413 to 45041.

[0138] In some embodiments, the protein is derived from Alicyclobacillus, Alkalihalobacillus, Anoxybacillus, Aspergillus, Bacillus, Cytophaga, Exiguobacterium, Geobacillus, Hamigera, Homo sapiens, Jeotgalibacillus, Neosartorya, Penicillium, Priestia, Pyrococcus, Rasamsonia, Sutcliffiella or Thermoascus.For example, in some embodiments, the protein is a native Alicyclobacillus, Alkalihalobacillus, Anoxybacillus, Aspergillus, Bacillus, Cytophaga, Exiguobacterium, Geobacillus, Hamigera, Homo sapiens, Jeotgalibacillus, Neosartorya, Penicillium, Priestia, Pyrococcus, Rasamsonia, Sutcliffiella or Thermoascus α - amylase, or a fragment / mutant / variant of an Alicyclobacillus, Alkalihalobacillus, Anoxybacillus, Aspergillus, Bacillus, Cytophaga, Exiguobacterium, Geobacillus, Hamigera, Homo sapiens, Jeotgalibacillus, Neosartorya, Penicillium, Priestia, Pyrococcus, Rasamsonia, Sutcliffiella or Thermoascus α - amylase.

[0139] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 41-42; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 41-42; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 132-133 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 41-42 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a)-f), The polypeptide is selected from the group consisting of fragments having glucan 1,4-α-glucosidase activity belonging to EC3.2.1.3. Examples of proteins having glucan 1,4-α-glucosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 41-42 are described herein as SEQ ID NOs: 45756-45904.

[0140] In some embodiments, the protein is derived from the genus Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rasamsonia or Saccharomycopsis. For example, in some embodiments, the protein is a native Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rasamsonia or Saccharomycopsis glucan 1,4-α-glucosidase, or a fragment / mutant / variant of a native Aspergillus, Bos, Elaphocordyceps, Fusarium, Penicillium, Rasamsonia or Saccharomycopsis glucan 1,4-α-glucosidase.

[0141] In some embodiments, the protein is a) a polypeptide having at least 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 with one or more of SEQ ID NOs: 43-45; b) a polypeptide having at least 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 with the mature polypeptide of any one of SEQ ID NOs: 43-45; c) a polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NOs: 134-136 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 43-45 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a)-f), wherein The polypeptide is selected from the group consisting of fragments having cellulase activity belonging to EC 3.2.1.4. Examples of proteins having an amino acid sequence that exhibits cellulase activity and is at least 70% identical to one or more of SEQ ID NOs: 43 to 45 are described herein as SEQ ID NOs: 45913 to 48750.

[0142] 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, Scytalidium, Sordaria, Staphylotrichum, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Trichocladium, Trichothecium or Triticum. For example, in some embodiments, the protein is from a natural Acremonium, Alteromonas, Ascomycota, Aspergillus, Bacillus, Chaetomium, Clonostachys, Corynascus, Cylindrocarpon, Escherichia, Fusarium, Humicola, Madurella, Melanocarpus, Myceliophthora, Neurospora,It is a cellulase of Podospora, Remersonia, Scytalidium, Sordaria, Staphylotrichum, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Trichocladium, Trichothecium or Triticum, or a fragment / mutant / variant of a cellulase of a natural Acremonium, Alteromonas, Ascomycota, Aspergillus, Bacillus, Chaetomium, Clonostachys, Corynascus, Cylindrocarpon, Escherichia, Fusarium, Humicola, Madurella, Melanocarpus, Myceliophthora, Neurospora, Podospora, Remersonia, Scytalidium, Sordaria, Staphylotrichum, Thermocarpiscus, Thermochaetoides, Thermothielavioides, Thielavia, Trichocladium, Trichothecium or Triticum.,

[0143] In some embodiments, the protein is a) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 46; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 46; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 137 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 46 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 46 by substitution, deletion or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having endo-1,3(4)-β-glucanase activity belonging to EC3.2.1.6. Examples of proteins having endo-1,3(4)-β-glucanase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 46 are described herein as SEQ ID NOs: 49229 to 49346.

[0144] In some embodiments, the protein is derived from the genus 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.

[0145] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 47; b) A polypeptide having at least 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 with any one of the mature polypeptides of SEQ ID NO: 47; c) A polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 138 or one or more of its cDNA sequences; d) A polypeptide derived from any one of SEQ ID NO: 47 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide has inulinase activity belonging to EC 3.2.1.7 and is selected from the group consisting of fragments. Examples of proteins having inulinase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 47 are described herein as SEQ ID NOs: 49347 to 49419.

[0146] In some embodiments, the protein is derived from Aspergillus, Penicillium, Pseudomonas or Talaromyces. For example, in some embodiments, the protein is a native Aspergillus, Penicillium, Pseudomonas or Talaromyces inulinase, or a fragment / mutant / variant of Aspergillus, Penicillium, Pseudomonas or Talaromyces inulinase.

[0147] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NOs: 48 - 53; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NOs: 48 - 53; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 139 to 144, or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 48 to 53 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from the mature polypeptide of any one of SEQ ID NOs: 48 to 53 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide has endo-1,4-β-xylanase activity belonging to EC 3.2.1.8, and is selected from the group consisting of fragments. Examples of proteins having endo-1,4-β-xylanase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 48 to 53 are described herein as SEQ ID NOs: 49453 to 49912.

[0148] In some embodiments, the protein is derived from Anaerocellum, Aspergillus, Bacillus, Caldicellulosiruptor, Clostridium, Dicytoglomus, Evansstolkia, Hordeum, Lactobacillus, Malbranchea, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rasamsonia, Saccharomyces, Talaromyces, Thermoclostridium, Thermomyces, Thermus or Viridiplantae. For example, in some embodiments, the protein is a native Anaerocellum, Aspergillus, Bacillus, Caldicellulosiruptor, Clostridium, Dicytoglomus, Evansstolkia, Hordeum, Lactobacillus, Malbranchea, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rasamsonia, Saccharomyces,It is an endo-1,4-β-xylanase of the genus Talaromyces, Thermoclostridium, Thermomyces, Thermus or Viridiplantae, or a fragment / mutant / variant of an endo-1,4-β-xylanase of the genus Anaerocellum, Aspergillus, Bacillus, Caldicellulosiruptor, Clostridium, Dicytoglomus, Evansstolkia, Hordeum, Lactobacillus, Malbranchea, Neosartorya, Nicotiana, Paecilomyces, Paenibacillus, Penicillium, Pyrococcus, Rasamsonia, Saccharomyces, Talaromyces, Thermoclostridium, Thermomyces, Thermus or Viridiplantae.

[0149] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 54; b) a polypeptide having at least 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 with any one of the mature polypeptides of SEQ ID NO: 54; c) a polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 145 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 54 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), The polypeptide is selected from the group consisting of fragments having dextranase activity belonging to EC 3.2.1.11. Examples of proteins having dextranase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 54 are described herein as SEQ ID NOs: 45063 to 45071.

[0150] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 56; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 56; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 147 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 56 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 56 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having lysozyme activity belonging to EC3.2.1.17. Examples of proteins having an amino acid sequence that exhibits lysozyme activity and is at least 70% identical to one or more of SEQ ID NO: 56 are described herein as SEQ ID NOs: 45443 to 45456.

[0151] In some embodiments, the protein is derived from the genus Clonostachys or the genus Sodiomyces. For example, in some embodiments, the protein is a native Clonostachys or Sodiomyces lysozyme, or a fragment / mutant / variant of a native Clonostachys or Sodiomyces lysozyme.

[0152] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 57; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NO: 57; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to SEQ ID NO: 148 or to one or more of the cDNA sequences thereof; d) a polypeptide derived from any one of SEQ ID NO: 57 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide has β-glucosidase activity belonging to EC 3.2.1.21 and is selected from the group of fragments. Examples of proteins having β-glucosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 57 are described herein as SEQ ID NOs: 45457 to 45754.

[0153] In some embodiments, the protein is derived from Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rasamsonia, Schizosaccharomyces, or Thermoascus. For example, in some embodiments, the protein is a native Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rasamsonia, Schizosaccharomyces, or Thermoascus β-glucosidase, or a fragment / mutant / variant of a native Aspergillus, Coccidioides, Evansstolkia, Neosartorya, Penicillium, Rasamsonia, Schizosaccharomyces, or Thermoascus β-glucosidase.

[0154] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 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; b) A polypeptide having at least 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 with any one of the mature polypeptides of SEQ ID NO: 58; c) A polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 149 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 58 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide has α-mannosidase activity belonging to EC3.2.1.24 and is selected from the group of fragments. Examples of proteins having α-mannosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 58 are described herein as SEQ ID NO: 45755.

[0155] In some embodiments, the protein is derived from Neobacillus. For example, in some embodiments, the protein is native Neobacillus α-mannosidase or a fragment / mutant / variant of native Neobacillus α-mannosidase.

[0156] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 59 - 60 and 45906; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 59 - 60 and 45906; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 150 - 151 and 72146, or the cDNA sequence thereof; 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; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), wherein the polypeptide is selected from the group consisting of fragments having endo - 1,3 - β - D - glucanase activity belonging to EC 3.2.1.39. Examples of proteins having endo - 1,3 - β - D - glucanase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 59 - 60 and 45906 are described herein as SEQ ID NOs: 45905 - 45912.

[0157] In some embodiments, the protein is derived from the genus Trichoderma. For example, in some embodiments, the protein is a native Trichoderma endo - 1,3 - β - D - glucanase or a fragment / mutant / variant of a native Trichoderma endo - 1,3 - β - D - glucanase.

[0158] In some embodiments, the protein is a) A polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 61; b) A polypeptide having at least 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 with any one of the mature polypeptides of SEQ ID NO: 61; c) A polypeptide encoded by a polynucleotide having at least 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 with SEQ ID NO: 152 or one or more of its cDNA sequences; d) A polypeptide derived from any one of SEQ ID NO: 61 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 61 by substitution, deletion or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a) to f), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to g), wherein the polypeptide has pullulanase activity belonging to EC 3.2.1.41 and is selected from the group consisting of fragments. Examples of proteins having pullulanase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 61 are described herein as SEQ ID NOs: 48751 to 49148.

[0159] In some embodiments, the protein is derived from the genus 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.

[0160] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 62; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NO: 62; 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 with SEQ ID NO: 153 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 62 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), the polypeptide has α-L-arabinofuranosidase activity belonging to EC 3.2.1.55, and is selected from the group consisting of fragments. Examples of proteins having α-L-arabinofuranosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 62 are described herein as SEQ ID NOs: 49149 to 49209.

[0161] In some embodiments, the protein is derived from Acremonium, Acrophialophora, 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 an α-L-arabinofuranosidase from a natural Acremonium, Acrophialophora, Actinomadura, Actinoplanes, Aureobasidium, Chaetomium, Gliomastix, Humicola, Hypocrea, Microdochium, Myceliophthora, Oculimacula, Penicillium, Streptomyces, Streptosporangium, Talaromyces, Thielavia, Trichoderma or Xylanibacterium, or is a fragment / mutant / variant of an α-L-arabinofuranosidase from a natural Acremonium, Acrophialophora, Actinomadura, Actinoplanes, Aspergillus, Aureobasidium, Chaetomium, Gliomastix, Humicola, Hypocrea, Microdochium, Myceliophthora, Oculimacula, Penicillium, Streptomyces, Streptosporangium, Talaromyces, Thielavia, Trichoderma or Xylanibacterium.

[0162] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 63-64; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 63-64; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 154-155, or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 63-64 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of a) to f), The polypeptide is selected from the group consisting of fragments having glucan endo-1,3-α-glucosidase activity belonging to EC 3.2.1.59. Examples of proteins having an amino acid sequence that exhibits glucan endo-1,3-α-glucosidase activity and is at least 70% identical to one or more of SEQ ID NOs: 63-64 are described herein as SEQ ID NOs: 49210-49228.

[0163] In some embodiments, the protein is derived from the genus Clonostachys, Hypocrea, Myceliophthora or Trichoderma. For example, in some embodiments, the protein is a native Clonostachys, Hypocrea, Myceliophthora or Trichoderma glucan endo-1,3-α-glucosidase, or a fragment / mutant / variant of a native Clonostachys, Hypocrea, Myceliophthora or Trichoderma glucan endo-1,3-α-glucosidase.

[0164] In some embodiments, the protein is a) A polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 65; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 65; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 156 or one or more of its cDNA sequences; d) A polypeptide derived from any one of SEQ ID NO: 65 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), wherein the polypeptide has licheninase activity belonging to EC 3.2.1.73 and is selected from the group consisting of fragments. Examples of proteins having licheninase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 65 are described herein as SEQ ID NOs: 49420 - 49446.

[0165] In some embodiments, the protein is derived from Bacillus or Salipaludibacillus. For example, in some embodiments, the protein is a native Bacillus or Salipaludibacillus licheninase, or a fragment / mutant / variant of a native Bacillus or Salipaludibacillus licheninase.

[0166] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 66 - 67; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 66 - 67; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 157 - 158, or one or more of these cDNA sequences; d) A polypeptide derived from any one of SEQ ID NOs: 66 - 67 by substitution, deletion, or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having glucan - 1,6 - β - glucosidase activity belonging to EC3.2.1.75. Examples of proteins exhibiting glucan endo - 1,6 - β - glucosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 66 - 67 are described herein as SEQ ID NOs: 49447 - 49451.

[0167] In some embodiments, the protein is derived from the genus Trichoderma. For example, in some embodiments, the protein is a native Trichoderma glucan endo - 1,6 - β - glucosidase or a fragment / mutant / variant of a native Trichoderma glucan endo - 1,6 - β - glucosidase.

[0168] In some embodiments, the protein is a) A polypeptide having a sequence identity 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% with one or more of SEQ ID NOs: 68 and 72144; b) a polypeptide having at least 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 with either of the mature polypeptides of SEQ ID NO: 68 and 72144; c) a polypeptide encoded by a polynucleotide having at least 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 with either SEQ ID NO: 159 and 72145, or one or more of these cDNA sequences; d) a polypeptide derived from either of SEQ ID NO: 68 and 72144 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from the mature polypeptide of either of SEQ ID NO: 68 and 72144 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide has mannan endo-1,4-β-mannosidase activity belonging to EC 3.2.1.78 and is selected from the group consisting of fragments. Examples of proteins having mannan endo-1,4-β-mannosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 68 and 72144 are described herein as SEQ ID NO: 49452.

[0169] In some embodiments, the protein is derived from the genus Alkalihalobacillus. For example, in some embodiments, the protein is the native Alkalihalobacillus mannan endo-1,4-β-mannosidase or a fragment / mutant / variant of the native Alkalihalobacillus mannan endo-1,4-β-mannosidase.

[0170] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 69; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NO: 69; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 160 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 69 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having mannan endo-1,6-α-mannosidase activity belonging to EC 3.2.1.101. Examples of proteins having mannan endo-1,6-α-mannosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 69 are described herein as SEQ ID NO: 45042.

[0171] In some embodiments, the protein is derived from the genus Talaromyces. For example, in some embodiments, the protein is a native Talaromyces mannan endo-1,6-α-mannosidase or a fragment / mutant / variant of a native Talaromyces mannan endo-1,6-α-mannosidase.

[0172] In some embodiments, the protein is a) A polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 70 - 75; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NOs: 70-75; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 161-166, or the cDNA sequences thereof; d) a polypeptide derived from any one of SEQ ID NOs: 70-75 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a)-f), wherein the polypeptide has endo - galactosaminidase activity belonging to EC 3.2.1.109 and is selected from the group consisting of fragments. Examples of proteins having endo - galactosaminidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 70-75 are described herein as SEQ ID NOs: 45043-45062.

[0173] In some embodiments, the protein is derived from Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urnula. For example, in some embodiments, the protein is a native Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urnula endogalactosaminidase, or a fragment / mutant / variant of a native Bjerkandera, Diaporthe, Fusarium, Neonectria, Ostropa, Pseudoplectania, Stenocarpella, or Urnula endogalactosaminidase.

[0174] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 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; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NOs: 76-77; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 167-168, or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 76-77 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a)-f), wherein the polypeptide is selected from the group consisting of fragments having the glycoprotein endo-α-1,2-mannosidase activity belonging to EC 3.2.1.130 and / or the α-mannan endo-1,2-α-mannosidase activity belonging to EC 3.2.1.198.

[0175] In some embodiments, the protein is derived from the genus Chryseobacterium or Lysobacter. For example, in some embodiments, the protein is a native Chryseobacterium or Lysobacter glycoprotein endo-α-1,2-mannosidase, or a fragment / mutant / variant of a native Chryseobacterium or Lysobacter glycoprotein endo-α-1,2-mannosidase. Similarly, in some embodiments, the protein is a native Chryseobacterium or Lysobacter α-mannan endo-1,2-α-mannanase, or a fragment / mutant / variant of a native Chryseobacterium or Lysobacter α-mannan endo-1,2-α-mannanase.

[0176] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 78; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NO: 78; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 169 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 78 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide is selected from the group consisting of fragments having glucan 1,4-α-maltohydrolase activity belonging to EC 3.2.1.133. Examples of proteins having glucan 1,4-α-maltohydrolase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 78 are described herein as SEQ ID NOs: 45072 to 45408.

[0177] In some embodiments, the protein is derived from Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus. For example, in some embodiments, the protein is a native Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus glucan 1,4-α-maltohydrolase, or a fragment / mutant / variant of a native Alicyclobacillus, Bacillus, Effusibacillus, or Geobacillus glucan 1,4-α-maltohydrolase.

[0178] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 79; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NO: 79; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to SEQ ID NO: 170 or to one or more of the cDNA sequences thereof; d) a polypeptide derived from any one of SEQ ID NO: 79 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) to f), wherein the polypeptide has 1,6-α-D-mannosidase activity belonging to EC 3.2.1.163 and is selected from the group consisting of fragments. Examples of proteins having 1,6-α-D-mannosidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 79 are described herein as SEQ ID NOs: 45437 to 45442.

[0179] In some embodiments, the protein is derived from Aspergillus, Evansstolkia, Penicillium, Rasamsonia, Talaromyces or Thermomyces. For example, in some embodiments, the protein is a native Aspergillus, Evansstolkia, Penicillium, Rasamsonia, Talaromyces or Thermomyces 1,6-α-D-mannosidase, or a fragment / mutant / variant of a native Aspergillus, Evansstolkia, Penicillium, Rasamsonia, Talaromyces or Thermomyces 1,6-α-D-mannosidase.

[0180] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more glucosidase activities belonging to EC 3.2. For example, Australian Patent Application Publication No. 2016101771A4; No. 2017203481A1; Brazilian Patent Registration No. 20193C1; Chinese Patent No. 101134949A; No. 101139556A; No. 101173226A; No. 101298604A; No. 101457230A; No. 101492661A; No. 101659948A; No. 101824401A; No. 101870956A; No. 101899458A; No. 101962633A; No. 102021191A; No. 102477437A; No. 102477438A; No. 102492707A; Chinese Patent No. 102703480A; No. 102796751A; No. 102827821A; No. 102851266A; No. 102994475A; No. 103060290A; No. 103184163A; No. 103194419A; No. 103343111A; No. 103525793A; No. 103555751A; No. 103789285A; No. 103805579A; No. 103834606A; No. 103966188A; No. 104130988A; No. 104293748A; No. 104313000A; No. 104450650A; No. 104450651A; No. 104480087A; No. 104498456A; No. 104561060A; No. 104789543A; No. 104862290A; No. 104928270A; No. 105039288A; No. 105062991A; No. 105155324A; No. 105176947A; No. 105177084A; No. 105441415A; No. 105623937A; No. 105671019A;Same as Specification No. 105671022A; Same as Specification No. 105695435A; Same as Specification No. 105734034A; Same as Specification No. 105802940A; Same as Specification No. 105802943A; Same as Specification No. 105886520A; Same as Specification No. 105907775A; Same as Specification No. 105969783A; Same as Specification No. 106084016A; Same as Specification No. 106148235A; Same as Specification No. 106190934A; Same as Specification No. 106754825A; Same as Specification No. 106754826A; Same as Specification No. 106801046A; Same as Specification No. 106929495A; Same as Specification No. 107022588A; Same as Specification No. 107058264A; Same as Specification No. 107236692A; Same as Specification No. 107312763A; Same as Specification No. 107326020A; Same as Specification No. 107475219A; Same as Specification No. 107513527A; Same as Specification No. 107586767A; Same as Specification No. 107603965A; Same as Specification No. 108102934A; Same as Specification No. 108588056A; Same as Specification No. 108611339A; Same as Specification No. 108623652A; Same as Specification No. 108795781A; Same as Specification No. 108823186A; Same as Specification No. 108841809A; Same as Specification No. 109022396A; Same as Specification No. 109055439A; Same as Specification No. 109207458A; Same as Specification No. 109234339A; Same as Specification No. 109321552A; Same as Specification No. 109370973A; Same as Specification No. 109439607A; Same as Specification No. 109439641A; Same as Specification No. 109486689A; Same as Specification No. 109486791A; Same as Specification No. 109777795A; Same as Specification No. 109810961A; Same as Specification No. 109825466A; Same as Specification No. 109897842A; Same as Specification No. 110066777A; Same as Specification No. 110157688A; Same as Specification No. 110229800A; Same as Specification No. 110343687A; Same as Specification No. 110423737A; Same as Specification No. 110495549A; Same as Specification No. 110592051A; Same as Specification No. 110628748A; Same as Specification No. 110699337A; Same as Specification No. 110713999A; Same as Specification No. 110724645A; Same as Specification No. 110724646A; Same as Specification No. 110951628A;Same as the specification of Patent No. 111454929A; same as the specification of Patent No. 111500558A; same as the specification of Patent No. 111518792A; same as the specification of Patent No. 111621490A; same as the specification of Patent No. 111793613A; same as the specification of Patent No. 111826377A; same as the specification of Patent No. 112063678A; same as the specification of Patent No. 112342208A; same as the specification of Patent No. 112522238A; same as the specification of Patent No. 112552382A; same as the specification of Patent No. 112680433A; same as the specification of Patent No. 112795554A; same as the specification of Patent No. 112795555A; same as the specification of Patent No. 113151327A; same as the specification of Patent No. 113234705A; same as the specification of Patent No. 113584075A; same as the specification of Patent No. 113667662A; same as the specification of Patent No. 113717864A; same as the specification of Patent No. 113817709A; same as the specification of Patent No. 113881654A; same as the specification of Patent No. 114350637A; same as the specification of Patent No. 114369588A; same as the specification of Patent No. 114457056A; same as the specification of Patent No. 114606216A; same as the specification of Patent No. 114686386A; same as the specification of Patent No. 114752583A; same as the specification of Patent No. 114790451A; same as the specification of Patent No. 115029334A; same as the specification of Patent No. 115074345A; same as the specification of Patent No. 115125226A; same as the specification of Patent No. 115197924A; same as the specification of Patent No. 115247165A; same as the specification of Patent No. 115478061A; same as the specification of Patent No. 115703996A; same as the specification of Patent No. 115704017A; same as the specification of Patent No. 115704018A; same as the specification of Patent No. 115704019A; same as the specification of Patent No. 1465699A; same as the specification of Patent No. 1594542A; same as the specification of Patent No. 1834249A; DD272102A; German Patent Application Publication No. 102004047777A1; same as the specification of Patent No. 10200 - 5062984A1; same as the specification of Patent No. 102014018149A1; same as the specification of Patent No. 102014212640A1; same as the specification of Patent No. 102014212643A1; German Patent Application Publication No. DE1020142254721; same as the specification of Patent No. 102014225473A1; same as the specification of Patent No. 102020205400A1; same as the specification of Patent No. 10309803A1; European Patent Application Publication No. 1764411A1; same as the specification of Patent No. 208491; same as the specification of Patent No. 2100948A1; same as the specification of Patent No. 2100950A1; same as the specification of Patent No. 2116136A1; same as the specification of Patent No. 2166092A1; same as the specification of Patent No. 2292773A1; same as the specification of Patent No. 2295582A2;Japanese Patent No. 2298904A1; Japanese Patent No. 2314698A1; Japanese Patent No. 2357220A1; Japanese Patent No. 2404928A1; Japanese Patent No. 2404930A1; Japanese Patent No. 2486799A1; Japanese Patent No. 2540825A2; Japanese Patent No. 2551335A1; Japanese Patent No. 260160; Japanese Patent No. 285123A; Japanese Patent No. 2993230A1; Japanese Patent No. 3034592A1; Japanese Patent No. 3121270A2; Japanese Patent No. 3228703A1; Japanese Patent No. 3241890A1; Japanese Patent No. 3241891A1; Japanese Patent No. 3301154A1; Japanese Patent No. 3330349A1; Japanese Patent No. 3339422A1; Japanese Patent No. 3428260A2; Japanese Patent No. 3485734A1; Japanese Patent No. 3502242A1; Japanese Patent No. 3502243A1; Japanese Patent No. 3653705A1; Japanese Patent No. 3653706A1; Japanese Patent No. 3730595A2; Japanese Patent No. 4001389A1; Japanese Patent No. 4047088A1; Japanese Patent No. 409299A; Japanese Patent No. 4952571; Japanese Patent No. 540784A1; Japanese Patent No. 605040A1; Japanese Patent No. 633311A1; Japanese Patent No. 683228A2; Japanese Patent No. 828002A2; French Patent No. 2665178A; French Patent No. 2676456A1; UK Patent No. 2479462A; Indian Patent No. 194800B; Indian Patent Application Publication No. 201811045754A; Indian Patent No. 9700577I1; Indian Patent No. 9702287I4; Japanese Unexamined Patent Application Publication No. 4058889; Japanese Unexamined Patent Application Publication No. 7059574; Japanese Unexamined Patent Application Publication No. 2000135093; Japanese Unexamined Patent Application Publication No. 2000245466; Japanese Unexamined Patent Application Publication No. 2004313022; Japanese Unexamined Patent Application Publication No. 2005171409; Japanese Unexamined Patent Application Publication No. 2011167076; Japanese Unexamined Patent Application Publication No. 2011223962; Japanese Unexamined Patent Application Publication No. 2016015894; Japanese Unexamined Patent Application Publication No. 2019146520; Japanese Unexamined Patent Application Publication No. 2020065514; Japanese Unexamined Patent Application Publication No. 2020184937; Japanese Unexamined Patent Application Publication No. 62104580; Korean Patent Application Publication No. 2001027418A; Korean Patent Application Publication No. 2004006812A; Korean Patent Application Publication No. 2011017208A; Korean Patent Application Publication No. 2011106174A; Korean Patent Application Publication No. 2012140565A; Korean Patent Application Publication No. 2013112172A; Korean Patent No. 834708B1;New Zealand Patent Specification No. 524303A; Russian Patent Specification No. 2574206C1; Turkish Patent Publication No. 201404579A; Taiwan Patent Publication No. 200811294; US Patent Application Publication No. 10563185B1; No. 2004191864A1; No. 2005108791A1; No. 2005196853A1; No. 2005214410A1; No. 2006246566A1; No. 2007044171A1; No. 2007244020A1; No. 2008044858A1; No. 2008148432A1; No. 2009111155A1; No. 2009117642A1; No. 2009158452A1; No. 2009181874A1; No. 2009203109A1; No. 2009209026A1; No. 2009238923A1; No. 2009252828A1; No. 2010021587A1; No. 2010124769A1; No. 2010204080A1; No. 2010323448A1; No. 2011039751A1; No. 2011099671A1; No. 2011195481A1; No. 2011252501A1; No. 2011269210A1; No. 2011287516A1; No. 2012156734A1; No. 2012252095A1; No. 2013011882A1; No. 2013074202A1; No. 2013252850A1; No. 2013269061A1; No. 2014017737A1; No. 2014127753A1; No. 2014256018A1; No. 2015064766A1; No. 2015299720A1; No. 2015337329A1; No. 2016032267A1; No. 2017247730A1; No. 2017342433A1; No. 2018010111A1; No. 2018155744A1; No. 2018163191A1; No. 2018216039A1;Same as the specification of Patent No. 2018258442A1; same as the specification of Patent No. 2019194634A1; same as the specification of Patent No. 2019359961A1; same as the specification of Patent No. 2019360012A1; same as the specification of Patent No. 2020181593A1; same as the specification of Patent No. 2020270593A1; same as the specification of Patent No. 2020306342A1; same as the specification of Patent No. 2020339917A1; same as the specification of Patent No. 2021122998A1; Specification; Japanese Patent No. 2021-163995 A1; Japanese Patent No. 2021-230644 A1; Japanese Patent No. 2021-254115 A1; Japanese Patent No. 2021-292688 A1; Japanese Patent No. 2021-317431 A1; Japanese Patent No. 2022-154236 A1; Japanese Patent No. 2022-204956 A1; Japanese Patent No. 2022-347262 A1; Japanese Patent No. 2023-002748 A1; Japanese Patent No. 5824532 A; Japanese Patent No. 5849549 A; Japanese Patent No. 6682923 B1; US Patent No. 6887986 B1; US Patent No. 7504490 B1; US Patent No. 8409836 B2; International Publication No. 2000 / 01796 A2 Pamphlet; International Publication No. 2000 / 29560 A1 Pamphlet; International Publication No. 2000 / 34452 A1 Pamphlet; International Publication No. 2000 / 43504 A1 Pamphlet; International Publication No. 2000 / 60058 A2 Pamphlet; International Publication No. 2000 / 60059 A2 Pamphlet; International Publication No. 2001 / 09294 A1 Pamphlet; International Publication No. 2001 / 16349 A1 Pamphlet; International Publication No. 2001 / 36586 A2 Pamphlet; International Publication No. 2001 / 42433 A2 Pamphlet; International Publication No. 2001 / 47956 A2 Pamphlet; International Publication No. 2001 / 51620 A2 Pamphlet; International Publication No. 2001 / 59141 A2 Pamphlet; International Publication No. 2001 / 64852 A1 Pamphlet; International Publication No. 2001 / 83559 A2 Pamphlet; International Publication No. 2001 / 88107 A2 Pamphlet; International Publication No. 2002 / 10355 A2 Pamphlet; International Publication No. 2002 / 12511 A1 Pamphlet; International Publication No. 2002 / 40997 A2 Pamphlet; International Publication No. 2002 / 68589 A2 Pamphlet; International Publication No. 2002 / 68597 A2 Pamphlet; International Publication No. 2003 / 012071 A2 Pamphlet; International Publication No. 2003 / 014358 A2 Pamphlet; International Publication No. 2003 / 016535 A2 Pamphlet; International Publication No. 2003 / 018766 A2 Pamphlet; International Publication No. 2003 / 089614 A2 Pamphlet; International Publication No. 2004 / 080923 A2 Pamphlet; International Publication No. 2004 / 081171 A2 Pamphlet; International Publication No. 2004 / 091544 A2 Pamphlet; International Publication No. 2004 / 113551 A1 Pamphlet; International Publication No. 2005 / 001036 A2 Pamphlet; International Publication No. 2005 / 001064 A2 Pamphlet; International Publication No. 2005 / 003311 A2 Pamphlet;Same as Pamphlet No. 2005019443A2; Same as Pamphlet No. 2005045018A1; Same as Pamphlet No. 2005052148A2; Same as Pamphlet No. 2005054475A1; Same as Pamphlet No. 2005056787A1; Same as Pamphlet No. 2005073368A1; Same as Pamphlet No. 2005096804A2; Same as Pamphlet No. 2005108537A1; Same as Pamphlet No. 2005111203A2; Same as Pamphlet No. 2005113785A2; Same as Pamphlet No. 2005117756A2; Same as Pamphlet No. 2006002643A2; Same as Pamphlet No. 2006012899A1; Same as Pamphlet No. 2006012902A2; Same as Pamphlet No. 2006031554A2; Same as Pamphlet No. 2006037483A2; Same as Pamphlet No. 2006066594A2; Same as Pamphlet No. 2006066596A2; Same as Pamphlet No. 2006069290A2; Same as Pamphlet No. 2006117432A1; Same as Pamphlet No. 2006136159A2; Same as Pamphlet No. 2006136160A2; Same as Pamphlet No. 2007028088A2; Same as Pamphlet No. 2007071820A1; Same as Pamphlet No. 2007113292A2; Same as Pamphlet No. 2007146944A2; Same as Pamphlet No. 2007149699A2; Same as Pamphlet No. 2008000632A1; Same as Pamphlet No. 2008006881A1; Same as Pamphlet No. 2008015861A1; Same as Pamphlet No. 2008024372A2; Same as Pamphlet No. 2008057637A2; Same as Pamphlet No. 2008080093A2; Same as Pamphlet No. 2008112459A2; Same as Pamphlet No. 2008148845A2; Same as Pamphlet No. 2008153805A2; Same as Pamphlet No. 2008153934A2; Same as Pamphlet No. 2008153935A2; Same as Pamphlet No. 2009026397A2; Same as Pamphlet No. 2009037279A1; Same as Pamphlet No. 2009061379A2; Same as Pamphlet No. 2009062942A2; Same as Pamphlet No. 2009071550A1; Same as Pamphlet No. 2009074650A2; Same as Pamphlet No. 2009075682A1;Same as Pamphlet No. 2009076655A2; Same as Pamphlet No. 2009098229A2; Same as Pamphlet No. 2009100102A2; Same as Pamphlet No. 2009100138A2; Same as Pamphlet No. 2009100990A1; Same as Pamphlet No. 2009108941A2; Same as Pamphlet No. 2009112992A1; Same as Pamphlet No. 2009126773A1; Same as Pamphlet No. 2009133096A2; Same as Pamphlet No. 2009134670A2; Same as Pamphlet No. 2009149130A2; Same as Pamphlet No. 2009149271A2; Same as Pamphlet No. 2009149395A2; Same as Pamphlet No. 2009158694A1; Same as Pamphlet No. 2009158716A1; Same as Pamphlet No. 2010022518A1; Same as Pamphlet No. 2010027857A2; Same as Pamphlet No. 2010036515A1; Same as Pamphlet No. 2010036970A2; Same as Pamphlet No. 2010072224A1; Same as Pamphlet No. 2010072225A1; Same as Pamphlet No. 2010074999A1; Same as Pamphlet No. 2010102982A1; Same as Pamphlet No. 2010104675A1; Same as Pamphlet No. 2010115021A2; Same as Pamphlet No. 2010115156A2; Same as Pamphlet No. 2010121933A1; Same as Pamphlet No. 2010132157A2; Same as Pamphlet No. 2010135836A1; Same as Pamphlet No. 2010138754A1; Same as Pamphlet No. 2010148148A2; Same as Pamphlet No. 2011020852A1; Same as Pamphlet No. 2011041391A1; Same as Pamphlet No. 2011048852A1; Same as Pamphlet No. 2011057101A1; Same as Pamphlet No. 2011057140A1; Same as Pamphlet No. 2011057159A1; Same as Pamphlet No. 2011057163A2; Same as Pamphlet No. 2011066187A1; Same as Pamphlet No. 2011076123A1; Same as Pamphlet No. 2011076897A1; Same as Pamphlet No. 2011080352A1; Same as Pamphlet No. 2011080353A1; Same as Pamphlet No. 2011080354A1; Same as Pamphlet No. 2011082425A2;Same as Pamphlet No. 2011082429A1; Same as Pamphlet No. 2011127820A1; Same as Pamphlet No. 2011128712A1; Same as Pamphlet No. 2011153516A2; Same as Pamphlet No. 2012013197A2; Same as Pamphlet No. 2012016960A1; Same as Pamphlet No. 2012021399A1; Same as Pamphlet No. 2012021400A1; Same as Pamphlet No. 2012021883A2; Same as Pamphlet No. 2012027282A2; Same as Pamphlet No. 2012027374A2; Same as Pamphlet No. 2012027395A2; Same as Pamphlet No. 2012044835A1; Same as Pamphlet No. 2012044836A1; Same as Pamphlet No. 2012044915A2; Same as Pamphlet No. 2012088303A2; Same as Pamphlet No. 2012088467A2; Same as Pamphlet No. 2012089024A1; Same as Pamphlet No. 2012101206A2; Same as Pamphlet No. 2012106824A1; Same as Pamphlet No. 2012122308A2; Same as Pamphlet No. 2012125865A1; Same as Pamphlet No. 2012125925A2; Same as Pamphlet No. 2012127001A1; Same as Pamphlet No. 2012128260A1; Same as Pamphlet No. 2012129697A1; Same as Pamphlet No. 2012129699A1; Same as Pamphlet No. 2012134626A2; Same as Pamphlet No. 2012159007A1; Same as Pamphlet No. 2013001078A1; Same as Pamphlet No. 2013001087A2; Same as Pamphlet No. 2013023938A1; Same as Pamphlet No. 2013029496A1; Same as Pamphlet No. 2013034106A1; Same as Pamphlet No. 2013039776A1; Same as Pamphlet No. 2013055676A1; Same as Pamphlet No. 2013057141A2; Same as Pamphlet No. 2013057143A2; Same as Pamphlet No. 2013063460A2; Same as Pamphlet No. 2013074956A2; Same as Pamphlet No. 2013076253A1; Same as Pamphlet No. 2013082486A1; Same as Pamphlet No. 2013089889A2; Same as Pamphlet No. 2013096294A1; Same as Pamphlet No. 2013115305A1;Same as Pamphlet No. 2013148993A1; same as Pamphlet No. 2013160316A1; 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Pamphlet No. 2015094809A1; Pamphlet No. 2015105835A1; Pamphlet No. 2015109405A1; Pamphlet No. 2015110473A2; Pamphlet No. 2015118123A1; Pamphlet No. 2015143144A1; Pamphlet No. 2015143324A1; Pamphlet No. 2015144782A1; Pamphlet No. 2015144824A1; Pamphlet No. 2015150457A1; Pamphlet No. 2015157656A1; Pamphlet No. 2015162038A1; Pamphlet No. 2015187697A2; Pamphlet No. 2015189370A1; Pamphlet No. 2015189371A1; Pamphlet No. 2015189372A1; Pamphlet No. 2015200659A1; Pamphlet No. 2016020478A1; Pamphlet No. 2016029107A1; Pamphlet No. 2016030448A1; Pamphlet No. 2016036648A1; Pamphlet No. 2016036834A1; Pamphlet No. 2016040464A1; Pamphlet No. 2016062875A2; Pamphlet No. 2016066896A1; Pamphlet No. 2016079110A2; Pamphlet No. 2016079305A1; Pamphlet No. 2016087327A1; Pamphlet No. 2016087445A1; Pamphlet No. 2016090472A1; Pamphlet No. 2016090473A1; Pamphlet No. 2016090474A1; Pamphlet No. 2016095856A1; Pamphlet No. 2016100837A1; Pamphlet No. 2016109758A2; Pamphlet No. 2016117549A1;Same as Pamphlet No. 2016124651A1; 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[0181] In some embodiments, the protein of the present disclosure exhibits one or more peptidase activities belonging to EC3.4, such as aminopeptidase activity belonging to EC3.4.11, serine endopeptidase activity belonging to EC3.4.21 (e.g., chymotrypsin activity belonging to EC3.4.21.1, trypsin activity belonging to EC3.4.21.4, α-lytic endopeptidase activity belonging to EC3.4.21.12, glutamyl endopeptidase activity belonging to EC3.4.21.19, cucumisin activity belonging to EC3.4.21.25, chimase activity belonging to EC3.4.21.39, lysyl endopeptidase activity belonging to EC3.4.21.50, leucyl endopeptidase activity belonging to EC3.4.21.57, subtilisin activity belonging to 3.4.21.62), cysteine endopeptidase activity belonging to 3.4.22 (e.g., papain activity belonging to EC3.4.22.2, actinidin activity belonging to EC3.4.22.14, calicain activity belonging to EC3.4.22.30, ananain activity belonging to EC3.4.22.31, bromelain activity belonging to EC3.4.22.32, bromelain activity belonging to EC3.4.22.33, legumain activity belonging to EC3.4.22.34, zingipain activity belonging to EC3.4.22.67), aspartic endopeptidase activity belonging to EC3.4.23 (e.g., phytopepsin activity belonging to EC3.4.23.40) and / or metalloendopeptidase activity belonging to EC3.4.24 (e.g., bacillolysin belonging to EC3.4.24.28), and optionally, has 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 described herein as SEQ ID NOs: 80-88, or consists essentially of or consists of these sequences.

[0182] In some embodiments, the protein of the present disclosure exhibits serine endoprotease activity belonging to EC3.4.21 and optionally has 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 described herein as SEQ ID NOs: 80-86, or consists essentially of or consists of such amino acid sequences.

[0183] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% to one or more of SEQ ID NOs: 80-81; b) a polypeptide having a sequence identity 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% to the mature polypeptide of any one of SEQ ID NOs: 80-81; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 171-172 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 80-81 by substitution, deletion or insertion of one or more amino acids; 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; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), wherein the polypeptide is selected from the group consisting of fragments having serine endopeptidase activity belonging to EC 3.4.21. Examples of proteins having serine endopeptidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NOs: 80-81 are described herein as SEQ ID NOs: 49913-50777.

[0184] 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, Dichomitus, Ganoderma, Grifola, Lenzites, Meripilus, Neolentinus, Nocardiopsis, Polyporus or Trametes serine endopeptidase or a fragment / mutant / variant of a native Cinereomyces, Dichomitus, Ganoderma, Grifola, Lenzites, Meripilus, Neolentinus, Nocardiopsis, Polyporus or Trametes serine endopeptidase.

[0185] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 82; b) A polypeptide having a sequence identity 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% with any one of the mature polypeptides of SEQ ID NO: 82; c) A polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 173 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 82 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) - f), The polypeptide has glutamyl endopeptidase activity belonging to EC 3.4.21.19 and is selected from the group consisting of fragments. Examples of proteins having glutamyl endopeptidase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 82 are described herein as SEQ ID NOs: 50778 - 50953.

[0186] 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 native Bacillus glutamyl endopeptidase.

[0187] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NOs: 83-87; b) a polypeptide having a sequence identity 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% with the mature polypeptide of any one of SEQ ID NOs: 83-87; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NOs: 174-178, or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 83-87 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NOs: 83 to 87 by substitution, deletion, or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide is selected from the group consisting of fragments having subtilisin activity belonging to EC 3.4.21.62. Examples of proteins having an amino acid sequence that exhibits subtilisin activity and is at least 70% identical to one or more of SEQ ID NOs: 83 to 87 are described herein as SEQ ID NOs: 50954 to 70838.

[0188] In some embodiments, the protein is derived from Alkalihalobacillus, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus. For example, in some embodiments, the protein is a native Alkalihalobacillus, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus subtilisin, or a fragment / mutant / variant of a native Alkalihalobacillus, Aspergillus, Bacillus, Brevia, Geomicrobium, Homo, Hordeum, Lederbergia, Saccharomyces, Shouchella, or Thermus subtilisin.

[0189] In some embodiments, the protein is a) a polypeptide having a sequence identity 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% with one or more of SEQ ID NO: 88; b) a polypeptide having a sequence identity 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% with any one of the mature polypeptides of SEQ ID NO: 88; c) a polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NO: 179 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 88 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 88 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having bacillolysin activity belonging to EC3.4.24.28. Examples of proteins having an amino acid sequence that exhibits bacillolysin activity and is at least 70% identical to one or more of SEQ ID NO: 88 are described herein as SEQ ID NOs: 70839 to 71903.

[0190] In some embodiments, the protein is derived from the genus Bacillus. For example, in some embodiments, the protein is native Bacillus bacillolysin or a fragment / mutant / variant of native Bacillus bacillolysin.

[0191] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more peptidase activities belonging to EC 3.4. For example, Canadian Patent No. 2829859A1; Chinese Patent No. 102676561A; No. 102703482A; No. 103013960A; No. 103243081A; No. 103255156A; No. 103602653A; No. 104232610A; No. 105132397A; No. 105176951A; No. 106350530 - Specification; No. 106801048A; No. 107384897A; No. 107828765A; No. 107937372A; No. 107937374A; No. 108004220 - No.; No. 108359659A; No. 108384771A; No. 108570461A; No. 108570462A; No. 109456957A; CN109593746 - Specification; Chinese Patent No. 110746494A; No. 110777136A; No. 110819612A; No. 110862979A; No. 110923221A; No. 110923222 - Specification; No. 111004794A; No. 111334494A; No. 111575265A; No. 111893126A; No. 111909979A; CN112301023 - No.; Chinese Patent No. 112458072A; No. 112501149A; No. 112574978A; No. 112662652A; No. 112662653A; CN113528493 - No.; Chinese Patent No. 113699138A; No. 113832130A; No. 113832131A; No. 113862244A; No. 114107266A; No. 114317502 - No.; No. 114540330A; No. 114561375A; No. 114574469A; No. 114591935A; No. 114774396A; CN114806990 Specification;Same as the specification of Patent No. 114836408A; same as the specification of Patent No. 114908074A; same as the specification of Patent No. 114958897A; same as the specification of Patent No. 115029337A; same as the specification of Patent No. 115074347A; Specification of CN115247166; Specification of Chinese Patent No. 1361279A; same as the specification of Patent No. 1814746A; same as the specification of Patent No. 1814755A; same as the specification of Patent No. 1995343A; Specification of German Patent No. 102006022224A1; same as the specification of Patent No. 102007044415-1; same as the specification of Patent No. 102007049830A1; same as the specification of Patent No. 102007051092A1; same as the specification of Patent No. 102008059446A1; same as the specification of Patent No. 102008059447A1; same as the specification of Patent No. 102009029513A1; same as the specification of Patent No. 102010028951A1; same as the specification of Patent No. 102011005354A1; same as the specification of Patent No. 102011118032A1; same as the specification of Patent No. 102012215642A1; same as the specification of Patent No. 102012220101A1; same as the specification of Patent No. 102013219467A1; same as the specification of Patent No. 102013221206A1; same as the specification of Patent No. 102014212643A1; same as the specification of Patent No. 102014224825A1; same as the specification of Patent No. 102014226681A1; same as the specification of Patent No. 102015223270A1; same as the specification of Patent No. 102016204814A1; same as the specification of Patent No. 102016204815A1; same as the specification of Patent No. 102016208463A1; same as the specification of Patent No. 102016210628A1; same as the specification of Patent No. 102017215628A1; same as the specification of Patent No. 102017215629A1; same as the specification of Patent No. 102017215631A1; same as the specification of Patent No. 102017223275A1; same as the specification of Patent No. 102018004206A1; same as the specification of Patent No. 102018004207A1; same as the specification of Patent No. 102019111047A1; same as the specification of Patent No. 102019111057A1; same as the specification of Patent No. 102019111075A1; same as the specification of Patent No. 102019210806A1; same as the specification of Patent No. 102020105720A1; same as the specification of Patent No. 102020105721A1; same as the specification of Patent No. 102020205381A1; same as the specification of Patent No. 102020205400A1; same as the specification of Patent No. 10260903A1; same as the specification of Patent No. 19530816A1; same as the specification of Patent No. 3821491A; same as the specification of Patent No. 4224125A1;Same as Japanese Patent No. 4411223A1; European Patent No. 1160327A2; European Patent No. 133756A; European Patent No. 2100948A1; European Patent No. 2607468A1; European Patent No. 3106508A1; European Patent No. 3275988A1; European Patent No. 3301155A1; European Patent No. 3309244A1; European Patent No. 3323875A1; European Patent No. 3339423A1; European Patent No. 3660146A1; European Patent No. 3660151A1; European Patent No. 398539A; European Patent No. 405901A; European Patent No. 405902A; European Patent No. 415296A; European Patent No. 416967A; European Patent No. 430637A; European Patent No. 443476A; European Patent No. 482879A; European Patent No. 516200A1; European Patent No. 571049A1; European Patent No. 687733A1; Japanese Unexamined Patent Application Publication No. 01-137972; No. 02-076586; No. 11-137282; Japanese Unexamined Patent Application Publication No. 2004-043660; No. 2004-313043; No. 2008-022828; No. 2011-234685; No. 2016-121081; No. 2017-079639; No. 2022-045888; US Patent Application Publication No. 2004091474A1; No. 2004197894A1; No. 2004223962A1; No. 2009087888A1; No. 2012067373A1; No. 2013123162A1; No. 2015125925A1; No. 2016032267A1; No. 2019185788A1; No. 2019185789A1; No. 2020306342A1; No. 2021122997A1; No. 2022098524A1; No. 4980288A; No. 5260207A; No. 5316935A; No. 5316941A; No. 5371008A; No. 5472855A; No. 5652136A; No. 5677272A; No. 5679630A; No. 5719021A;Same as the specification of Patent No. 6017871A; same as No. 6271012-1; same as the specification of Patent No. 6312936B1; same as the specification of Patent No. 6440717B1; Pamphlet of International Publication No. 200022103A1; Pamphlet of International Publication No. 200024924A2; Pamphlet of International Publication No. 200037599A1; Pamphlet of International Publication No. 200037621A1; Pamphlet of International Publication No. 200037622A1; Pamphlet of International Publication No. 200037623A1; Pamphlet of International Publication No. 200037624A1; Pamphlet of International Publication No. 200037625A1; Pamphlet of International Publication No. 200037626A1; Pamphlet of International Publication No. 200037627A1; Pamphlet of International Publication No. 200071683A1; Pamphlet of International Publication No. 200071684A1; Pamphlet of International Publication No. 200071685A1; Pamphlet of International Publication No. 200071686A1; Pamphlet of International Publication No. 200071687A1; Pamphlet of International Publication No. 200071688A1; Pamphlet of International Publication No. 200071689A1; Pamphlet of International Publication No. 200071690A1; Pamphlet of International Publication No. 200071691A1; Pamphlet of International Publication No. 200116285A2; Pamphlet of International Publication No. 200168821A2; Pamphlet of International Publication No. 200175087A2; Pamphlet of International Publication No. 200183559A2; Pamphlet of International Publication No. 200210183A1; Pamphlet of International Publication No. 200216547A2; Pamphlet of International Publication No. 200218588A1; Pamphlet of International Publication No. 200222796A1; Pamphlet of International Publication No. 200231133A1; Pamphlet of International Publication No. 200240997A2; Pamphlet of International Publication No. 200277289A1; Pamphlet of International Publication No. 200288340A2; Pamphlet of International Publication No. 2003038082A2; Pamphlet of International Publication No. 2003054184A1; Pamphlet of International Publication No. 2003054185A1; Pamphlet of International Publication No. 2003055974A2; Pamphlet of International Publication No. 2003057713A2; Pamphlet of International Publication No. 2003062381A2; Pamphlet of International Publication No. 2003093453A2;International Publication No. WO 2004 / 003186 A2 Pamphlet; International Publication No. WO 2004 / 016752 A2 Pamphlet; International Publication No. WO 2004 / 042049 A1 Pamphlet; International Publication No. WO 2004 / 064744 A2 Pamphlet; International Publication No. WO 2004 / 099401 A1 Pamphlet; International Publication No. WO 2004 / 111219 A1 Pamphlet; International Publication No. WO 2005 / 024002 A1 Pamphlet; International Publication No. WO 2005 / 035747 A1 Pamphlet; International Publication No. WO 2005 / 078074 A2 Pamphlet; International Publication No. WO 2005 / 079826 A1 Pamphlet; International Publication No. WO 2005 / 095592 A2 Pamphlet; International Publication No. WO 2005 / 115445 A1 Pamphlet; International Publication No. WO 2005 / 118793 A2 Pamphlet; International Publication No. WO 2005 / 123911 A2 Pamphlet; International Publication No. WO 2005 / 123914 A1 Pamphlet; International Publication No. WO 2005 / 124012 A1 Pamphlet; International Publication No. WO 2006 / 088325 A1 Pamphlet; International Publication No. WO 2006 / 136159 A2 Pamphlet; International Publication No. WO 2006 / 136160 A2 Pamphlet; International Publication No. WO 2007 / 006305 A1 Pamphlet; International Publication No. WO 2007 / 019858 A2 Pamphlet; International Publication No. WO 2007 / 044993 A2 Pamphlet; International Publication No. WO 2007 / 080197 A2 Pamphlet; International Publication No. WO 2007 / 122175 A1 Pamphlet; International Publication No. WO 2008 / 010925 A2 Pamphlet; International Publication No. WO 2008 / 112258 A2 Pamphlet; International Publication No. WO 2008 / 141281 A1 Pamphlet; International Publication No. WO 2008 / 153934 A2 Pamphlet; International Publication No. WO 2008 / 153935 A2 Pamphlet; International Publication No. WO 2009 / 005647 A2 Pamphlet; International Publication No. WO 2009 / 021867 A2 Pamphlet; International Publication No. WO 2009 / 058518 A1 Pamphlet; International Publication No. WO 2009 / 071550 A1 Pamphlet; International Publication No. WO 2009 / 074650 A2 Pamphlet; International Publication No. WO 2009 / 149144 A2 Pamphlet; International Publication No. WO 2009 / 149145 A2 Pamphlet; International Publication No. WO 2009 / 149200 A2 Pamphlet; International Publication No. WO 2010 / 056640 A2 Pamphlet; International Publication No. WO 2010 / 056653 A2 Pamphlet; International Publication No. WO 2010 / 056671 A1 Pamphlet;Pamphlet of International Publication No. WO 2010 / 078462 A1; Pamphlet of International Publication No. WO 2010 / 123754 A1; Pamphlet of International Publication No. WO 2011 / 014278 A1; Pamphlet of International Publication No. WO 2011 / 036263 A1; Pamphlet of International Publication No. WO 2011 / 072099 A2; Pamphlet of International Publication No. WO 2011 / 072117 A1; Pamphlet of International Publication No. WO 2011 / 091370 A1; Pamphlet No.; International Publication No. WO 2011 / 110625 A1; International Publication No. WO 2011 / 130076 A1; International Publication No. WO 2011 / 130222 A2; International Publication No. WO 2011 / 140316 A1; International Publication No. WO 2011 / 140364 A1; International Publication No. WO 2012 / 080202 A1; International Publication No. WO 2012 / 151480 A2; International Publication No. WO 2012 / 151534 A1; International Publication No. WO 2013 / 086219 A1; International Publication No. WO 2013 / 092635 A1; International Publication No. WO 2013 / 110766 A1; International Publication No. WO 2013 / 159032 A1; International Publication No. WO 2014 / 037438 A1; International Publication No. WO 2014 / 055778 A2; International Publication No. WO 2014 / 055782 A1; International Publication No. WO 2014 / 081884 A1; International Publication No. WO 2014 / 194034 A2; International Publication No. WO 2014 / 207228 A1; International Publication No. WO 2015 / 038792 A1; International Publication No. WO 2015 / 048332 A2; International Publication No. WO 2015 / 048339 A2; International Publication No. WO 2015 / 065871 A1; International Publication No. WO 2015 / 089441 A1; International Publication No. WO 2015 / 089447 A1; International Publication No. WO 2015 / 143360 A2; International Publication No. WO 2015 / 144932 A1; International Publication No. WO 2015 / 144936 A1; International Publication No. WO 2015 / 185689 A1; International Publication No. WO 2016 / 040464 A1; International Publication No. WO 2016 / 046234 A2; International Publication No. WO 2016 / 069552 A1; International Publication No. WO 2016 / 069557 A1; International Publication No. WO 2016 / 069563 A1; International Publication No. WO 2016 / 069569 A2; International Publication No. WO 2016 / 097405 A1; International Publication No. WO 2016 / 145428 A1; International Publication No. WO 2016 / 164096 A1; International Publication No. WO 2016 / 174234 A2; International Publication No. WO 2016 / 180928 A1;International Publication No. WO 2016 / 183509 A1 Pamphlet; International Publication No. WO 2016 / 203064 A2 Pamphlet; International Publication No. WO 2016 / 205710 A1 Pamphlet; International Publication No. WO 2016 / 205755 A1 Pamphlet; International Publication No. WO 2017 / 006266 A1 Pamphlet; International Publication No. WO 2017 / 050291 A1 Pamphlet; International Publication No. WO 2017 / 081274 A1 Pamphlet; International Publication No. WO 2017 / 089093 A1 Pamphlet; International Publication No. WO 2017 / 089366 A1 Pamphlet; International Publication No. WO 2017 / 089456 A1 Pamphlet; International Publication No. WO 2017 / 106676 A1 Pamphlet; International Publication No. WO 2017 / 177153 A1 Pamphlet; International Publication No. WO 2017 / 189720 A1 Pamphlet; International Publication No. WO 2017 / 192692 A1 Pamphlet; International Publication No. WO 2017 / 210295 A1 Pamphlet; International Publication No. WO 2017 / 219011 A1 Pamphlet; International Publication No. WO 2018 / 015303 A1 Pamphlet; International Publication No. WO 2018 / 015304 A1 Pamphlet; International Publication No. WO 2018 / 118917 A1 Pamphlet; International Publication No. WO 2018 / 118950 A1 Pamphlet; International Publication No. WO 2018 / 161899 A1 Pamphlet; International Publication No. WO 2018 / 188667 A1 Pamphlet; International Publication No. WO 2018 / 222990 A1 Pamphlet; International Publication No. WO 2019 / 048486 A1 Pamphlet; International Publication No. WO 2019 / 048495 A1 Pamphlet; International Publication No. WO 2019 / 108599 A1 Pamphlet; International Publication No. WO 2019 / 180111 A1 Pamphlet; International Publication No. WO 2019 / 238761 A1 Pamphlet; International Publication No. WO 2019 / 245704 A1 Pamphlet; International Publication No. WO 2019 / 245705 A1 Pamphlet; International Publication No. WO 2019 / 245838 A1 Pamphlet; International Publication No. WO 2019 / 245839 A1 Pamphlet; International Publication No. WO 2020 / 002255 A1 Pamphlet; International Publication No. WO 2020 / 007863 A1 Pamphlet; International Publication No. WO 2020 / 023411 A1 Pamphlet; International Publication No. WO 2020 / 076697 A1 Pamphlet; International Publication No. WO 2020 / 112599 A1 Pamphlet; International Publication No. WO 2020 / 114968 A1 Pamphlet; International Publication No. WO 2020 / 156419 A1 Pamphlet; International Publication No. WO 2020 / 169564 A1 Pamphlet;International Publication No. WO 2020 / 176443 A1 Pamphlet; International Publication No. WO 2020 / 188095 A1 Pamphlet; International Publication No. WO 2020 / 200198 A1 Pamphlet; International Publication No. WO 2020 / 201403 A1 Pamphlet; International Publication No. WO 2020 / 207944 A1 Pamphlet; International Publication No. WO 2020 / 243738 A1 Pamphlet; International Publication No. WO 2021 / 013685 A1 Pamphlet; International Publication No. WO 2021 / 013686 A1 Pamphlet; International Publication No. WO 2021 / 025872 A1 Pamphlet; International Publication No. WO 2021 / 030400 A1 Pamphlet; International Publication No. WO 2021 / 080948 A2 Pamphlet; International Publication No. WO 2021 / 119304 A1 Pamphlet; International Publication No. WO 2021 / 122120 A2 Pamphlet; International Publication No. WO 2021 / 130167 A1 Pamphlet; International Publication No. WO 2021 / 133701 A1 Pamphlet; International Publication No. WO 2021 / 148364 A1 Pamphlet; International Publication No. WO 2021 / 209548 A1 Pamphlet; International Publication No. WO 2021 / 230359 A1 Pamphlet; International Publication No. WO 2021 / 231621 A1 Pamphlet; International Publication No. WO 2021 / 231623 A1 Pamphlet; International Publication No. WO 2021 / 248045 A2 Pamphlet; International Publication No. WO 2022 / 043547 A1 Pamphlet; International Publication No. WO 2022 / 043563 A1 Pamphlet; International Publication No. WO 2022 / 043745 A1 Pamphlet; International Publication No. WO 2022 / 106400 A1 Pamphlet; International Publication No. WO 2022 / 129166 A1 Pamphlet; International Publication No. WO 2022 / 171120 A1 Pamphlet; International Publication No. WO 2022 / 171667 A1 Pamphlet; International Publication No. WO 2022 / 175263 A2 Pamphlet; International Publication No. WO 2022 / 225696 A2 Pamphlet; International Publication No. WO 2022 / 226158 A2 Pamphlet; International Publication No. WO 2022 / 261003 A1 Pamphlet; International Publication No. WO 2023 / 288294 A1 Pamphlet; International Publication No. WO 88 / 07581 Specification; International Publication No. WO 91 / 02792 Specification; International Publication No. WO 91 / 06637 Specification; International Publication No. WO 92 / 11348 A1 Pamphlet; International Publication No. WO 92 / 11357 A1 Pamphlet; International Publication No. WO 92 / 21760 A1 Pamphlet; International Publication No. WO 93 / 07276 A1 Pamphlet; International Publication No. WO 94 / 02618 A1 Pamphlet;Please refer to International Publication No. WO94 / 18329A2; International Publication No. WO94 / 23053A1; International Publication No. WO95 / 07991A2; International Publication No. WO95 / 10591A1; International Publication No. WO95 / 10615A1; International Publication No. WO95 / 23221A1; International Publication No. WO95 / 23614A1; International Publication No. WO95 / 30011A2; International Publication No. WO96 / 28557A2; International Publication No. WO96 / 28566A2; International Publication No. WO96 / 34935A2; International Publication No. WO96 / 34946A1; International Publication No. WO98 / 20115A1; International Publication No. WO98 / 30682A1; International Publication No. WO98 / 55634A1; International Publication No. WO99 / 20770A2; International Publication No. WO99 / 27082A1; International Publication No. WO99 / 67370A1.;

[0192] In some embodiments, the protein of the present disclosure exhibits one or more hydrolase activities belonging to EC3.5, including amidohydrolase and amidase activities belonging to EC3.5.1 (e.g., asparaginase activity belonging to EC3.5.1.1, 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, N-acetylglucosaminidase activity belonging to EC3.5.1.33, D-glutaminase activity belonging to 3.5.1.35, glutaminase (asparaginase) activity belonging to 3.5.1.38, chitin deacetylase activity belonging to 3.5.1.41, peptidyl-glutaminase activity belonging to 3.5.1.43, protein-glutamine glutaminase activity belonging to 3.5.1.44, pentanamidase activity belonging to 3.5.1.50, peptidoglycan N-acetylglucosaminidase belonging to EC3.5.1.104), amidase and deiminase activities belonging to EC3.5.3 (e.g., arginase activity belonging to EC3.5.3.1, arginine deiminase activity belonging to EC3.5.3.6, D-arginase activity belonging to EC3.5.3.10, protein-arginine deiminase activity belonging to EC3.5.3.15) and / or deiminase activities belonging to EC3.5.4 (e.g., cytosine deaminase activity belonging to EC3.5.4.1, adenine deaminase activity belonging to EC3.5.4.2, guanine deaminase activity belonging to EC3.5.4.3, adenosine deaminase activity belonging to EC3.5.4.4), and optionally, has 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 described herein as SEQ ID NOs: 89-90, or consists essentially of or consists of these amino acid sequences.

[0193] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NOs: 89-90; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one of SEQ ID NOs: 89-90; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NOs: 180-181 or one or more of these cDNA sequences; d) a polypeptide derived from any one of SEQ ID NOs: 89-90 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide is selected from the group consisting of fragments having asparaginase activity belonging to EC 3.5.1.1. Examples of proteins having an amino acid sequence that exhibits asparaginase activity and is at least 70% identical to one or more of SEQ ID NOs: 89 to 90 are described herein as SEQ ID NOs: 71904 to 72141.

[0194] In some embodiments, the protein is derived from the genus Aspergillus. For example, in some embodiments, the protein is a native Aspergillus asparaginase or a fragment / mutant / variant of a native Aspergillus asparaginase.

[0195] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more hydrolase activities belonging to EC 3.5. See, for example, Chinese Patent No. 109486689A; European Patent No. 2295582A2; US Patent No. 7504490B1; International Publication No. 2004032648A1 pamphlet; No. 2008110513A1 pamphlet; No. 2008128974A1 pamphlet; No. 2008128975A1 pamphlet; No. 2011134916A1 pamphlet; No. 2012068047A2 pamphlet; No. 2014027062A1 pamphlet; No. 2014027063A1 pamphlet; No. 2014147189A1 pamphlet.

[0196] In some embodiments, the proteins of the present disclosure exhibit one or more lyase activities belonging to Enzyme Classification Number 4 (EC4). For example, in some embodiments, the proteins of the present disclosure are capable of: a) preventing / treating / suppressing / eliminating / reducing the deleterious effects of parasitism / infection by various pests including, but not limited to, phytopathogenic pests such as spider mites, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses, and weeds; b) reducing one or more aspects of disease severity in plants infested with one or more phytopathogenic pests; c) pretreating surfaces / substances susceptible to parasitism / infection by pests; d) cleaning surfaces / substances parasitized / infected by pests; e) improving the environment in which plants are grown; f) enhancing nutrient availability in the plant growth environment; g) reducing the amount of exogenous chemical fertilizers required to obtain a desired result; h) improving the growth, development, and yield characteristics of plants; 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 reducing the tolerance / phytotoxicity induced by chemical pesticides.

[0197] In some embodiments, the proteins of the present disclosure exhibit one or more carbon-carbon lyase activities belonging to EC4.1, such as carboxy-lyase activities belonging to EC4.1.1 (e.g., aspartate-1-decarboxylase activity belonging to EC4.1.1.11, aspartate 4-decarboxylase activity belonging to EC4.1.1.12, valine decarboxylase activity belonging to EC4.1.1.14, glutamate decarboxylase activity belonging to EC4.1.1.15, lysine decarboxylase activity belonging to EC4.1.1.18, arginine decarboxylase activity belonging to EC4.1.1.19, histidine decarboxylase activity belonging to EC4.1.1.22, tyrosine decarboxylase activity belonging to EC4.1.1.25, phenylalanine decarboxylase activity belonging to EC4.1.1.53, methionine decarboxylase activity belonging to EC4.1.1.57, L-tryptophan decarboxylase activity belonging to EC4.1.1.105) and / or carbon-carbon lyase activities belonging to EC4.1.99 (tryptophanase activity belonging to EC4.1.99.1, tyrosine phenol-lyase activity belonging to EC4.1.99.2).

[0198] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more carbon-carbon lyase activities belonging to EC4.1.

[0199] In some embodiments, the protein of the present disclosure exhibits one or more carbon-oxygen lyase activities belonging to EC4.2, such as polysaccharide lyase activity belonging to EC4.2.2 (for example, pectate lyase belonging to EC4.2.2.2, pectin lyase activity belonging to EC4.2.2.10, glucan lyase activity belonging to EC4.2.2.13, gellan lyase activity belonging to EC4.2.2.25, oligo-arginase lyase activity belonging to EC4.2.2.26, pectin-monosaccharide-lyase activity belonging to EC4.2.2.27), and optionally, has an amino acid sequence with 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% identity to the amino acid sequences described herein as SEQ ID NO: 91 and 55, or consists essentially of or consists of these amino acid sequences.

[0200] In some embodiments, the protein is 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; 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; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 182 or one or more of this cDNA sequence; d) A polypeptide derived from any one of SEQ ID NO: 91 by substitution, deletion or insertion of one or more amino acids; 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; f) A polypeptide derived from any one of the polypeptides of a) to e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) A fragment of any one of the polypeptides of a) to f), wherein the polypeptide has pectate lyase activity belonging to EC 4.2.2.2 and is selected from the group consisting of fragments. Examples of proteins having pectate lyase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 91 are described herein as SEQ ID NOs: 72142 to 72143.

[0201] In some embodiments, the protein is derived from the genus 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.

[0202] In some embodiments, the protein is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one or more of SEQ ID NO: 55; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one of the mature polypeptides of SEQ ID NO: 55; c) a polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with SEQ ID NO: 146 or one or more of this cDNA sequence; d) a polypeptide derived from any one of SEQ ID NO: 55 by substitution, deletion or insertion of one or more amino acids; e) a polypeptide derived from any one of the mature polypeptides of SEQ ID NO: 55 by substitution, deletion or insertion of one or more amino acids; f) a polypeptide derived from any one of the polypeptides of a) - e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) a fragment of any one of the polypeptides of a) - f), The polypeptide is selected from the group consisting of fragments having pectin lyase activity belonging to EC 4.2.2.10. Examples of proteins exhibiting pectin lyase activity and having an amino acid sequence that is at least 70% identical to one or more of SEQ ID NO: 55 are described herein as SEQ ID NOs: 45409 to 45436.

[0203] In some embodiments, the protein is derived from the genus Aspergillus, Botrytis, Neosartorya, Penicillium or Pseudomyllocerus. For example, in some embodiments, the protein is a native Aspergillus, Botrytis, Neosartorya, Penicillium or Pseudomyllocerus pectin lyase or a fragment / mutant / variant of a native Aspergillus, Botrytis, Neosartorya, Penicillium or Pseudomyllocerus pectin lyase.

[0204] One of ordinary skill in the art will understand methods for identifying, isolating, characterizing, producing, recovering and formulating proteins having one or more carbon-oxygen lyase activities belonging to EC 4.2. See, for example, U.S. Patent Application Publication No. 2015045535A1, WO 9927083A1.

[0205] In some embodiments, the protein of the present disclosure exhibits one or more carbon-nitrogen lyase activities belonging to EC4.3, such as ammonia-lyase activity belonging to EC4.3.1 (e.g., aspartate ammonia-lyase activity belonging to EC4.3.1.1, histidine ammonia-lyase activity belonging to EC4.3.1.3, L-serine ammonia-lyase activity belonging to EC4.3.1.17, D-serine ammonia-lyase activity belonging to EC4.3.1.18, threonine ammonia-lyase activity belonging to EC4.3.1.19, tyrosine ammonia-lyase activity belonging to EC4.3.1.23, phenylalanine ammonia-lyase activity belonging to EC4.3.1.24, phenylalanine / tyrosine ammonia-lyase activity belonging to EC4.3.1.25, L-lysine cyclodeaminase activity belonging to EC4.3.1.28, L-tryptophan ammonia-lyase activity belonging to EC4.3.1.31).

[0206] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more carbon-nitrogen lyase activities belonging to EC4.3.

[0207] In some embodiments, the protein of the present disclosure exhibits one or more carbon-sulfur lyase activities belonging to EC4.4, such as cysteine lyase activity belonging to EC4.4.1.10, methionine gamma-lyase activity belonging to EC4.4.1.11, L-cysteine desulfurase belonging to EC4.4.1.28, L-cysteine β-lyase activity belonging to EC4.4.1.35.

[0208] Those skilled in the art will understand methods for identifying, isolating, characterizing, producing, recovering, and formulating proteins having one or more carbon-sulfur lyase activities belonging to EC4.4.

[0209] In some embodiments, the protein comprises, consists essentially of, or consists of wild-type polypeptides. For example, in some embodiments, the protein comprises, consists essentially of, or consists of one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 or mature polypeptides thereof 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 wild-type polypeptides.

[0210] In some embodiments, the protein comprises, consists essentially of, or consists of variant polypeptides. For example, in some embodiments, the protein comprises, consists essentially of, or consists of one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 or mature polypeptides thereof 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 variant polypeptides.

[0211] In some embodiments, the protein comprises, consists essentially of, or consists of a catalytic domain, a binding module, and a linker between the enzyme domain and the binding module.

[0212] The present disclosure extends to proteins capable of exhibiting two, three, four, five or more distinct catalytic activities, including but not limited to proteins having two or more distinct catalytic activities inherently and fusion proteins comprising two or more polypeptides having distinct catalytic activities.

[0213] In some embodiments, the protein is a hybrid protein.

[0214] In some embodiments, the protein comprises two or more catalytic domains.

[0215] In some embodiments, the protein comprises two or more binding modules.

[0216] In some embodiments, the protein is a fusion protein (e.g., a fusion protein comprising a first polypeptide having a first enzyme activity and a second polypeptide having a second enzyme activity).

[0217] In some embodiments, the protein is a fusion protein comprising a first polypeptide and a second polypeptide, the second polypeptide being distinct from the first polypeptide, and the first polypeptide is a) a polypeptide having a sequence identity 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% with any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or the cDNA sequences thereof; 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; e) A mature 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; f) A polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; g) Selected from the group consisting of fragments of any one of the polypeptides of a)-f), optionally, the second polypeptide is, h) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; i) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; j) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or the cDNA sequence thereof; k) A mature 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; l) 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; A polypeptide derived from any one of the polypeptides of (m) to (l), wherein the N-terminus and / or C-terminus is extended by the addition of one or more amino acids; n) It is selected from the group consisting of fragments of any one of the polypeptides of (h) to (m).

[0218] In a preferred embodiment, the protein of the present disclosure comprises, consists essentially of, or consists of any one of the amino acid sequences of SEQ ID NOs: 1 to 91, 45906, 72144, 72147, and 72149, or their mature polypeptides.

[0219] In a preferred embodiment, the protein of the present disclosure is encoded by a polynucleotide that comprises, consists essentially of, or consists of any one of SEQ ID NOs: 92 to 182, 72145 to 72146, 72148, and 72150, or their cDNA.

[0220] In some embodiments, the protein of the present disclosure comprises, consists essentially of, or consists of a fragment of any one of SEQ ID NOs: 1 to 91, 45906, 72144, 72147, and 72149, or their mature polypeptides. For example, the protein can be a fragment of any one of SEQ ID NOs: 1 to 91, 45906, 72144, 72147, and 72149, or their mature peptides, and the fragment can contain 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.

[0221] As described above, in some embodiments, the protein of the present disclosure is one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or has 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), 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 amino acids) 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 amino acids). The amino acid changes can 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; typically small deletions of 1-30 amino acids; small amino-terminal or carboxy-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 tract, an antigenic epitope, or a binding module.

[0222] Important 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, a single alanine mutation is incorporated for each residue in the molecule, and the resulting molecule is evaluated for hexosaminidase activity to identify amino acid residues essential for the activity of the molecule. See also Hilton et al., 1996, J. Biol. Chem. 271:4699-4708. Also, the active site of an enzyme or other biological interaction can be determined by physical analysis of the structure measured by techniques such as nuclear magnetic resonance, crystal structure analysis, electron diffraction, or photoaffinity labeling, in combination with mutations of the putative contact site amino acids. See, for example, 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. Identification of essential amino acids can also be inferred from alignment with related polypeptides and / or from sequence homology and conserved catalytic mechanisms with related polypeptides or polypeptides / proteins derived from a common ancestor within a polypeptide or protein family (typically having similar three-dimensional structures, functions, and significant sequence similarity). In addition, or alternatively, protein structure prediction tools can be used for protein structure modeling to identify essential amino acids and / or the active site of a polypeptide. See, for example, Jumper et al., 2021, “Highly accurate protein structure prediction with AlphaFold”, Nature 596:583-589.

[0223] Substitutions, deletions, and / or insertions of one or more amino acids can be made and tested using known mutagenesis, recombination, and / or shuffling methods, followed by related 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; International Publication No. WO 95 / 17413 pamphlet; or International Publication No. WO 95 / 22625 pamphlet. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30:10832-10837; U.S. Patent No. 5,223,409; International Publication No. WO 92 / 06204 pamphlet), and site-directed mutagenesis (Derbyshire et al., 1986, Gene 46:145; Ner et al., 1988, DNA 7:127).

[0224] The mutagenesis / shuffling method can be combined with a high-throughput automated screening method to detect the activity of a cloned, mutagenized polypeptide expressed by a host cell (Ness et al., 1999, Nature Biotechnology 17:893-896). The mutagenized DNA molecule encoding the active polypeptide can be recovered from the host cell and easily sequenced using standard methods in the art. These methods allow for the rapid determination of the importance of individual amino acid residues within the polypeptide.

[0225] Table 1 provides a non-exhaustive list of proteins useful in the compositions and methods of the present disclosure.

[0226] [Table 1]

[0227]

Table 2

[0228]

Table 3

[0229]

Table 4

[0230]

Table 5

[0231]

Table 6

[0232] The protein of the present disclosure can be derived from microorganisms of any genus.

[0233] In some embodiments, the protein is derived from and / or obtained from Gram-negative bacteria such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma.

[0234] In some embodiments, the protein is from the genus Alkalihalobacillus (e.g., A. akibai, A. clausii), the genus 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, B. subtilis, B. thuringiensis), the genus Clostridium, the genus Effusibacillus (e.g., E. pohliae), the genus Enterococcus, the genus Geobacillus (e.g., G. stearothermophilus), the genus Lactobacillus, the genus Lactococcus, the genus Lederbergia (e.g., L. lenta), the genus Neobacillus (e.g., N. novalis), the genus Nocardiopsis, the genus Oceanobacillus (e.g., O. barbara), the genus Staphylococcus, the genus Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, S.derived from Gram-positive bacteria such as Actinobacillus pleuropneumoniae, Actinomyces pyogenes, Arcanobacterium pyogenes, Bacillus anthracis, Bacillus cereus, Bacillus subtilis, Brevibacterium linens, Corynebacterium glutamicum, Corynebacterium pseudotuberculosis, Enterococcus faecalis, Enterococcus faecium, Erysipelothrix rhusiopathiae, Lactobacillus casei, Lactobacillus plantarum, Listeria monocytogenes, Micrococcus luteus, Mycobacterium bovis, Mycobacterium tuberculosis, Mycoplasma bovis, Mycoplasma mycoides, Mycoplasma pneumoniae, Nocardia asteroides, Propionibacterium acnes, Rhodococcus equi (R. equi subsp. equi and R. equi subsp. Zooepidemicus), or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala), etc.

[0235] In some embodiments, the protein is from the genus Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. carnegiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis 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. graminicola (C.graminicola)), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (C. hirsutus), Cryphonectria (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. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila (M.Thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T.It is derived from fungi such as Thermophilus (T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. 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).

[0236] In some embodiments, the protein is derived from yeasts such as Candida, Hansenula, Komagataella (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).

[0237] With respect to the foregoing species, it will be understood that the present disclosure encompasses both complete and incomplete states, as well as other taxonomic equivalents (e.g., anamorphs), regardless of the names of the species in which they are known. Those skilled in the art will readily appreciate the equivalence of appropriate equivalents.

[0238] Proteins can be identified and derived from other sources, including microorganisms isolated from nature (e.g., soil, compost, water, etc.) or DNA samples directly obtained from natural substances (e.g., soil, compost, water, etc.), using the above probes. Methods for directly isolating microorganisms and DNA from their natural habitats are well known in the art. Next, polynucleotides encoding the proteins can be obtained by similarly screening genomic DNA or cDNA libraries of another microorganism or a mixed DNA sample. After detecting the polynucleotide encoding the protein using the probe, the polynucleotide can be isolated or cloned by utilizing techniques known to those skilled in the art (e.g., see Davis et al., 2012, Basic Methods in Molecular Biology, Elsevier).

[0239] The proteins of the present disclosure can similarly be derived from plants of any genus.

[0240] In some embodiments, the protein is derived from a plant selected from the Amaranthaceae (e.g., amaranth, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, purple coneflower, achillea, guayule, lettuce, marigold, safflower, sunflower, centaury), Brassicaceae (e.g., arugula, broccoli, Chinese cabbage, mizuna, cabbage, cauliflower, rape, collard greens, daikon, horseradish, kale, mustard, radish, oilseed rape, rutabaga, tulip, wasabi, horseradish, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew melon, melon, pumpkin (e.g., butternut squash, buttercup squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentil, mesquite, pea, peanut, soybean, tamarind, tragacanth, broad bean), Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, cola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, grass (e.g., bahiagrass, bermudagrass, strawberry clover, buffalograss, Japanese lawngrass, fescue or zoysia), millet, oats, ornamental grass, rice, rye, sorghum, sugarcane, triticale, wheat and other crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, quince, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, chili pepper, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape).

[0241] The proteins of the present disclosure can be produced and obtained thereby using any suitable method including, but not limited to, shake flask culture and large-scale fermentation methods (including continuous, batch, fed-batch, solid state, and / or microcarrier-based fermentation).

[0242] The present disclosure extends to a method for producing a protein of the present disclosure, comprising: (a) culturing cells that produce the protein in its wild-type form under conditions that promote protein production; and optionally, (b) recovering the protein.

[0243] The present disclosure also extends to a method for producing a protein of the present disclosure, comprising: (a) culturing a recombinant host cell of the present disclosure under conditions that promote protein production; and optionally, (b) recovering the protein.

[0244] In some embodiments, the protein is produced and obtained from Gram-negative bacteria such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0245] In some embodiments, the protein is from the genus Alkalihalobacillus (e.g., A. akibai, A. clausii), the genus 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, B. subtilis, B. thuringiensis), the genus Clostridium, the genus Effusibacillus (e.g., E. pohliae), the genus Enterococcus, the genus Geobacillus (e.g., G. stearothermophilus), the genus Lactobacillus, the genus Lactococcus, the genus Lederbergia (e.g., L. lenta), the genus Neobacillus (e.g., N. novalis), the genus Nocardiopsis, the genus Oceanobacillus (e.g., O. barbara), the genus Staphylococcus, the genus Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, S.produced by and obtained from Gram-positive bacteria such as Actinobacillus pleuropneumoniae, Actinobacillus suis, Arcanobacterium pyogenes, Bacillus anthracis, Brevibacterium linens, Clostridium acetobutylicum, Clostridium perfringens, Corynebacterium glutamicum, Dermatophilus congolensis, Enterococcus faecalis, Erysipelothrix rhusiopathiae, Lactobacillus casei, Lactobacillus plantarum, Listeria monocytogenes, Micrococcus luteus, Mycobacterium bovis, Mycobacterium leprae, Mycobacterium tuberculosis, Nocardia asteroides, Propionibacterium acnes, Rhodococcus equi (including R. equi subsp. equi and R. equi subsp. Zooepidemicus), or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala).

[0246] In some embodiments, the protein is from the genus Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. carnegiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis 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. graminicola (C.graminicola)), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (C. hirsutus), Cryphonectria (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. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila (M.Thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T.Produced from and obtained from fungal cells such as Thermophilus (T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. 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).

[0247] In some embodiments, the protein is produced from and obtained from yeast cells such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., K. 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., Y. lipolytica).

[0248] In some embodiments, the protein is from the Amaranthaceae family (e.g., amaranth, spinach, sugar beet, quinoa), the Asteraceae family (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, purple coneflower, Echinacea, guayule, lettuce, marigold, safflower, sunflower, hundred-day flower), the Brassicaceae family (e.g., arugula, broccoli, Chinese cabbage, collard greens, cabbage, cauliflower, rape, kale, daikon, horseradish, mustard, radish, oilseed rape, rutabaga, tulip, wasabi, horseradish tree, Arabidopsisproduced by and obtained from plant cells selected from Arabidopsis thaliana, Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew melon, melon, pumpkin (e.g., butternut squash, buttercup squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentil, mesquite, pea, peanut, soybean, tamarind, tragacanth, chickpea), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, cola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, grass (e.g., bahiagrass, bermudagrass, strawberry clover, buffalograss, chaboushinoshippei, fescue or zoysia), cereal, oats, ornamental grass, rice, rye, sorghum, sugarcane, triticale, wheat and other crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, quince, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, chili pepper, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape).

[0249] Cells may be cultured in a nutrient medium suitable for protein production using methods known in the art. For example, cells may be cultured by shake flask culture in a suitable medium and under conditions that allow for protein expression and / or isolation, or by small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid-state, and / or microcarrier-based fermentations) in an experimental or industrial fermenter. Suitable media are available from commercial suppliers or may be prepared according to published compositions (e.g., in the catalog of the American Type Culture Collection). If the protein is secreted into the nutrient medium, the protein can be recovered directly from the medium. If the protein is not secreted, it can be recovered from the cell lysate.

[0250] The protein can be detected using methods known in the art that are specific for the protein, including but not limited to the use of specific antibodies, formation of enzyme products, disappearance of enzyme substrates, or assays that determine the relative or specific activity of the protein.

[0251] The protein can be recovered from the 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, a cell-free fermentation broth containing the protein is recovered.

[0252] In some embodiments, the protein is secreted extracellularly.

[0253] In some embodiments, the protein is isolated.

[0254] In some embodiments, the protein is purified.

[0255] The protein may be purified by various procedures known in the art to obtain substantially pure protein and / or 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).

[0256] In an alternative embodiment, the protein is not recovered.

[0257] The present disclosure also provides tools and methods for producing such recombinant host cells, including cells that naturally express the native proteins of the present disclosure, cells genetically modified to express the heterologous proteins of the present disclosure (e.g., recombinant host cells comprising a polynucleotide of the present disclosure operably linked to one or more control sequences for the production of a protein of the present disclosure), and polynucleotides encoding the proteins of the present disclosure and nucleic acid constructs comprising such polynucleotides.

[0258] In some embodiments, the cells are Gram-negative bacteria such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma.

[0259] In some embodiments, the cells are from the genus Alkalihalobacillus (e.g., A. akibai, A. clausii), the genus 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, B. subtilis, B. thuringiensis), the genus Clostridium, the genus Effusibacillus (e.g., E. pohliae), the genus Enterococcus, the genus Geobacillus (e.g., G. stearothermophilus), the genus Lactobacillus, the genus Lactococcus, the genus Lederbergia (e.g., L. lenta), the genus Neobacillus (e.g., N. novalis), the genus Nocardiopsis, the genus Oceanobacillus (e.g., O. barbara), the genus Staphylococcus, the genus Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis and S.Gram-positive bacteria such as Equine subspecies Zooepidemicus (S.equi subsp.Zooepidemicus)) or the genus Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), the genus Sutcliffiella (e.g., S. halmapala).

[0260] In some embodiments, the cell is of the genus Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. carnegiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis 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. graminicola (C.graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (C. hirsutus), Cryphonectria (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. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila (M.Thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T.Fungal cells such as Thermophilus (T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. 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).

[0261] In some embodiments, the cells are yeast cells such as Candida, Hansenula, Komagataella (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).

[0262] In some embodiments, the cell is a plant cell, optionally from the Amaranthaceae family (e.g., amaranth, spinach, sugar beet, quinoa), the Asteraceae family (e.g., artichoke, aster, chamomile, chicory, chrysanthemum, dahlia, daisy, purple coneflower, Echinacea, guayule, lettuce, marigold, safflower, sunflower, hundred-day flower), the Brassicaceae family (e.g., arugula, broccoli, Chinese cabbage, collard greens, cabbage, cauliflower, rape, kale, daikon, horseradish, mustard, radish, oilseed rape, rutabaga, tulip, wasabi, watercress, ArabidopsisArabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew melon, melon, pumpkin (e.g., butternut squash, buttercup squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentil, mesquite, pea, peanut, soybean, tamarind, tragacanth, broad bean), Malvaceae (e.g., cocoa, cotton, durian, hibiscus, kenaf, cola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, grass (e.g., bahiagrass, bermudagrass, strawberry clover, buffalograss, chaboushinoshippei, fescue or zoysia), millet, oats, ornamental grass, rice, rye, sorghum, sugarcane, triticale, wheat and other crops), Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almond, apple, apricot, blackberry, blueberry, cherry, peach, plum, quince, raspberry, rose, strawberry), Solanaceae (e.g., bell pepper, chili pepper, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape).

[0263] In some embodiments, the cell is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 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; b) A polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; c) A polypeptide encoded by a polynucleotide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or the cDNA sequences thereof; d) A polypeptide derived from any one of the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a)-e), wherein the N-terminus and / or C-terminus is extended by addition of one or more amino acids; and / or g) Expresses a fragment of any one of the polypeptides of a)-f).

[0264] In a preferred embodiment, the cell expresses a polypeptide comprising, consisting essentially of, or consisting of any one of the amino acid sequences of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a mature polypeptide thereof.

[0265] In some embodiments, the cell expresses a polypeptide comprising, consisting essentially of, or consisting of a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a mature polypeptide thereof. For example, a microorganism can express a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or the mature peptide, wherein the fragment comprises 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.

[0266] In some embodiments, the cell comprises, consists essentially of, or consists of these mature polypeptides having one or more of the amino acids of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or 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), 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 amino acids) 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 amino acids). The amino acid changes can 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; typically small deletions of 1 to 30 amino acids; small amino-terminal or carboxy-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 tract, an antigenic epitope or a binding module.

[0267] In some embodiments, the cell comprises a homologous or heterologous sequence of a nucleic acid 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 described herein as SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150 or their cDNA sequences.

[0268] In preferred embodiments, the cell comprises, consists essentially of, or consists of a polypeptide comprising any one of the amino acid sequences of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149, or a polynucleotide encoding these or their mature polypeptides.

[0269] In some embodiments, the cell comprises, consists essentially of, or consists of a polynucleotide comprising a nucleic acid sequence encoding a polypeptide having a sequence identity 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% with any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149.

[0270] In some embodiments, the cell comprises, consists essentially of, or consists of a polynucleotide encoding a polypeptide having at least 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 the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149.

[0271] In preferred embodiments, the cell comprises, consists essentially of, or consists of a polynucleotide of any one of SEQ ID NOs: 92-182, 72145-72146, 72148 and 72150, or a cDNA sequence thereof.

[0272] In some embodiments, the cell comprises, consists essentially of, or consists of a polypeptide comprising a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149, or a polynucleotide encoding such mature peptide. For example, the microorganism comprises a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149, or a polynucleotide encoding the mature peptide thereof, and the fragment comprises 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.

[0273] In some embodiments, the cell comprises, consists essentially of, or consists of these mature polypeptides having one or more of the amino acids of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or 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), 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 amino acids) 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 amino acids). The amino acid changes can 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; typically small deletions of 1 to 30 amino acids; small amino-terminal or carboxy-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 tract, an antigenic epitope or a binding module.

[0274] Accordingly, the present disclosure encompasses a method for producing a protein of the present disclosure, comprising culturing a (transgenic) plant or plant part comprising a polynucleotide encoding the protein under conditions that promote protein production, and optionally recovering the protein, wherein the plant or plant part is genetically modified to (over)express one or more proteins of the present disclosure, and the plant or plant part that expresses one or more proteins of the present disclosure. In alternative embodiments, such plants may be used 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.).

[0275] In some embodiments, the plant is a) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; b) a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the mature polypeptide of any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147 and 72149; c) A polypeptide encoded by a polynucleotide having a sequence identity 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% with SEQ ID NOs: 92 - 182, 72145 - 72146, 72148 and 72150, or one or more of these cDNA sequences; d) A polypeptide derived from any one of the mature polypeptides of SEQ ID NOs: 1 - 91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids; e) A polypeptide derived from any one of the mature polypeptides of SEQ ID NOs: 1 - 91, 45906, 72144, 72147 and 72149 by substitution, deletion or insertion of one or more amino acids; f) A polypeptide derived from any one of the polypeptides of a) - e), wherein the N - terminus and / or C - terminus is extended by the addition of one or more amino acids; and / or g) Expresses a fragment of any one of the polypeptides of a) - f).

[0276] In a preferred embodiment, the plant comprises, consists essentially of, or consists of a polypeptide having an amino acid sequence of any one of SEQ ID NOs: 1 - 91, 45906, 72144, 72147 and 72149, or expresses a mature polypeptide.

[0277] In some embodiments, the plant expresses a polypeptide comprising, consisting essentially of, or consisting of a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a mature peptide thereof. For example, the microorganism can express a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a mature peptide thereof, and the fragment comprises 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.

[0278] In some embodiments, the plant comprises, consists essentially of, or consists of these mature polypeptides having one or more of the amino acids of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or 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), 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 amino acids) 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 amino acids). The amino acid changes can 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; typically small deletions of 1 to 30 amino acids; small amino-terminal or carboxy-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 tract, an antigenic epitope or a binding module.

[0279] In some embodiments, the plant comprises a nucleic acid sequence as set forth in SEQ ID NOs: 92-182, 72145-72146, 72148, and 72150 herein, or one or more of their cDNA sequences, or a homologous or heterologous sequence of a nucleic acid 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 thereto.

[0280] In preferred embodiments, the plant comprises, consists essentially of, or consists of a polypeptide comprising any one of the amino acid sequences of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or a polynucleotide encoding these or their mature polypeptides.

[0281] In some embodiments, the plant comprises, consists essentially of, or consists of a polynucleotide comprising a nucleic acid sequence encoding a polypeptide having a sequence identity 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% with any one or more of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0282] In some embodiments, the plant comprises, consists essentially of, or consists of a polynucleotide encoding a polypeptide having at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 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 the mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149.

[0283] In preferred embodiments, the plant comprises, consists essentially of, or consists of a polynucleotide of any one of SEQ ID NOs: 92-182, 72145-72146, 72148, and 72150, or their cDNA.

[0284] In some embodiments, the plant comprises, consists essentially of, or consists of a polynucleotide encoding a polypeptide comprising, consisting essentially of, or consisting of a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or their mature peptides. For example, the microorganism comprises a polynucleotide encoding a fragment of any one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or their mature peptides, and the fragment comprises 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.

[0285] In some embodiments, the plant comprises, consists essentially of, or consists of these mature polypeptides having one or more of an N-terminal extension of one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or 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), 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 amino acids) 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 amino acids). The amino acid changes can 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; typically small deletions of 1 to 30 amino acids; small amino-terminal or carboxy-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 tract, an antigenic epitope, or a binding module.

[0286] Furthermore, the progeny of such plants, plant parts, and plant cells are also included within the scope of the present disclosure.

[0287] As described above, the present disclosure extends to tools and methods for producing such recombinant host cells that express one or more proteins of the present disclosure, including polynucleotides encoding the proteins of the present disclosure and nucleic acid constructs containing such polynucleotides.

[0288] 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 for producing such polynucleotides.

[0289] The polynucleotide can be genomic DNA, cDNA, synthetic DNA, synthetic RNA, mRNA, or a combination thereof.

[0290] The polynucleotide may be cloned from any suitable genus, species, or strain.

[0291] In some embodiments, the protein is cloned from Gram-negative bacteria such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella, or Ureaplasma.

[0292] In some embodiments, the polynucleotide is from the genus Alkalihalobacillus (e.g., A. akibai, A. clausii), the genus 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, B. subtilis, B. thuringiensis), the genus Clostridium, the genus Effusibacillus (e.g., E. pohliae), the genus Enterococcus, the genus Geobacillus (e.g., G. stearothermophilus), the genus Lactobacillus, the genus Lactococcus, the genus Lederbergia (e.g., L. lenta), the genus Neobacillus (e.g., N. novalis), the genus Nocardiopsis, the genus Oceanobacillus (e.g., O. barbara), the genus Staphylococcus, the genus Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, S.It is cloned from Gram-positive bacteria such as Actinobacillus pleuropneumoniae, Actinobacillus suis, Streptococcus suis (e.g., S. suis serotype 2), Pasteurella multocida (e.g., P. multocida type A), Haemophilus parasuis, Actinomyces pyogenes, Arcanobacterium pyogenes, Mycoplasma hyopneumoniae, Mycoplasma hyosynoviae, Mycoplasma suis, Streptococcus uberis, S. equi subsp. Zooepidemicus, or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala).

[0293] In some embodiments, the polynucleotide is from a genus including Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. carnegiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis 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. graminicola (C.graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (C. hirsutus), Cryphonectria (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. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila (M.Thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T.It is cloned from fungi such as Thermophilus (T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. 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).

[0294] In some embodiments, the polynucleotide is cloned from yeasts such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., K. 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., Y. lipolytica).

[0295] In some embodi...

Claims

1. The use of an enzymatically active protein and / or a microorganism expressing an enzymatically active protein, a. Treating surfaces or materials that are susceptible to parasitism or infection by one or more harmful organisms; b. Cleaning a surface or substance that has been infested / infected by one or more pests; c. Treating plants or plant parts; d. Measures to improve the plant's growing environment; e. To treat agricultural equipment / facilities / horticultural equipment / planting equipment; f. To prevent, treat, control, and / or eliminate the parasitic / infection of surfaces / materials by one or more harmful organisms; g. To prevent, treat, control and / or eliminate the infestation / infection of plants, plant parts, plant growing environments, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities by one or more plant pathogenic pests; h. Reducing one or more aspects of disease severity in plants or plant parts affected by one or more plant pathogenic pests; i. To reduce one or more aspects of disease severity in plants or plant parts grown in a plant environment in which one or more plant pathogenic pests have been parasitized or infected; j. To reduce one or more aspects of disease severity in plants or plant parts that have grown in or come into contact with agricultural / flower cultivation / horticultural / afforestation equipment / facilities that are infected by / parasitized by / infected by / these plant pathogens; k. To improve one or more soil properties; l. To improve nutrient utilization / uptake / storage; m. To improve one or more characteristics of plant growth and / or development; n. To reduce the need for external fertilization; o. To reduce the amount of exogenous chemical fertilizers required to achieve the desired result; p. To improve one or more characteristics of plant yield; q. To extend the shelf life of harvested plants or plant parts; r. Delaying the ripening of harvested plants or plant parts; s. To promote the ripening of harvested plants or plant parts; t. To improve the effectiveness of chemical pesticides; u. To improve the effectiveness of biological pesticides; v. To improve the effectiveness of pre-harvest treatment agents; w. To improve the effectiveness of post-harvest treatment agents; x. Preventing, treating, controlling, and / or eliminating resistance and / or plant toxicity of pests induced by chemical pesticides; y. To prevent, treat, control and / or eliminate resistance and / or plant toxicity of pests induced by biological pesticides; and / or z. For inclusion as part of an integrated pest and disease management program / strategy, The enzymatically active proteins mentioned above include glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1, cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucanendo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucanendo-1,3-α-glucosidase, licheninase, and glucanendo Use exhibiting activity of -1,6-β-glucosidase, mannan-endo-1,4-β-mannosidase, mannan-endo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein-endo-α-1,2-mannosidase, α-mannan-endo-1,2-α-mannanase, glucan-1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectinate lyase.

2. A composition for preventing, treating, suppressing and / or eliminating the parasitism / infection of plants, plant parts, plant growing environments, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities by one or more plant pathogenic pests, comprising an agriculturally acceptable carrier and an enzymatically active protein, The enzymatically active proteins mentioned above include glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1, cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, licheninase, glucan endo- A composition exhibiting activity of 1,6-β-glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

3. The composition according to claim 2, further comprising a microorganism that expresses the enzymatically active protein.

4. A method for preventing, treating, suppressing and / or eliminating the parasitism / infection of plants, plant parts, plant growing environments, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities by one or more plant pathogenic pests, wherein the method is as follows: i) The step of determining an effective amount of an enzymatically active protein and / or a microorganism expressing the enzymatically active protein for treating the parasitism / infection of the plant, plant parts, plant growing environment, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities; and ii) A step of applying the enzymatically active protein and / or the microorganism in the effective amount to the plant, plant part, plant growing environment, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

5. A method for preventing, treating, controlling and / or eliminating parasitism / infection of a plant or plant part by one or more plant pathogenic pests, wherein the method is as follows: i) the step of introducing an enzymatically active protein and / or a microorganism expressing the enzymatically active protein into the plant growth environment; and ii) A step of growing the plant or plant part in the plant growing environment, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

6. A method for preventing, treating, controlling and / or eliminating the parasitism / infection of a plant growing environment by one or more plant pathogenic pests, wherein the method is as follows: i) The step of introducing a plant or plant part containing a heterologous polynucleotide encoding an enzymatically active protein into the plant growth environment; and ii) A step of growing the plant or plant part in the plant growing environment, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

7. A method for preventing, treating, controlling and / or eliminating parasitic / infecting a plant growing environment by one or more plant pathogenic pests, wherein the method is as follows: i) a step of treating a plant or plant part with an enzymatically active protein and / or a microorganism expressing the enzymatically active protein; and ii) A step of introducing the treated plant or plant part into the plant growing environment, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

8. A method for preventing, treating, controlling and / or eliminating parasitism / infection of a plant or plant part by one or more plant pathogenic pests, the method being as follows: i) The step of growing a plant or plant part in a plant growing environment; and ii) A step of applying an enzymatically active protein and / or the enzymatically active protein to the plant or plant part, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

9. A method for preventing, treating, controlling and / or eliminating the parasitism / infection of plants, plant parts, plant growing environments, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities by one or more plant pathogenic pests, wherein the method is as follows: i) the step of introducing an enzymatically active protein and / or the enzymatically active protein onto an agriculturally acceptable carrier to produce a composition treated therewith; and ii) A step of applying the treated composition to the plant, plant part, plant growing environment, or agricultural / flower cultivation / horticultural / afforestation equipment / facilities, It is characterized by including, The above method involves the enzymatically active protein being glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1 Cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, rikeninase, glucan endo-1,6-β A method further characterized by exhibiting activity of glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoprotein endo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

10. A plant cell comprising a heterologous polynucleotide encoding an enzymatically active protein, The enzymatically active proteins mentioned above include glucose oxidase, cellobiose oxidase, laccase, catalase, peroxidase, soluble cellulose monooxygenase, γ-glutamyltransferase, triacylglycerol lipase, lysophospholipase, pectin esterase, phospholipase A1, cutinase, phospholipase C, inositol phospholipid phospholipase C, α-amylase, glucan 1,4-α-glucosidase, cellulase, endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase, dextranase, lysozyme, β-glucosidase, α-mannosidase, glucan endo-1,3-β-D-glucosidase, pullulanase, α-L-arabinofuranosidase, glucan endo-1,3-α-glucosidase, licheninase, glucan endo- Plant cells exhibiting activity of 1,6-β-glucosidase, mannanendo-1,4-β-mannosidase, mannanendo-1,6-α-mannosidase, endogalactosaminidase, glycoproteinendo-α-1,2-mannosidase, α-mannanendo-1,2-α-mannanase, glucan 1,4-α-maltohydrase, 1,6-α-D-mannosidase, serine endopeptidase, glutamyl endopeptidase, subtilisin, basyl lysin, asparaginase, and / or pectin acid lyase.

11. The one or more plant pathogenic pests are: Blumeria graminis, Botrytis cinerea, Fusarium graminea, Fusarium virguliforme, Magnaporte grisea, Penicillium digitatum, Penicillium expansum, Penicillium italicum The composition according to claim 2, selected from (italicum), Phakopsora pachyrhizi, Phytophthora infestans, Pseudoperonospora cubensis, Puccinia striiformis, Pyricularia grisea, and Zymoseptoria tritici.

12. The enzymatically active protein a. Polypeptides having at least 90% sequence identity with one or more polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149; b. Polypeptides having at least 90% sequence identity with one or more mature polypeptides of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149; c. A polypeptide comprising one or more of Sequence IDs 1-91, 45906, 72144, 72147, and 72149, or a mature polypeptide thereof; d. A polypeptide comprising one enzymatically active fragment of any of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149, or its mature polypeptide; e. Polypeptides comprising an enzymatically active polypeptide derived from one of SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 by substitution, deletion, or insertion of one or more amino acids; f. Polypeptides comprising an enzymatically active polypeptide derived from one of the mature polypeptides SEQ ID NOs: 1-91, 45906, 72144, 72147, and 72149 by substitution, deletion, or insertion of one or more amino acids; g. Polypeptides containing one or more of sequence numbers 183-72143 or their mature polypeptides; h. Polypeptides comprising an enzymatically active polypeptide derived from one of sequence numbers 183 to 72143 by substitution, deletion, or insertion of one or more amino acids; i. Polypeptides comprising an enzymatically active polypeptide derived from one of the mature polypeptides SEQ ID NOs. 183 to 72143 by substitution, deletion, or insertion of one or more amino acids; j. A polypeptide comprising an enzymatically active polypeptide derived from any one of a to i, wherein the N-terminus and / or C-terminus are elongated by the addition of one or more amino acids; k. Polypeptide containing one enzymatically active fragment from a to j; l. A fusion protein comprising a first polypeptide having a first enzymatic activity and a second polypeptide having a second enzymatic activity. A composition according to claim 2, selected from the following.