A METHOD FOR PRODUCING A POLYPEPTIDE WITH BETA-XYLOSIDASE ACTIVITY, A PROCESS FOR DEGRADING OR CONVERTING A CELLULOSIC OR XYLANE-CONTAINING MATERIAL, FOR SYNTHESIZING A FERMENTATION PRODUCT, AND FOR FERMENTING A CELLULOSIC OR XYLANE-CONTAINING MATERIAL

Abstract

1 / 1 ABSTRACT “ISOLATE POLYPEPTIDE AND POLYNUCLEOTIDE, RECOMBINANT HOST CELL, METHODS FOR PRODUCING A POLYPEPTIDE, A MUTANT OF A PRECURSOR CELL, AND A PROTEIN, AND FOR INHIBITING THE EXPRESSION OF A POLYPEPTIDE, TRANSGENIC PLANT, PLANT PART OR PLANT CELL, RNA MOLECULE, PROCESSES FOR DEGRADING OR CONVERTING A CELLULOSIC OR XYLAN-CONTAINING MATERIAL, TO SYNTHESIS A FERMENTATION PRODUCT, AND TO FERMENT A CELLULOSIC MATERIAL OR CONTAINING XYLAN, AND, COMPLETE BROTH FORMULATION OR CELL CULTURE COMPOSITION†The present invention relates to isolated polypeptides with beta-xylosidase activity and polynucleotides that encode the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides, as well as methods of producing and using the polypeptides.

Description

141 A METHOD FOR PRODUCING A POLYPEPTIDE WITH BETA-XYLOSIDASE ACTIVITY, A PROCESS FOR DEGRADING OR CONVERTING A CELLULOSIC OR XYLANE-CONTAINING MATERIAL, FOR SYNTHESIZING A FERMENTATION PRODUCT, AND FOR FERMENTING A CELLULOSIC OR XYLANE-CONTAINING MATERIAL Declaration of rights for inventions resulting from research and development sponsored by the federal government.

[0001] This invention was realized in part with the assistance of the Government under cooperation agreement DE-FC36-08GO18080, granted by the Department of Energy. The Government retains certain rights in this invention. Reference to a Sequence Listing

[0002] This application contains a listing of sequences in computer-readable form, which is incorporated herein by reference. Fundamentals of the Invention Field of Invention

[0003] The present invention relates to polypeptides with beta-xylosidase activity and polynucleotides encoding the polypeptides. The present invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides, as well as methods of producing and using the polypeptides. Description of the Related Technique

[0004] Lignocellulose, the largest source of renewable biomass in the world, is composed mainly of lignin, cellulose, and hemicellulose, a large part of which is xylan. Xylanases (e.g., endo-1,4beta-xylanase, EC 3.2.1.8) hydrolyze the internal ε-1,4-xylosidic linkages in xylan to produce xylose and lower molecular weight xylo-oligomers. Xylans are polysaccharides formed from D-xylopyranoses linked to 1,4-ε-glycosides. Beta-xylosidases catalyze the exo-hydrolysis of beta Petition 870210014734, dated 12 / 02 / 2021, page 9 / 154 / 141 (1 ^4)-short xylo-oligosaccharides to remove successive Dxylose residues from non-reducing ends.

[0005] Cellulose is a glucose polymer linked by beta 1,4 linkages. Many microorganisms produce enzymes that hydrolyze beta-linked glycans. These enzymes include endoglucanases, cellobiohydrolases, and beta-glucosidases. Endoglucanases digest the cellulose polymer at random sites, opening it up for attack by cellobiohydrolases. Cellobiohydrolases sequentially release cellobiose molecules from the ends of the cellulose polymer. Cellobiose is a water-soluble 1,4beta-linked glucose dimer. Beta-glucosidases hydrolyze cellobiose into glucose.

[0006] The conversion of lignocellulosic raw materials into ethanol presents the advantages of the immediate availability of large quantities of raw material, the advantage of avoiding burning or landfilling the materials, and the cleanliness of the fuel ethanol. Wood, agricultural residues, herbaceous crops, and municipal solid waste are considered raw materials for ethanol production. These materials consist mainly of cellulose, hemicellulose, and lignin. Once lignocellulose is converted into fermentable sugars, for example, glucose, the fermentable sugars are easily fermented by yeast into ethanol.

[0007] There is a need in the art to improve cellulolytic enzyme compositions by supplementing with additional enzymes to increase efficiency and to provide inexpensive enzyme solutions for lignocellulose degradation.

[0008] The present invention provides polypeptides with beta-xylosidase activity and polynucleotides that encode the polypeptides. Summary of the Invention

[0009] The present invention relates to isolated polypeptides with beta-xylosidase activity selected from the group consisting of: Petition 870210014734, dated 12 / 02 / 2021, page 10 / 154 / 141 (a) a polypeptide that has at least 60% sequence identity with the mature polypeptide of SEQ ID NO: 6 or SEQ ID NO: 8; at least 65% sequence identity with the mature polypeptide of SEQ ID NO: 2; or at least 75% sequence identity with the mature polypeptide of SEQ ID NO: 4 or SEQ ID NO: 10; (b) a polypeptide encoded by a polynucleotide that hybridizes under at least medium-high severity conditions to (i) the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, or SEQ ID NO: 9, (ii) the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 7, or (iii) the full-size complement of (i) or (ii); (c) a polypeptide encoded by a polynucleotide that has at least 60% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 5 or SEQ ID NO: 7, or the cDNA sequences thereof; at least 65% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 1 or the cDNA sequence thereof; or at least 75% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 3 or the cDNA sequence thereof or SEQ ID NO: 9; (d) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10 comprising a substitution, deletion, and / or insertion at one or more (e.g., multiple) positions; and (e) a fragment of the polypeptide of (a), (b), (c), or (d) that exhibits beta-xylosidase activity.

[00010] The present invention also relates to isolated polynucleotides encoding the polypeptides of the present invention; nucleic acid constructs, recombinant expression vectors, and recombinant host cells comprising the polynucleotides; and methods of producing the Petition 870210014734, dated 12 / 02 / 2021, page 11 / 154 / 141 polypeptides.

[00011] The present invention also relates to processes for degrading or converting a cellulosic or xylan-containing material, comprising: treating the cellulosic or xylan-containing material with an enzymatic composition in the presence of a polypeptide with beta-xylosidase activity of the present invention. In one aspect, the processes further comprise recovering the degraded or converted cellulosic or xylan-containing material.

[00012] The present invention also relates to processes for synthesizing a fermentation product, comprising: (a) saccharifying a cellulosic or xylan-containing material with an enzymatic composition in the presence of a polypeptide with beta-xylosidase activity of the present invention; (b) fermenting the saccharified or xylan-containing cellulosic material with one or more (e.g., several) fermenting microorganisms to synthesize the fermentation product; and (c) recovering the fermentation product from the fermentation.

[00013] The present invention also relates to processes for fermenting a cellulosic or xylan-containing material, comprising: fermenting the cellulosic or xylan-containing material with one or more (e.g., several) fermenting microorganisms, wherein the cellulosic or xylan-containing material is saccharified with an enzymatic composition in the presence of a polypeptide with beta-xylosidase activity of the present invention. In one aspect, the fermentation of the cellulosic or xylan-containing material synthesizes a fermentation product. In another aspect, the processes further comprise recovering the fermentation product from the fermentation.

[00014] The present invention also relates to a polynucleotide encoding a signal peptide comprising or consisting of amino acids 1 to 19 of SEQ ID NO: 2, amino acids 1 to 19 of SEQ ID NO: 4, Petition 870210014734, dated 12 / 02 / 2021, page 12 / 154 / 141 amino acids 1 to 19 of SEQ ID NO: 6, amino acids 1 to 21 of SEQ ID NO: 8, or amino acids 1 to 20 of SEQ ID NO: 10, which is operably linked to a gene encoding a protein, wherein the protein is foreign to the signal peptide; nucleic acid constructs, expression vectors, and recombinant host cells comprising the polynucleotides; and methods of producing a protein. Brief Description of the Figures Figure 1 shows a restriction map of the pGH3_ZY577211_92 plasmid. Figure 2 shows a restriction map of the pGH3_ZY577202_22 plasmid. Figure 3 shows a restriction map of the pGH3_ZY569167_685 plasmid. Figure 4 shows a restriction map of the plasmid pGH3_ZY654890_6424. Figure 5 shows a restriction map of the plasmid pGH3_PE04100001596. Figure 6 shows the effect of Thermoascus aurantiacus beta-xylosidase GH3 (P24GP2) on the hydrolysis of corn cobs pretreated with Penicillium sp. xylanase GH10 at 50°C. Figure 7 shows the effect of beta-xylosidase GH3 (P24GP2) from Thermoascus aurantiacus on the hydrolysis of corn cobs pretreated with xylanase GH10 from Penicillium sp. at 60°C. Definitions

[00015] Acetylxylan esterase: The term “acetylxylan esterase” means a carboxylesterase (EC 3.1.1.72) that catalyzes the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-naphthyl acetate, and p-nitrophenylacetate. For the purposes of the present invention, the activity of acetylxylan esterase is determined using Petition 870210014734, dated 12 / 02 / 2021, page 13 / 154 / 141 p-nitrophenylacetate 0.5 mM as substrate in sodium acetate 50 mM, pH 5.0, containing TWEEN™ 20 0.01% (polyoxyethylene sorbitan monolaurate). One unit of acetylxylan esterase is defined as the amount of enzyme capable of releasing 1 pmol of p-nitrophenolate anion per minute at pH 5, 25°C.

[00016] Allelic variant: The term “allelic variant” means any of two or more alternative forms of a gene occupying the same chromosomal locus. Allelic variation naturally increases through mutation and can result in polymorphism in populations. Gene mutations can be silent (no change in the encoded polypeptide) or can encode polypeptides with altered amino acid sequences. An allelic variant of a polypeptide is a polypeptide encoded by an allelic variant of a gene.

[00017] Alpha-L-arabinofuranosidase: The term “alpha-L-arabinofuranosidase” means an alpha-L-arabinofuranoside arabinofuranohydrolase (EC 3.2.1.55) that catalyzes the hydrolysis of terminal unreduced alpha-L-arabinofuranoside residues into alpha-L-arabinosides. The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinanes containing (1,3) and / or (1,5) linkages, arabinoxylans, and arabinogalactans. Alpha-L-arabinofuranosidase is also known as arabinosidase, alpha-arabinosidase, alpha-L-arabinosidase, alpha-arabinofuranosidase, alpha-L-arabinofuranosidase polysaccharide, alpha-L-arabinofuranoside hydrolase, Larabinosidase, or alpha-L-arabinanase. For the purposes of the present invention, alpha-L-arabinofuranosidase activity is determined using 5 mg of medium viscosity wheat arabinoxylan (Megazyme International Ireland, Ltd., Bray, Co.Wicklow, Ireland) per mL of 100 mM sodium acetate, pH 5, in a total volume of 200 pL for 30 minutes at 40°C, followed by arabinose analysis by AMINEX® HPX-87H column chromatography (Bio-Rad Laboratories, Inc., Hercules, CA, USA). Petition 870210014734, dated 12 / 02 / 2021, p. 14 / 154 / 141

[00018] Alpha-glucuronidase: The term “alpha-glucuronidase” means an alpha-D-glucosiduronate glucuronoidrolase (EC 3.2.1.139) that catalyzes the hydrolysis of an alpha-D-glucuronide into D-glucuronide and an alcohol. For the purposes of the present invention, the alpha-glucuronidase activity is determined in accordance with de Vries, 1998, J. Bacteriol. 180: 243-249. One unit of alpha-glucuronidase is equal to the amount of enzyme capable of releasing 1 pmol of glucuronic acid or 4-O-methylglucuronic acid per minute at pH 5, 40°C.

[00019] Beta-glucosidase: The term “beta-glucosidase” means a beta-D-glucoside glucohydrolase (EC 3.2.1,21) that catalyzes the hydrolysis of terminal non-reducing beta-D-glucose residues with the release of beta-D-glucose. For the purposes of the present invention, beta-glucosidase activity is determined using p-nitrophenyl-beta-D-glucopyranoside as a substrate, according to the procedure of Venturi et al., 2002, Extracellular beta-Dglucosidase from Chaetomium thermophilum var. coprophilum: production, purification and some biochemical properties, J. Basic Microbiol. 42: 55-66. One unit of beta-glucosidase is defined as 1.0 pmol of p-nitrophenolate anion produced per minute at 25°C, pH 4.8, from 1 mM p-nitrophenylbeta-D-glucopyranoside as substrate in 50 mM sodium citrate containing 0.01% TWEEN® 20.

[00020] Beta-xylosidase: The term “beta-xylosidase” means a beta-D-xyloside xylohydrolase (EC 3.2.1.37) that catalyzes the exo-hydrolysis of short beta ^(4)-xylo-oligosaccharides to remove successive D-xylose residues from the non-reducing ends. For the purposes of the present invention, one unit of beta-xylosidase is defined as 1.0 pmol of p-nitrophenolate anion produced per minute at 40°C, pH 5, from 1 mM p-nitrophenylbeta-D-xyloside as substrate in 100 mM sodium citrate containing 0.01% TWEEN® 20.

[00021] The polypeptides of the present invention have at least 20%, for example, at least 40%, at least 50%, at least 60%, by Petition 870210014734, dated 12 / 02 / 2021, page 15 / 154 / 141 less than 70%, at least 80%, at least 90%, at least 95% and at least 100%, of the beta-xylosidase activity of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8 or SEQ ID NO: 10.

[00022] cDNA: The term cDNA means a DNA molecule that can be prepared by reverse transcription of a mature, joined mRNA molecule obtained from a eukaryotic cell. cDNA needs intron sequences that may be present in the corresponding genomic DNA. The initial and primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including joining, before appearing as mature joined mRNA.

[00023] Cellobiohydrolase: The term “cellobiohydrolase” means a 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91 and EC 3.2.1.176) that catalyzes the hydrolysis of 1,4-beta-D-glycosidic linkages in cellulose, cellooligosaccharides, or any polymer containing glucose linked to beta-1,4, which releases cellobiose from the reducing end (cellobiohydrolase I) or non-reducing end (cellobiohydrolase II) of the chain (Teeri, 1997, Crystalline cellulose degradation: New insight into the function of cellobiohydrolases, Trends in Biotechnology 15: 160-167; Teeri et al., 1998, Trichoderma reesei cellobiohydrolases: why so efficient on crystalline cellulose?, Biochem. Soc. Trans. 26: 173-178). Cellobiohydrolase activity is determined according to the procedures described Lever et al., 1972, Anal. Biochem. 47: 273-279; van Tilbeurgh et al., 1982, FEBS Letters, 149: 152-156; van Tilbeurgh and Claeyssens, 1985, FEBS Letters, 187: 283-288; and Tomme et al., 1988, Eur. J. Biochem.170: 575-581.

[00024] Cellulolytic enzyme or cellulase: The term “cellulolytic enzyme” or “cellulase” means one or more (e.g., several) enzymes that hydrolyze a cellulosic material. Such enzymes include endoglucanase(s), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof. The two basic approaches to measuring cellulolytic activity include: Petition 870210014734, dated 12 / 02 / 2021, page 16 / 154 / 141 (1) measure total cellulolytic activity, and (2) measure individual cellulolytic activities (endoglucanases, cellobiohydrolases, and beta-glucosidases) in the manner revised in Zhang et al., Outlook for cellulase improvement: Screening and selection strategies, 2006, Biotechnology Advances 24: 452481. Total cellulolytic activity is generally measured using insoluble substrates, including Whatman filter paper ^1, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common total cellulolytic activity assay is the filter paper assay using Whatman filter paper ^1 as the substrate. The assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Measurement of cellulase activities, Pure Appl. Chem. 59: 257-68).

[00025] For the purposes of the present invention, the activity of the cellulolytic enzyme is determined by measuring the increase in the hydrolysis of a cellulolytic material by the cellulolytic enzyme(s) under the following conditions: 1-50 mg of cellulolytic enzyme protein / g of cellulose in PCS (or other pre-treated cellulosic material) for 3-7 days at a suitable temperature, for example, 50 °C, 55 °C, or 60 °C, compared to a control hydrolysis without the addition of cellulolytic enzyme protein. Typical conditions are 1 mL reactions, washed and unwashed PCS, 5% insoluble solids, 50 mM sodium acetate pH 5, 1 mM MnSO4, 50 °C, 55 °C, or 60 °C, 72 hours, sugar analysis by AMINEX® HPX-87H column (Bio-Rad Laboratories, Inc., Hercules, CA, USA).

[00026] Cellulosic material: The term “cellulosic material” means any material containing cellulose. The predominant polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemicellulose, and the third is pectin. The secondary cell wall, produced after the cell stops growing, also contains polysaccharides and is reinforced by polymeric lignin covalently cross-linked to hemicellulose. Cellulose is a homopolymer of anhydrocellulose and thus a beta-(1-4)-D-glucan. Petition 870210014734, dated 12 / 02 / 2021, page 17 / 154 / 141 linear, while hemicelluloses include a variety of compounds, such as xylans, xyloglucans, arabinoxylans, and mannans in complex branched structures with a spectrum of substituents. Although generally polymorphic, cellulose is found in plant tissue primarily as an insoluble crystalline matrix of parallel glycan chains. Hemicelluloses generally bind hydrogen to cellulose, as well as to other hemicelluloses, which helps stabilize the cell wall matrix.

[00027] Cellulose is generally found, for example, in the stems, leaves, sepals, bark and cobs of plants or in the leaves, branches and wood of trees. Cellulolytic material may be, but is not limited to, agricultural residue, herbaceous material (including energy-providing crops), municipal solid waste, pulp and ground paper residue, waste paper, and wood (including forest residues) (see, for example, Wiselogel et al., 1995, in Handbook on Bioethanol (Charles E. Wyman, editor), pp. 105-118, Taylor & Francis, Washington DC; Wyman, 1994, Bioresource Technology 50: 3-16; Lynd, 1990, Applied Biochemistry and Biotechnology 24 / 25: 695-719; Mosier et al., 1999, Recent Progress in Bioconversion of Lignocellulosics, in Advances in Biochemical Engineering / Biotechnology, T. Scheper, managing editor, Volume 65, pp. 23-40, Springer-Verlag, New York).It is understood here that cellulose may be in the form of lignocellulose, a plant cell wall material containing lignin, cellulose, and hemicellulose in a mixed matrix. In a preferred aspect, the cellulolytic material is any biomass material. In another preferred aspect, the cellulosic material is lignocellulose, which comprises cellulose, hemicelluloses, and lignin.

[00028] In one aspect, cellulosic material is agricultural waste. In another aspect, cellulosic material is herbaceous waste (including crops for energy production). In another aspect, cellulosic material is municipal solid waste. In another aspect, cellulosic material is waste from pulp and ground paper. In another aspect, cellulosic material is Petition 870210014734, dated 12 / 02 / 2021, page 18 / 154 / 141 residual paper. In another aspect, the cellulosic material is wood (including forest residue).

[00029] In another aspect, the cellulosic material is arundo. In another aspect, the cellulosic material is bagasse. In another aspect, the cellulosic material is bamboo. In another aspect, the cellulosic material is corn cob. In another aspect, the cellulosic material is corn fiber. In another aspect, the cellulosic material is corn residue. In another aspect, the cellulosic material is Miscanthus. In another aspect, the cellulosic material is orange peel. In another aspect, the cellulosic material is rice straw. In another aspect, the cellulosic material is yellow millet. In another aspect, the cellulosic material is wheat straw.

[00030] In another aspect, the cellulosic material is aspen. In another aspect, the cellulosic material is eucalyptus. In another aspect, the cellulosic material is pine. In another aspect, the cellulosic material is pine. In another aspect, the cellulosic material is poplar. In another aspect, the cellulosic material is fir. In another aspect, the cellulosic material is willow.

[00031] In another aspect, the cellulosic material is algal cellulose. In another aspect, the cellulosic material is bacterial cellulose. In another aspect, the cellulosic material is cotton linters. In another aspect, the cellulosic material is filter paper. In another aspect, the cellulosic material is microcrystalline cellulose. In another aspect, the cellulosic material is cellulose treated with phosphoric acid.

[00032] In another aspect, cellulosic material is an aquatic biomass. As used here, the term aquatic biomass means biomass produced in an aquatic environment by a process of photosynthesis. Aquatic biomass can be algae, emergent plants, plants with floating leaves, or submerged plants.

[00033] Cellulolytic material can be used as is, or it can be Petition 870210014734, dated 12 / 02 / 2021, page 19 / 154 / 141 submitted to pretreatment, using conventional methods known in the art, in the manner described herein. In a preferred aspect, the cellulolytic material is pretreated.

[00034] Coding sequence: 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, which begins with a start codon such as ATG, GTG, or TTG, and ends with a stop codon such as TAA, TAG, or TGA. The coding sequence can be genomic DNA, cDNA, synthetic DNA, or a combination thereof.

[00035] Control sequences: The term “control sequences” means nucleic acid sequences necessary for the expression of a polynucleotide encoding a mature polypeptide of the present invention. Each control sequence may be natural (i.e., from the same gene) or foreign (i.e., from a different gene) to the polynucleotide encoding the polypeptide, or natural or foreign to each other. Such control sequences include, but are not limited to, a key sequence, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, the control sequences include a promoter and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites that facilitate the binding of the control sequences to the coding region of the polynucleotide encoding a polypeptide.

[00036] Endoglucanase: The term “endoglucanase” means an endo-1,4-(1,3;1,4)-beta-D-glucan 4-glucanohydrolase (EC 3.2.1.4) that catalyzes the endohydrolysis of 1,4-beta-D-glycosidic linkages in cellulose, cellulose derivatives (such as carboxymethyl cellulose and hydroxyethyl cellulose), lichen, beta-1,4 linkages in mixed beta-1,3 glycans, such as beta-D-glycans or xyloglucans from cereals and other plant material containing Petition 870210014734, dated 12 / 02 / 2021, page 20 / 154 / 141 cellulolytic components. Endoglucanase activity can be determined by measuring the reduction in substrate viscosity or the increase in end reduction determined by a sugar reduction assay (Zhang et al., 2006, Biotechnology Advances 24: 452-481). For the purposes of the present invention, endoglucanase activity can be determined using carboxymethyl cellulose (CMC) as a substrate according to the procedure of Ghose, 1987, Pure and Appl. Chem. 59: 257-268, at pH 5, 40°C.

[00037] Expression: The term “expression” includes any step involved in the production of the polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification and secretion.

[00038] Expression vector: The term “expression vector” means a linear or circular DNA molecule comprising a polynucleotide encoding a polypeptide, and is operably linked to control sequences that provide its expression.

[00039] Glycoside Hydrolase Family 61: The term “Glycoside Hydrolase Family 61” or “GH61 Family” or “GH61” means a polypeptide belonging to glycoside hydrolase family 61, according to Henrissat, B., 1991, A classification of glycosyl hydrolases based on aminoacid sequence similarities, Biochem. J. 280: 309-316, and Henrissat, B., and Bairoch, A. 1996, Updating the sequence-based classification of glycosyl hydrolases, Biochem. J. 316: 695-696. The enzymes in this family were originally classified as a glycoside hydrolase family based on the measurement of very weak endo-1,4-beta-D-glucanase activity in one element of the family. The structure and mode of action of these enzymes are non-canonical and cannot be considered authentic glycosidases. However, they are retained in the CAZy classification based on their ability to enhance lignocellulose breakdown when used in conjunction with a cellulase or a mixture of cellulases. Petition 870210014734, dated 12 / 02 / 2021, page 21 / 154 / 141

[00040] Feruloyl esterase: The term “feruloyl esterase” means a hydrolysis of the sugar 4-hydroxy-3-methoxycinnamoyl (EC 3.1.1.73) that catalyzes the hydrolysis of 4-hydroxy-3-methoxycinnamoyl (feruloyl) groups from esterified sugar, which is generally arabinose in natural biomass substrates, to produce ferulate (4-hydroxy-3-methoxycinnamate). Feruloyl esterase is also known as ferulic acid esterase, hydroxycinnamoyl esterase, FAE-III, cinnamoyl ester hydrolase, FAEA, cinnAE, FAE-I, or FAE-II. For purposes of the present invention, feruloyl esterase activity is determined using 0.5 mM p-nitrophenylferulate as a substrate in 50 mM sodium acetate, pH 5.0. One unit of feruloyl esterase is equivalent to the amount of enzyme capable of releasing 1 μmol of p-nitrophenolate anion per minute at pH 5, 25°C.

[00041] Fragment: The term “fragment” means a polypeptide with one or more (e.g., several) amino acids missing from the amino and / or carboxyl terminus of a mature or main polypeptide; wherein the fragment exhibits beta-xylosidase activity. In one aspect, a fragment contains at least 630 amino acid residues, for example, at least 670 amino acid residues or at least 710 amino acid residues of SEQ ID NO: 2. In another aspect, a fragment contains at least 690 amino acid residues, for example, at least 730 amino acid residues or at least 770 amino acid residues of SEQ ID NO: 4. In another aspect, a fragment contains at least 710 amino acid residues, for example, at least 750 amino acid residues or at least 790 amino acid residues of SEQ ID NO: 6.In another aspect, a fragment contains at least 630 amino acid residues, for example, at least 670 amino acid residues or at least 710 amino acid residues of SEQ ID NO: 8. In another aspect, a fragment contains at least 660 amino acid residues, for example, at least 700 amino acid residues or at least 740 amino acid residues of SEQ ID NO: 10. Petition 870210014734, dated 12 / 02 / 2021, page 22 / 154 / 141

[00042] Hemicellulolytic enzyme or hemicellulase: The term “hemicellulolytic enzyme” or “hemicellulase” means one or more (e.g., several) enzymes that hydrolyze a hemicellulosic material. See, for example, Shallom, D. and Shoham, Y. Microbial hemicellulases. Current Opinion in Microbiology, 2003, 6(3): 219-228). Hemicellulases are key components in the degradation of plant biomass. Examples of hemicellulases include, but are not limited to, acetylmannan esterase, acetylxylan esterase, arabinanase, arabinofuranosidase, coumaric acid esterase, feruloyl esterase, galactosidase, glucuronidase, glucuronoyl esterase, mannanase, mannosidase, xylanase, and xylosidase. The substrates of these enzymes, hemicelluloses, are a heterogeneous group of branched and linear polysaccharides that are linked via hydrogen bonds to the cellulose microfibrils in the plant cell wall, cross-linking them into a strong network.Hemicelluloses are also covalently attached to lignin, forming a very complex structure together with cellulose. The variable structure and organization of hemicelluloses require the combined action of many enzymes for their complete degradation. The catalytic modes of hemicellulases are both glycoside hydrolases (GHs), which hydrolyze glycosidic bonds, and carbohydrate esterases (CEs), which hydrolyze acetate ester bonds or ferulic acid side groups. These catalytic modes, based on the homology of their primary sequence, can be determined into the GH and CE families. Some families, with a similar complete folding, can be further grouped into clans, labeled alphabetically (e.g., GH-A). A more informative classification and the updated classification of these and other carbohydrate-active enzymes are available in the Carbohydrate-Active Enzymes (CAZy) database.The activities of the hemicellulolytic enzyme can be evaluated according to Ghose and Bisaria, 1987, Pure & Appl. Chem. 59: 1739-1752, at a suitable temperature. Petition 870210014734, dated 12 / 02 / 2021, page 23 / 154 / 141, for example, 50 °C, 55 °C, or 60 °C, and in pH, for example, 5.0 or 5.5.

[00043] High severity conditions: The term “high severity conditions” means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, SDS 0.3%, 200 micrograms / mL of denatured and sheared salmon sperm DNA, and formamide 50%, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each for 15 minutes using SSC 2X, SDS 0.2% at 65°C.

[00044] Host cell: The term host cell means any type of cell that is susceptible to transformation, transfection, transduction, or similar to a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term “host cell” includes any progeny of a mother cell that is not identical to the mother cell by virtue of mutations that occur during replication.

[00045] Isolate: The term “isolate” means a substance in a form or environment that does not occur in nature. Non-limiting examples of isolated substances include (1) any non-naturally occurring substance, (2) any substance including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide, or cofactor that is at least partially removed from one or more, or all, of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by human manipulation related to that substance found in nature; or (4) any substance modified by increasing the amount of the related substance in relation to other components with which it is naturally associated (e.g., recombinant production in a host cell; multiple copies of a gene encoding the substance; and use of a stronger promoter than the promoter naturally associated with the gene encoding the substance).

[00046] Low severity conditions: The term “low severity conditions Petition 870210014734, dated 12 / 02 / 2021, page 24 / 154 / 141 "low severity" means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, SDS 0.3%, 200 micrograms / mL of denatured and sheared salmon sperm DNA, and formamide 25%, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each, for 15 minutes, using SSC 2X, SDS 0.2% at 50°C.

[00047] Mature polypeptide: The term “mature polypeptide” means a polypeptide in its final form after translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc. In one aspect, the mature polypeptide has amino acids 20 to 777 of SEQ ID NO: 2 (P244Y5) based on the SignalP program (Nielsen et al., 1997, Protein Engineering 10: 1-6) which predicts that amino acids 1 to 19 of SEQ ID NO: 2 are a signal peptide. In another aspect, the mature polypeptide has amino acids 20 to 825 of SEQ ID NO: 4 (P244Y4) based on the SignalP program which predicts that amino acids 1 to 19 of SEQ ID NO: 4 are a signal peptide. In another aspect, the mature polypeptide presents amino acids 20 to 851 of SEQ ID NO: 6 (P241KM) based on the SignalP program which predicts that amino acids 1 to 19 of SEQ ID NO: 6 are a signal peptide.In another aspect, the mature polypeptide presents amino acids 22 to 767 of SEQ ID NO: 8 (P24QRU) based on the SignalP program which predicts that amino acids 1 to 21 of SEQ ID NO: 8 are a signal peptide. In another aspect, the mature polypeptide presents amino acids 21 to 800 of SEQ ID NO: 10 (P24FP2) based on the SignalP program which predicts that amino acids 1 to 20 of SEQ ID NO: 10 are a signal peptide.

[00048] It is known in the art that a host cell can produce a mixture of two or more different mature polypeptides (i.e., with a different C-terminal and / or N-terminal amino acid) expressed by the same polynucleotide. Petition 870210014734, dated 12 / 02 / 2021, p. 25 / 154 / 141

[00049] Mature polypeptide-coding sequence: The term “mature polypeptide-coding sequence” means a polynucleotide that codes for a mature polypeptide with beta-xylosidase activity. In one aspect, the mature polypeptide-coding sequence features nucleotides 58 to 2399 of SEQ ID NO: 1 (D822K1) or its cDNA sequence based on the SignalP program (Nielsen et al., 1997, supra) which predicts that nucleotides 1 to 57 of SEQ ID NO: 1 code for a signal peptide. In another aspect, the mature polypeptide-coding sequence features nucleotides 58 to 2668 of SEQ ID NO: 3 (D822JZ) or its cDNA sequence based on the SignalP program, which predicts that nucleotides 1 to 57 of SEQ ID NO: 3 code for a signal peptide.In another aspect, the sequence encoding the mature polypeptide has nucleotides 58 to 2829 of SEQ ID NO: 5 (D72UE7) or the cDNA sequence thereof based on the SignalP program which predicts that nucleotides 1 to 57 of SEQ ID NO: 5 encode a signal peptide. In another aspect, the sequence encoding the mature polypeptide has nucleotides 64 to 2634 of SEQ ID NO: 7 (D13874) based on the SignalP program which predicts that nucleotides 1 to 63 of SEQ ID NO: 7 encode a signal peptide. In another aspect, the sequence that encodes the mature polypeptide presents nucleotides 61 to 2400 of SEQ ID NO: 9 (D82RN1) or the cDNA sequence of this based on the SignalP program which predicts that nucleotides 1 to 60 of SEQ ID NO: 9 encode a signal peptide.

[00050] Medium severity conditions: The term “medium severity conditions” means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, 0.3% SDS, 200 micrograms / mL of denatured and sheared salmon sperm DNA, and 35% formamide, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each for 15 minutes using SSC 2X, 0.2% SDS at 55°C. Petition 870210014734, dated 12 / 02 / 2021, p. 26 / 154 / 141

[00051] Medium-high severity conditions: The term “medium-high severity conditions” means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, 0.3% SDS, 200 micrograms / mL of denatured and sheared salmon sperm DNA, and 35% formamide, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each for 15 minutes using SSC 2X, 0.2% SDS at 60°C.

[00052] Nucleic acid construct: The term nucleic acid construct means a nucleic acid molecule, either single-stranded or double-stranded, that is isolated from a naturally occurring gene or is modified to contain nucleic acid segments in a manner that may not otherwise exist in nature, or that is synthetic, comprising one or more control sequences.

[00053] Operably linked: The term “operably linked” means a configuration in which a control sequence is placed in an appropriate position, relative to the coding sequence of a polynucleotide, in such a way that the control sequence directs the expression of the coding sequence.

[00054] Polypeptide with improved cellulolytic activity: The term “polypeptide with improved cellulolytic activity” means a GH61 polypeptide that catalyzes the improvement of the hydrolysis of a cellulosic material by an enzyme exhibiting cellulolytic activity. For the purposes of the present invention, improved cellulolytic activity is determined by evaluating the increase in reducing sugars, or the increase in total cellobiose and glucose from the hydrolysis of a cellulosic material by a cellulolytic enzyme under the following conditions: 1-50 mg of total protein / g of cellulose in pretreated corn residue (PCS), wherein the total protein comprises 50-99.5% w / w of enzymatic cellulolytic protein and 0.5-50% w / w of protein from a GH61 polypeptide with improved cellulolytic activity for 1-7 days in a Petition 870210014734, dated 12 / 02 / 2021, page 27 / 154 / 141 appropriate temperature, for example, 50°C, 55°C, or 60°C, and a pH, for example, 5.0 or 5.5, compared to a control hydrolysis with the same total protein load without improved cellulolytic activity (1-50 mg of cellulolytic protein / g of cellulose in PCS). In a preferred aspect, a mixture of CELLUCLAST® 1.5L (Novozymes UM / S, Bagsvsrd, Denmark) in the presence of 2-3% total weight of Aspergillus oryzae beta-glucosidase protein (recombinantly produced in Aspergillus oryzae according to WO 02 / 095014), or 2-3% total weight of Aspergillus fumigatus beta-glucosidase protein (recombinantly produced in Aspergillus oryzae as described in WO 2002 / 095014) of cellulase protein load is used as the source of cellulolytic activity.

[00055] GH61 polypeptides with improved cellulolytic activity improve the hydrolysis of a cellulosic material, catalyzed by an enzyme that exhibits cellulolytic activity, by reducing the amount of cellulolytic enzyme required to achieve the same degree of hydrolysis, preferably by at least 1.01 times, for example, at least 1.05 times, at least 1.10 times, at least 1.25 times, at least 1.5 times, at least 2 times, at least 3 times, at least 4 times, at least 5 times, at least 10 times, or at least 20 times.

[00056] Pretreated corn residue: The term “PCS” or “pretreated corn residue” means a cellulolytic material derived from corn residue by treatment with heat and diluted sulfuric acid, alkaline pretreatment or neutral pretreatment.

[00057] Sequence identity: The relationship between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.

[00058] For the purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453), as implemented in the Needle program of the package. Petition 870210014734, dated 12 / 02 / 2021, page 28 / 154 / 141 EMBOSS (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or higher. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 substitution matrix (EMBOSS version of BLOSUM62). The Needle yield marked as “best identity” (obtained using the non-summarized option) is used as the percent identity and is calculated as follows: (Identical residuals x 100) / (Alignment size - Total number of gaps in the alignment)

[00059] For the purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch 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), preferably version 5.0.0 or higher. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL substitution matrix (EMBOSS version NCBI NUC4.4). The Needle yield marked as “best identity” (obtained using the non-summarized option) is used as the percent identity and is calculated as follows: (Number of identical deoxyribonucleotides x 100) / (Alignment size / Total number of gaps in the alignment)

[00060] Subsequence: The term “subsequence” means a polynucleotide with one or more (e.g., multiple) nucleotides missing at the 5' and / or 3' end of a sequence encoding the mature polypeptide; wherein the subsequence encodes a fragment with beta-xylosing activity. In one aspect, a subsequence contains at least 1890 nucleotides, for example, at least 2010 nucleotides or at least 2130 nucleotides of SEQ ID NO: 1. In another aspect, a Petition 870210014734, dated 12 / 02 / 2021, page. 29 / 154 / 141 subsequence contains at least 2070 nucleotides, for example, at least 2190 nucleotides or at least 2310 nucleotides of SEQ ID NO: 3. In another aspect, a subsequence contains at least 2130 nucleotides, for example, at least 2250 nucleotides or at least 2370 nucleotides of SEQ ID NO: 5. In another aspect, a subsequence contains at least 1890 nucleotides, for example, at least 2010 nucleotides or at least 2130 nucleotides of SEQ ID NO: 7. In another aspect, a subsequence contains at least 1980 nucleotides, for example, at least 2100 nucleotides or at least 2220 nucleotides of SEQ ID NO: 9.

[00061] Variant: The term “variant” means a polypeptide with beta-xylosidase activity comprising an alteration, i.e., a substitution, insertion, and / or deletion, at one or more (e.g., multiple) positions. A substitution means the exchange of the amino acid occupying a position for a different amino acid; a deletion means the removal of the amino acid occupying a position; and an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.

[00062] Very high severity conditions: The term “very high severity conditions” means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, SDS 0.3%, 200 micrograms / mL of denatured and sheared salmon sperm DNA, and formamide 50%, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each for 15 minutes using SSC 2X, SDS 0.2% at 70°C.

[00063] Very low severity conditions: The term “very low severity conditions” means probes of at least 100 nucleotides in length, pre-hybridization and hybridization at 42°C in SSPE 5X, 0.3% SDS, 200 micrograms / mL of denatured and sheared sperm DNA from Petition 870210014734, dated 12 / 02 / 2021, p. 30 / 154 / 141 salmon, and 25% formamide, following standard Southern blotting procedures for 12 to 24 hours. The carrier material is finally washed three times each for 15 minutes using 2X SSC, 0.2% SDS at 45°C.

[00064] Xylan-containing material: The term “xylan-containing material” means any material comprising a plant cell wall polysaccharide containing a major moiety of beta-(1-4)-linked xylose residues. Terrestrial plant xylans are heteropolymers possessing a major moiety of beta-(1-4)-D-xylopyranose, which is a branched short-chain carbohydrate. They comprise D-glucuronic acid or its 4-O-methyl ether, L-arabinose and / or various oligosaccharides composed of D-xylose, L-arabinose, D- or L-galactose and D-glucose. Xylan-type polysaccharides can be divided into homoxylans and heteroxylans, which include glucuronoxylans, (arabino)glucuronoxylans, (glucurono)arabinoxylans, arabinoxylans and complex heteroxylans. See, for example, Ebringerova et al., 2005, Adv. Polym. Sci. 186: 1-67.

[00065] In the processes of the present invention, any xylan-containing material can be used. In a preferred embodiment, the xylan-containing material is lignocellulose.

[00066] Xylane-degrading activity or xylanolytic activity: The term “xylane-degrading activity” or “xylanolytic activity” means a biological activity that hydrolyzes xylan-containing material. The two basic approaches to measuring xylanolytic activity include: (1) measuring total xylanolytic activity, and (2) measuring individual xylanolytic activities (endoxylanases, beta-xylosidases, arabinofuranosidases, alpha-glucuronidases, acetylxylan esterases, feruloyl esterases, and alpha-glucuronyl esterases). Recent progress in xylanolytic enzyme assays has been summarized in, for example, several publications, including Biely and Puchard, Recent progress in the assays of xylanolytic enzymes, 2006, Journal of the Science of Food and Agriculture 86(11): 1636-1647; Spanikova and Biely, 2006, GlycuronoylPetition 870210014734, dated 12 / 02 / 2021, p. 31 / 154 / 141 esterase - Novel carbohydrate esterase produced by Schizophyllum commune, FEBS Letters 580(19): 4597-4601; Herrmann, Vrsanska, Jurickova, Hirsch, Biely and Kubicek, 1997, A beta-D-xylosidase from Trichoderma reesei is a multifunctional beta-D-xylane oxylohydrolase, Biochemical Journal 321: 375-381.

[00067] Total xylan-degrading activity can be measured by determining the sugar reduction formed from various types of xylan including, for example, oat spelt, beech wood and larch wood xylans, or by photometric determination of stained xylan fragments released from various covalently stained xylans. The most common assay for total xylanolytic activity is based on the production of reduced sugars from polymeric 4-O-methyl glucuronoxylane, in the manner described in Bailey, Biely, Poutanen, 1992, Interlaboratory testing of methods for assay of xylanase activity, Journal of Biotechnology 23(3): 257-270.Xylanase activity can also be determined with 0.2% AZCL-arabinoxylan as substrate in TRITON® X-100 0.01% (4-(1,1,3,3-tetramethylbutyl)phenylpolyethylene glycol) and 200 mM sodium sulfate buffer pH 6 at 37°C. One unit of xylanase activity is defined as 1.0 pmol of azurin produced per minute at 37°C, pH 6, from 0.2% AZCL-arabinoxylan as substrate in 200 mM sodium phosphate buffer, pH 6.

[00068] For the purposes of the present invention, xylan-degrading activity is determined by measuring the increase in hydrolysis of birch xylan (Sigma Chemical Co., Inc., St. Louis, MO, USA) by xylan-degrading enzyme(s) under the following typical conditions: reactions of 1 mL, 5 mg / mL of substrate (total solids), 5 mg of xylanolytic protein / g of substrate, 50 mM sodium acetate at pH 5, 50°C, 24 hours, sugar analysis using the p-hydroxybenzoic acid hydrazide (PHBAH) assay as described by Lever, 1972, A new reaction for colorimetric determination of carbohydrates, Anal. Biochem 47: 273-279.

[00069] Xylanase: The term “xylanase” means a 1,4-beta-D-xylan Petition 870210014734, dated 12 / 02 / 2021, page 32 / 154 / 141 xylohydrolase (EC 3.2.1.8) that catalyzes the endohydrolysis of 1,4-betaD-xylosidic linkages in xylanes. For the purposes of the present invention, xylanase activity is determined with 0.2% AZCL-arabinoxylan as substrate in 0.01% TRITON X-100 and 200 mM sodium phosphate buffer, pH 6 at 37°C. One unit of xylanase activity is defined as 1.0 μmol of azurin produced per minute at 37°C, pH 6, from 0.2% AZCL-arabinoxylan as substrate in 200 mM sodium phosphate buffer, pH 6. Detailed Description of the Invention Polypeptides with cellobiohydrolase activity

[00070] In one embodiment, the present invention relates to isolated polypeptides having a sequence identity with the mature polypeptide of SEQ ID NO: 6 or SEQ ID NO: 8 of at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%;the mature polypeptide of SEQ ID NO: 2 of at least 65%, for example, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%; or the mature polypeptide of SEQ ID NO: 4 or SEQ ID NO: 10 of at least 75%, for example, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example; Petition 870210014734, dated 12 / 02 / 2021, p. 33 / 154 / 141 less than 96%, at least 97%, at least 98%, at least 99% or 100%; which exhibits beta-xylosidase activity. In one aspect, the polypeptides differ by up to 10 amino acids, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10, from the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8 or SEQ ID NO: 10.

[00071] A polypeptide of the present invention preferably comprises or consists of the amino acid sequence SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8 or SEQ ID NO: 10 or an allelic variant thereof; or is a fragment thereof with beta-xylosidase activity. In another aspect, the polypeptide comprises or consists of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8 or SEQ ID NO: 10. In another aspect, the polypeptide comprises or consists of amino acids 20 to 777 of SEQ ID NO: 2, amino acids 20 to 825 of SEQ ID NO: 4, amino acids 20 to 851 of SEQ ID NO: 6, amino acids 22 to 767 of SEQ ID NO: 8 or amino acids 21 to 800 of SEQ ID NO: 10.

[00072] In another embodiment, the present invention relates to isolated polypeptides with beta-xylosidase activity encoded by polynucleotides that hybridize under very low severity conditions, low severity conditions, medium severity conditions, medium-high severity conditions, high severity conditions, or very high severity conditions in (i) the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9; (ii) the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5 or SEQ ID NO: 7, or (iii) the full-size complement of (i) or (ii) (Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual, 2nd edition, Cold Spring Harbor, New York).

[00073] The polynucleotide with SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9, or a subsequence thereof, as well as the polypeptide with SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ Petition 870210014734, dated 12 / 02 / 2021, p. 34 / 154 / 141 Sequence ID No. 8 or Sequence ID No. 10, or a fragment thereof, can be used to determine nucleic acid probes for identifying and cloning DNA encoding polypeptides with beta-xylosidase activity from strains of different genera or species, according to well-known methods in the art. In particular, such probes can be used for hybridization with genomic DNA or cDNA from a cell of interest, following standard Southern blotting procedures, in order to identify and isolate the corresponding gene therein. Such probes can be considerably smaller than the total sequence, but can have at least 15, for example, at least 25, at least 35, or at least 70 nucleotides in size.Preferably, the nucleic acid probe has at least 100 nucleotides in size, for example, at least 200 nucleotides, at least 300 nucleotides, at least 400 nucleotides, at least 500 nucleotides, at least 600 nucleotides, at least 700 nucleotides, at least 800 nucleotides, or at least 900 nucleotides in size. Both DNA and RNA probes can be used. The probes are typically labeled to detect the corresponding gene (for example, with 32P, 3H, 35S, biotin, or avidin). Such probes are included by the present invention.

[00074] A genomic DNA or cDNA library prepared from such other strains can be selected for DNA that hybridizes with the probes described above and encodes a polypeptide with beta-xylosidase activity. Genomic or other DNA from such other strains can be separated by agarose or polyacrylamide gel electrophoresis, or other separation techniques. The DNA from the libraries or the separated DNA can be transferred and immobilized on nitrocellulose or other suitable carrier material. In order to identify a clone or DNA that hybridizes to SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9, or sequences encoding the mature polypeptide of these, or subsequences Petition 870210014734, dated 12 / 02 / 2021, page 35 / 154 / 141 of these, the carrier material is used in a Southern blot.

[00075] For purposes of the present invention, hybridization indicates that the polynucleotide hybridizes to a labeled nucleic acid probe corresponding to (i) SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9; (ii) the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9; (iii) the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5 or SEQ ID NO: 7; (iv) the full-length complement thereof; or (v) a subsequence thereof; under very low to very high severity conditions. Molecules with which the nucleic acid probe hybridizes under these conditions can be detected using, for example, X-ray film or any other detection method known in the art.

[00076] In one aspect, the nucleic acid probe is a polynucleotide encoding the polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10; the mature polypeptide thereof; or a fragment thereof. In another aspect, the nucleic acid probe is SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, or SEQ ID NO: 9; the sequences encoding the mature polypeptide thereof; or the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 7, or the mature polypeptide-coding sequences thereof.

[00077] In another embodiment, the present invention relates to isolated polypeptides with beta-xylosidase activity encoded by polynucleotides with a sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 5 or SEQ ID NO: 7 or the cDNA sequences thereof, of at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, Petition 870210014734, dated 12 / 02 / 2021, page 36 / 154 / 141 at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%; the sequence encoding the mature polypeptide of SEQ ID NO: 1 or the cDNA sequence thereof of at least 65%, for example, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%; or the sequence encoding the mature polypeptide of SEQ ID NO: 3 or the cDNA sequence thereof or SEQ ID NO: 9 of at least 75%, for example, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

[00078] In another embodiment, the present invention relates to variants of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8 or SEQ ID NO: 10 comprising a substitution, deletion, and / or insertion at one or more (e.g., multiple) positions. In one embodiment, the number of amino acid substitutions, deletions, and / or insertions introduced into the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10 is up to 10, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. Amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions,such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension, Petition 870210014734, dated 12 / 02 / 2021, page 37 / 154 / 141, which facilitates purification by changing the net charge or another function, such as a polyhistidine tract, an antigenic epitope, or a binding domain.

[00079] Examples of conservative substitutions are found in the basic amino acid groups (arginine, lysine, and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, and valine), aromatic amino acids (phenylalanine, tryptophan, and tyrosine), and small amino acids (glycine, alanine, serine, threonine, and methionine). Amino acid substitutions that generally do not alter specific activity are known in the art and are described, for example, by H. Neurath and RL Hill, 1979, in The Proteins, Academic Press, New York. Common substitutions are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly.

[00080] Alternatively, amino acid changes are of such a nature that the physicochemical properties of polypeptides are altered. For example, amino acid changes can improve the thermal stability of the polypeptide, alter substrate specificity, change the optimal pH, and the like.

[00081] The essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine screening mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced at each residue in the molecule, and the resulting mutant molecules are tested for betaxylosidase activity to identify amino acid residues that are important for the molecule's activity. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The enzyme's active site or other biological interaction can also be determined by physical analysis of the structure, in the manner determined by Petition 870210014734, dated 12 / 02 / 2021, pp. 38 / 154 / 141, such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, along with mutation of amino acids at the supposed contact site. 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. The identities of essential amino acids can also be inferred from identity analysis with polypeptides that are related to the parent polypeptide. The identity of essential amino acids can also be inferred from an alignment with a related polypeptide.

[00082] Single or multiple amino acid substitutions, deletions, and / or insertions can be performed and tested using known mutagenesis, recombination, and / or shuffling methods, followed by a relevant selection procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95 / 17413; or WO 95 / 22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; US patent 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127).

[00083] Mutagenesis / shuffling methods can be combined with high-throughput automated selection methods to detect the activity of cloned and mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules encoding active polypeptides can be recovered from host cells and rapidly sequenced using standard methods in the technique. These methods allow for the rapid determination of the importance of individual amino acid residues in a polypeptide.

[00084] The polypeptide can be a hybrid polypeptide, in which a Petition 870210014734, dated 12 / 02 / 2021, page 39 / 154 / 141 region of a polypeptide is fused to the N-terminus or C-terminus of a region of another polypeptide.

[00085] The polypeptide may be a fusion polypeptide or a cleavable fusion polypeptide, wherein another polypeptide is fused to the N-terminus or C-terminus of the polypeptide of the present invention. A fusion polypeptide is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention. Techniques for producing fusion polypeptides are known in the art and include linking the coding sequences that encode the polypeptides so that they are in alignment and the expression of the fusion polypeptide is under the control of the same promoter(s) and terminator(s). Fusion polypeptides may also be constructed using intein technology, in which fusion polypeptides are created post-translationally (Cooper et al., 1993, EMBO J. 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779).

[00086] A fusion polypeptide may additionally comprise a cleavage site between the two polypeptides. Upon secretion of the fusion protein, the site is cleaved, releasing the two polypeptides. Examples of cleavage sites include, but are not limited to, the sites 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. Polypeptide sources with beta-xylosidase activity

[00087] A polypeptide with beta-xylosidase activity of the present invention can be obtained from a microorganism of any genus. For purposes of the present invention, the term "obtained from," as used herein, Petition 870210014734, dated 12 / 02 / 2021, page 40 / 154 / 141, along with a given source, may mean that the polypeptide encoded by a polynucleotide is produced by the source or by a strain into which the source polynucleotide has been inserted. In one aspect, the polypeptide obtained from a given source is secreted extracellularly.

[00088] In one aspect, the polypeptide is a Scytalidium polypeptide. In another aspect, the polypeptide is a Scytalidium thermophilum polypeptide. In another aspect, the polypeptide is a Penicillium polypeptide. In another aspect, the polypeptide is a Penicillium oxalicum polypeptide. In another aspect, the polypeptide is a Rhizomucor polypeptide. In another aspect, the polypeptide is a Rhizomucor pumillus polypeptide. In another aspect, the polypeptide is a Thermoascus polypeptide. In another aspect, the polypeptide is a Thermoascus aurantiacus polypeptide.

[00089] It will be understood that, for the species previously mentioned, the invention includes both perfect and imperfect stages, and other taxonomic equivalents, for example, anamorphs, without regard to the species name by which they are known. Those skilled in the art will readily recognize the identity of suitable equivalents.

[00090] Strains of these species are readily accessible to the public in numerous culture collections, such as the American Type Culture Collection (ATCC), Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ), Centraalbureau Voor Schimmelcultures (CBS), and the Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL).

[00091] The polypeptide can be identified and obtained from other sources, including microorganisms isolated from nature (e.g., soil, compost, water, etc.) or DNA samples obtained directly from natural materials (e.g., soil, compost, water, etc.) using probes Petition 870210014734, dated 12 / 02 / 2021, pp. 41 / 154 / 141 previously mentioned. Techniques for isolating microorganisms and DNA directly from their natural habitats are well known in technology. A polynucleotide encoding the polypeptide can then be obtained by similarly selecting a genomic DNA or cDNA library from another microorganism or mixed DNA sample. Once a polynucleotide encoding a polypeptide has been detected with the probe(s), the polynucleotide can be isolated or cloned using techniques known to those skilled in the art (see, for example, Sambrook et al., 1989, supra). Polynucleotides

[00092] The present invention also relates to isolated polynucleotides encoding a polypeptide of the present invention, in the manner described herein.

[00093] The techniques used to isolate or clone a polynucleotide are known in the technology and include isolation from genomic DNA or cDNA, or a combination thereof. Cloning of polynucleotides from genomic DNA can be performed, for example, using the well-known polymerase chain reaction (PCR) or antibody selection from expression libraries to detect cloned DNA fragments with similar structural characteristics. See, for example, Innis et al., 1990, PCR: A Guide to Methods and Application, Academic Press, New York. Other nucleic acid amplification procedures, such as ligase chain reaction (LCR), ligation-activated transcription (LAT), and polynucleotide base amplification (NASBA), can be used.Polynucleotides can be cloned from a strain of Scytalidium, Penicillium, Rhizomucor, or Thermoascus, or a related organism, and thus, for example, can be an allelic species or variant of the polynucleotide region that codes for the polypeptide.

[00094] The modification of a polynucleotide that codes for a Petition 870210014734, dated 12 / 02 / 2021, page 42 / 154 / 141. The polypeptide of the present invention may be necessary to synthesize polypeptides substantially similar to the polypeptide. The term "substantially similar" to the polypeptide refers to non-naturally occurring forms of the polypeptide. These polypeptides may differ in some genetically modified way from the polypeptide isolated from its natural source, for example, variants that differ in specific activity, thermostability, ideal pH, or similar.Variants can be constructed based on the polynucleotide presented as the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, or SEQ ID NO: 9, or the cDNA sequence of the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 7 by introducing nucleotide substitutions that do not result in a change in the amino acid sequence of the polypeptide but correspond to the intended host organism codon for enzyme production, or by introducing nucleotide substitutions that may give rise to a different amino acid sequence. For a general description of nucleotide substitution, see, for example, Ford et al., 1991, Protein Expression and Purification 2: 95-107. Nucleic acid constructs

[00095] The present invention also relates to nucleic acid constructs comprising a polynucleotide of the present invention operably linked to one or more control sequences, which direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences.

[00096] The polynucleotide can be manipulated in a variety of ways to provide polypeptide expression. Manipulation of the polynucleotide prior to its insertion into a vector may be desirable or necessary depending on the expression vector. Techniques for modifying polynucleotides using recombinant DNA methods are well established. Petition 870210014734, dated 12 / 02 / 2021, page 43 / 154 / 141 known in technology.

[00097] The control sequence can be a promoter, a polynucleotide that is recognized by a host cell for the expression of a polynucleotide encoding a polypeptide of the present invention. The promoter contains transcriptional control sequences that mediate the expression of the polypeptide. The promoter can be any polynucleotide that shows transcriptional activity in the host cell, including mutant, truncated, and hybrid promoters, and can be obtained from genes encoding extracellular or intracellular polypeptides that are either homologous or heterologous to the host cell.

[00098] Examples of suitable promoters for directing the transcription of the nucleic acid constructs of the present invention in a bacterial host cell are promoters obtained from the alpha-amylase gene of Bacillus amyloliquefaciens (amyQ), alpha-amylase gene of Bacillus licheniformis (amyL), penicillinase gene of Bacillus licheniformis (penP), maltogenic amylase gene of Bacillus stearothermophilus (amyM), levanasucrase gene of Bacillus subtilis (sacB), xylA and xylB genes of Bacillus subtilis, cryIIIA gene of Bacillus thuringiensis (Agaisse and Lereclus, 1994, Molecular Microbiology 13: 97-107), lac operon of E. coli, trc promoter of E. coli (Egon et al., 1988, Gene 69: 301-315), gene of agarase from Streptomyces coelicolor (dagA), and prokaryotic beta-lactamase gene (Villa-Kamaroff et al., 1978, Proc. Natl. Acad. Sci. USA 75: 3727-3731), as well as the tac promoter (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA 80: 2125).Additional promoters are described in Useful proteins from recombinant bacteria in Gilbert et al., 1980, Scientific American 242: 74-94; and in Sambrook et al., 1989, supra. Examples of tandem promoters are disclosed in WO 99 / 43835.

[00099] Examples of promoters suitable for directing the transcription of nucleic acid constructs of the present invention, in a Petition 870210014734, dated 12 / 02 / 2021, p. 44 / 154 / 141 host cell of filamentous fungus, are the promoters obtained from the genes for acetamidase from Aspergillus nidulans, neutral alpha-amylase from Aspergillus niger, stable acid alpha-amylase from Aspergillus niger, glucoamylase from Aspergillus niger or Aspergillus awamori (glaA), TAKA amylase from Aspergillus oryzae, alkaline protease from Aspergillus oryzae, triose phosphate isomerase from Aspergillus oryzae, trypsin-like protease from Fusarium oxysporum (WO 96 / 00787), amyloglucosidase from Fusarium venenatum (WO 00 / 56900), Daria from Fusarium venenatum (WO 00 / 56900), Quinn from Fusarium venenatum (WO 00 / 56900), lipase from Rhizomucor miehei, aspartic proteinase from Rhizomucor miehei, beta-glucosidase from Trichoderma reesei, cellobiohydrolase I from Trichoderma reesei, cellobiohydrolase II from Trichoderma reesei, endoglucanase I from Trichoderma reesei, endoglucanase II from Trichoderma reesei, endoglucanase III from Trichoderma reesei,endoglucanase V from Trichoderma reesei, xylanase I from Trichoderma reesei, xylanase II from Trichoderma reesei, xylanase III from Trichoderma reesei, betaxilosidase from Trichoderma reesei, and translation elongation factor from Trichoderma reesei, as well as the NA2-tpi promoter (a modified promoter of a neutral alpha-amylase gene from Aspergillus, wherein the untranslated main portion has been replaced by an untranslated main portion from a triose phosphate isomerase gene from Aspergillus; non-limiting examples include modified promoters from a neutral alpha-amylase gene from Aspergillus niger, wherein the untranslated main portion has been replaced by an untranslated main portion from a triose phosphate isomerase gene from Aspergillus nidulans or Aspergillus oryzae); and mutant, truncated, and hybrid promoters thereof. Other promoters are described in US patent 6,011,147. [000100] In a host yeast, the promoters used are obtained from the genes for Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae galactokinase (GAL1), alcohol Petition 870210014734, dated 12 / 02 / 2021, page 45 / 154 / 141. Saccharomyces cerevisiae dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH1, ADH2 / GAP), Saccharomyces cerevisiae triose phosphate isomerase (TPI), Saccharomyces cerevisiae metallothionein (CUP1), and Saccharomyces cerevisiae 3-phosphoglycerate kinase. Other promoters used for yeast as host cells are described by Romanos et al., 1992, Yeast 8: 423-488. [000101] The control sequence can also be a transcription terminator, which is recognized by a host cell to terminate transcription. The terminator is operably linked to the 3' end of the polynucleotide encoding the polypeptide. Any terminator that is functional in the host cell can be used in the present invention. [000102] The preferred terminators for bacterial host cells are obtained from the genes for alkaline protease from Bacillus clausii (aprH), alpha-amylase from Bacillus licheniformis (amyL), and ribosomal RNA from Escherichia coli (rrnB). [000103] The preferred terminators for filamentous fungal host cells are obtained from the genes for acetamidase from Aspergillus nidulans, anthranilate synthase from Aspergillus nidulans, glucoamylase from Aspergillus niger, alpha-glucosidase from Aspergillus niger, TAKA amylase from Aspergillus oryzae, trypsin-like protease from Fusarium oxysporum, beta-glucosidase from Trichoderma reesei, cellobiohydrolase I from Trichoderma reesei, cellobiohydrolase II from Trichoderma reesei, endoglucanase I from Trichoderma reesei, endoglucanase II from Trichoderma reesei, endoglucanase III from Trichoderma reesei, endoglucanase V from Trichoderma reesei, xylanase I from Trichoderma reesei, xylanase Trichoderma reesei II, Trichoderma reesei xylanase III, Trichoderma reesei beta-xylosidase, and Trichoderma reesei translation elongation factor. [000104] The preferred terminators for yeast as host cells are obtained from the enolase genes of Saccharomyces cerevisiae, Petition 870210014734, dated 12 / 02 / 2021, page 46 / 154 / 141 cytochrome C of Saccharomyces cerevisiae (CYC1) and glyceraldehyde-3-phosphate dehydrogenase of Saccharomyces cerevisiae. Other terminators used for yeast as host cells are described by Romanos et al., 1992, supra. [000105] The control sequence can also be a stabilizing mRNA region downstream of a promoter and upstream of a gene's coding sequence that increases gene expression. [000106] Examples of suitable mRNA stabilizing regions are obtained from a cryllIIA gene from Bacillus thuringiensis (WO 94 / 25612) and an SP82 gene from Bacillus subtilis (Hue et al., 1995, Journal of Bacteriology 177: 3465-3471). [000107] The control sequence can also be a major part, an untranslated region of an mRNA that is important for translation by the host cell. The major part is operably linked to the 5' end of the polynucleotide that codes for the polypeptide. Any major part that is functional in the host cell can be used. [000108] The preferred principal parts for filamentous fungal host cells are obtained from the genes for TAKA amylase from Aspergillus oryzae and triose phosphate isomerase from Aspergillus nidulans. [000109] The main parts suitable for yeast as host cells are obtained from the genes for Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase, Saccharomyces cerevisiae factor alpha, and Saccharomyces cerevisiae alcohol dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH2 / GAP). [000110] The control sequence can also be a polyadenylation sequence, a sequence operably linked to the 3' end of the polynucleotide and, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to the transcribed mRNA. Any polyadenylation sequence that is functional in the host cell can be used. Petition 870210014734, dated 12 / 02 / 2021, page 47 / 154 / 141 [000111] The preferred polyadenylation sequences for filamentous fungal host cells are obtained from the genes for anthranilate synthase from Aspergillus nidulans, glucoamylase from Aspergillus niger, alpha-glucosidase from Aspergillus niger, TAKA amylase from Aspergillus oryzae, and trypsin-like protease from Fusarium oxysporum. [000112] The polyadenylation sequences used for yeast host cells are described by Guo and Sherman, 1995, Mol. Cellular Biol. 15: 5983-5990. [000113] The control sequence can also be a region that encodes a signal peptide, which encodes a signal peptide bound to the N-terminus of a polypeptide, and directs the polypeptide in the cell's secretion pathway. The 5' end of the polynucleotide coding sequence may intrinsically contain a naturally bound coding signal peptide sequence in the open reading frame, with the coding sequence segment encoding the polypeptide. Alternatively, the 5' end of the coding sequence may contain a coding signal peptide sequence that is foreign to the coding sequence. A foreign coding signal peptide sequence may be required where the coding sequence does not naturally contain a coding signal peptide sequence. Alternatively, a foreign coding signal peptide sequence may simply replace the natural coding signal peptide sequence in order to enhance polypeptide secretion.However, any coding signal peptide sequence that directs the expressed polypeptide in the secretory pathway of a host cell can be used. [000114] The efficient signal peptide sequences coding for bacterial host cells are the signal peptide sequences coding for NCIB 11837 genes: maltogenic amylase from Bacillus, subtilisin from Bacillus licheniformis, beta-lactamase from Bacillus licheniformis, alpha-amylase from Bacillus stearothermophilus, neutral proteases Petition 870210014734, dated 12 / 02 / 2021, pp. 48 / 154 / 141 of Bacillus stearothermophilus (nprT, nprS, nprM) and prsA of Bacillus subtilis. Additional signal peptides are described by Simonen and Palva, 1993, Microbiological Reviews 57: 109-137. [000115] The efficient coding signal peptide sequences for filamentous fungal host cells are the coding signal peptide sequences obtained from the genes for neutral amylase from Aspergillus niger, glucoamylase from Aspergillus niger, TAKA amylase from Aspergillus oryzae, cellulase from Humicola insolens, endoglucanase V from Humicola insolens, lipase from Humicola lanuginosa, and aspartic proteinase from Rhizomucor miehei. [000116] The signal peptides used for yeast as host cells are obtained from the genes for Saccharomyces cerevisiae alpha factor and Saccharomyces cerevisiae invertase. Other coding signal peptide sequences used are described by Romanos et al., 1992, supra. [000117] The control sequence can also be a coding propeptide sequence that encodes a propeptide positioned at the N-terminus of a polypeptide. The resulting polypeptide is known as a proenzyme or propolypeptide (or a zymogen in some cases). A propolypeptide is generally inactive and can be converted into an active polypeptide by catalytic or autocatalytic cleavage of the propeptide from the propolypeptide. The coding propeptide sequence can be obtained from genes for alkaline protease from Bacillus subtilis (aprE), neutral protease from Bacillus subtilis (nprT), laccase from Myceliophthora thermophila (WO 95 / 33836), aspartic proteinase from Rhizomucor miehei, and factor alpha from Saccharomyces cerevisiae. [000118] Where both the signal peptide and the propeptide sequence are present, the propeptide sequence is positioned close to the N-terminus of a polypeptide, and the signal peptide sequence is positioned close to the N-terminus of the propeptide sequence. [000119] It may also be desirable to add regulatory sequences Petition 870210014734, dated 12 / 02 / 2021, pp. 49 / 154 / 141, which regulate polypeptide expression in relation to host cell growth. Examples of regulatory sequences are those that cause gene expression to be activated and deactivated in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory sequences in prokaryotic systems include the lac, tac, and trp operating systems. In yeast, the ADH2 system or the GAL1 system can be used. In filamentous fungi, the glucoamylase promoter of Aspergillus niger, the TAKA alpha-amylase promoter of Aspergillus oryzae, the cellobiohydrolase I promoter of Trichoderma reesei, and the cellobiohydrolase II promoter of Trichoderma reesei can be used. Other examples of regulatory sequences are those that allow gene amplification.In eukaryotic systems, these regulatory sequences include the dihydrofolate reductase gene, which is amplified in the presence of methotrexate, and metallothionein genes, which are amplified with heavy metals. In these cases, the polynucleotide encoding the polypeptide can be operationally linked to the regulatory sequence. Expression vectors [000120] The present invention also relates to recombinant expression vectors comprising a polynucleotide of the present invention, a promoter, and transcriptional and translational stop signals. The various nucleotide and control sequences can be joined to produce a recombinant expression vector that may include one or more (e.g., multiple) restriction sites convenient to allow insertion or substitution of the polynucleotide encoding the polypeptide at such sites. Alternatively, the polynucleotide can be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into a vector suitable for expression. In creating the expression vector, the coding sequence is located in the vector in such a way that the sequence Petition 870210014734, dated 12 / 02 / 2021, page 50 / 154 / 141, the encoding must be operably linked with the appropriate control sequences for the expression. [000121] The recombinant expression vector can be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA procedures and can result in polynucleotide expression. The choice of vector will typically depend on the compatibility of the vector with the host cell into which the vector will be introduced. The vector can be a linear or closed circular plasmid. [000122] The vector may be a self-replicating vector, that is, a vector that exists as an extrachromosomal entity whose replication is independent of chromosomal replication, for example, a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means to ensure self-replication. Alternatively, the vector may be one that, when introduced into the host cell, is integrated into the genome and replicated along with the chromosome(s) into which it has been integrated. Furthermore, a single vector, or plasmid, or two or more vectors or plasmids that together contain the total DNA to be introduced into the host cell genome, or a transposon, may be used. [000123] The vector preferably contains one or more selectable markers that allow easy selection of transformed, transfected, transduced or similar cells. A selectable marker is a gene product that provides biocidal or viral resistance, heavy metal resistance, prototrophy to auxotrophs and the like. [000124] Examples of selectable bacterial markers are the dal genes of Bacillus licheniformis or Bacillus subtilis, or markers that confer antibiotic resistance such as resistance to ampicillin, chloramphenicol, kanamycin, neomycin, spectinomycin, or tetracycline. Suitable markers for yeast host cells include, but Petition 870210014734, dated 12 / 02 / 2021, page 51 / 154 / 141 without limitation, ADE2, HIS3, LEU2, LYS2, MET3, TRP1 and URA3. Selectable markers for use in a filamentous fungal host cell include, but are not limited to, adeA (phosphoribosylaminoimidazolesuccinocarboxamide synthase), adeB (phosphoribosylaminoimidazole synthase), amdS (acetamidase), argB (ornithine carbamoyltransferase), bar (phosphinothricin acetyltransferase), hph (hygromycin phosphotransferase), niaD (nitrate reductase), pyrG (orotidine-5'-phosphate decarboxylase), sC (sulfate adenyltransferase), and trpC (anthranilate synthase), as well as equivalents thereof. Preferred for use in an Aspergillus cell are the amdS and pyrG genes from Aspergillus nidulans or Aspergillus oryzae and a bar gene from Streptomyces hygroscopicus. The adeA, adeB, amdS, hph, and pyrG genes are preferred for use in a Trichoderma cell. [000125] The selectable marker may be a dual selectable marker system as described in WO 2010 / 039889. In one aspect, the dual selectable marker is a dual hph-tk selectable marker system. [000126] The vector preferably contains one or more elements that enable(s) integration of the vector into the host cell genome or autonomous replication of the vector in the genome-independent cell. [000127] For integration into the host cell genome, the vector may depend on the polynucleotide sequence encoding the polypeptide, or any other element of the vector for integration into the genome by homologous or non-homologous recombination. Alternatively, the vector may contain additional polynucleotides to target homologous recombination integration into the host cell genome at an exact location(s) on the chromosome(s). To increase the probability of integration at a precise location, the integration elements may contain a sufficient number of nucleic acids, such as 100 to 10,000 base pairs, 400 to 10,000 base pairs, and 800 to 10,000 base pairs, that exhibit a high degree of sequence identity with the corresponding target sequence for Petition 870210014734, dated 12 / 02 / 2021, page 52 / 154 / 141, aims to improve the probability of homologous recombination. Integration elements can be any sequence that is homologous to the target sequence in the host cell genome. Furthermore, integration elements can be non-coding or coding polynucleotides. On the other hand, the vector can be integrated into the host cell genome by non-homologous recombination. [000128] For autonomous replication, the vector may additionally comprise an origin of replication that enables the vector to replicate autonomously in the host cell in question. The origin of replication may be any replicating plasmid that mediates autonomous replication functioning in a cell. The term “origin of replication” or “replicating plasmid” means a polynucleotide that enables a plasmid or vector to replicate in vivo. [000129] Examples of bacterial replication origins are the replication origins of plasmids pBR322, pUC19, pACYC177, and pACYC184 that allow replication in E. coli, and pUB110, pE194, pTA1060, and pAMB1 that allow replication in Bacillus. [000130] Examples of origins of replication for use in a yeast host cell are the 2-micron origins of replication, ARS1, ARS4, the combination of ARS1 and CEN3, and the combination of ARS4 and CEN6. [000131] Examples of origins of replication used in a filamentous cell are AMA1 and ANS1 (Gems et al., 1991, Gene 98: 61-67; Cullen et al., 1987, Nucleic Acids Res. 15: 9163-9175; WO 00 / 24883). Isolation of the AMA1 gene and construction of plasmids or vectors comprising the gene can be performed according to the methods disclosed in WO 00 / 24883. [000132] More than one copy of a polynucleotide of the present invention can be inserted into a host cell to increase the production of a polypeptide. An increase in the number of copies of the polynucleotide can be obtained by integrating at least one additional copy. Petition 870210014734, dated 12 / 02 / 2021, page 53 / 154 / 141 of the sequence in the host cell genome, or including an amplifiable selectable marker gene with the polynucleotide, where cells containing amplified copies of the selectable marker gene and, through this, additional copies of the polynucleotide, can be selected by culturing the cells in the presence of the appropriate selectable agent. [000133] The procedures used to link the elements described above to construct the recombinant expression vectors of the present invention are well known to those skilled in the art (see, for example, Sambrook et al., 1989, supra). Host cells [000134] The present invention also relates to recombinant host cells comprising a polynucleotide of the present invention operably linked to one or more control sequences that direct the production of a polypeptide of the present invention. A construct or vector comprising a polynucleotide is introduced into a host cell in such a way that the construct or vector is maintained as a chromosomal integral or as an extrachromosomal self-replicating vector as described above. The term host cell includes any progeny of a mother cell that is not identical to the mother cell by virtue of mutations that occur during replication. The choice of a host cell will depend greatly on the gene encoding the polypeptide and its source. [000135] The host cell can be any cell used in the recombinant production of a polypeptide of the present invention, for example, a prokaryote or a eukaryote. [000136] The prokaryotic host cell can be any Gram-positive or Gram-negative bacterium. Gram-positive bacteria include, but are not limited to, Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, and Streptomyces. Gram-negative bacteria include, but are not limited to, Petition 870210014734, dated 12 / 02 / 2021, p. 54 / 154 / 141 Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma. [000137] The bacterial host cell can be any Bacillus cell including, but not limited to, cells of Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus subtilis, and Bacillus thuringiensis. [000138] The bacterial host cell can also be any Streptococcus cell including, but not limited to, Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi subsp. zooepidemicus cells. [000139] The bacterial host cell can also be any Streptomyces cell including, but not limited to, Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, and Streptomyces lividans cells. [000140] The introduction of DNA into a Bacillus cell can be accomplished by protoplast transformation (see, for example, Chang and Cohen, 1979, Mol. Gen. Genet. 168: 111-115), competent cell transformation (see, for example, Young and Spizizen, 1961, J. Bacteriol. 81: 823-829, or Dubnau and Davidoff-Abelson, 1971, J. Mol. Biol. 56: 209-221), electroporation (see, for example, Shigekawa and Dower, 1988, Biotechniques 6: 742-751), or conjugation (see, for example, Koehler and Thorne, 1987, J. Bacteriol. 169: 5271-5278). The introduction of DNA into an E. coli cell can be accomplished by protoplast transformation (see, for example, Hanahan, 1983, J. Mol. Biol. 166: 557-580) or electroporation (see, for example, Dower et al., 1988, Nucleic Acids Res. 16: 6127-6145). The introduction of DNA into a Streptomyces cell can be accomplished by protoplast transformation, electroporation (see, for example, Gong et al., Petition 870210014734, dated 12 / 02 / 2021, page 55 / 154 / 141 2004, Folia Microbiol. (Praha) 49: 399-405), conjugation (see, for example, Mazodier et al., 1989, J. Bacteriol. 171: 3583-3585), or transduction (see, for example, Burke et al., 2001, Proc. Natl. Acad. Sci. USA 98: 6289-6294). The introduction of DNA into a Pseudomonas cell can be accomplished by electroporation (see, for example, Choi et al., 2006, J. Microbiol. Methods 64: 391-397) or conjugation (see, for example, Pinedo and Smets, 2005, Appl. Environ. Microbiol. 71: 51-57). The introduction of DNA into a Streptococcus cell can be accomplished by natural competence (see, for example, Perry and Kuramitsu, 1981, Infect. Immun. 32: 1295-1297), protoplast transformation (see, for example, Catt and Jollick, 1991, Microbios 68: 189-207), electroporation (see, for example, Buckley et al., 1999, Appl. Environ. Microbiol. 65: 3800-3804), or conjugation (see, for example, Clewell, 1981, Microbiol. Rev. 45: 409-436).However, any method known in the art for introducing DNA into a host cell can be used. [000141] The host cell can also be a eukaryote, such as a mammalian, insect, plant, or fungal cell. [000142] The host cell may be a fungal cell. “Fungi” as used herein includes the phyla Ascomycota, Basidiomycota, Chytridiomycota and Zygomycota, as well as the Oomycota and all mitosporic fungi (as defined by Hawksworth et al., in, Ainsworth and Bisby's Dictionary of the Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UK). [000143] The fungal host cell may be a yeast cell. “Yeast,” as used herein, includes ascosporogenous yeasts (Endomycetales), basidiosporogenous yeasts, and yeasts belonging to the imperfect fungi (Blastomycetes). Since the classification of yeast may change in the future, for the purposes of this invention, yeasts may be defined as described in Biology and Activities of Yeast (Skinner, Passmore, and Davenport, editors, Soc. App. Bacteriol. Symposium). Petition 870210014734, dated 12 / 02 / 2021, pages 56 / 154 / 141 serial number 9, 1980). [000144] The yeast as a host cell can be a Candida, Hansenula, Kluyveromyces, Pichia, Saccharomyces cell, Schizosaccharomyces, or Yarrowia, such as a cell of Kluyveromyces lactis, Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces norbensis, Saccharomyces oviformis, or Yarrowia lipolytica. [000145] The fungal host cell can be a filamentous fungal cell. “Filamentous fungi” include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al., 1995, supra). Filamentous fungi are generally characterized by a mycelial wall composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth is by hyphal elongation, and carbon catabolism is obligately aerobic. In contrast, vegetative growth of yeasts, such as Saccharomyces cerevisiae, is by budding from a unicellular thallus, and carbon catabolism can be fermentative. [000146] The filamentous fungal host cells may be an Acremonium, Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Chrysosporium, Coprinus, Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus, Schizophyllum, Talaromyces, Thermoascus, Thielavia, Tolypocladium, Trametes, or Trichoderma cell. [000147] For example, the filamentous fungal host cell may be a cell of Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Bjerkandera adusta, Ceriporiopsis aneirina, Ceriporiopsis caregiea, Ceriporiopsis gilvescens, Ceriporiopsis Petition 870210014734, of 12 / 02 / 2021, p. 57 / 154 / 141 pannocinta, Ceriporiopsis rivulosa, Ceriporiopsis subrufa, Ceriporiopsis subvermispora, Chrysosporium inops, Chrysosporium keratinophilum, Chrysosporium lucknowense, Chrysosporium merdarium, Chrysosporium pannicola, Chrysosporium queenslandicum, Chrysosporium tropicum, Chrysosporium zonatum, Coprinus cinereus, Coriolus hirsutus, Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusarium venenatum, Humicola insolens, Humicola lanuginosa, Mucor miehei, Myceliophthora thermophila, Neurospora crassa, Penicillium purpurogenum, Phanerochaete chrysosporium, Phlebia radiata, Pleurotus eryngii, Thielavia terrestris,Trametes villosa, Trametes versicolor, Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, ou Trichoderma viride., [000148] Fungal cells can be transformed by a process involving protoplast formation, protoplast transformation, and cell wall regeneration in a manner known as se. Suitable procedures for transforming Aspergillus and Trichoderma host cells are described in EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81: 1470-1474, and Christensen et al., 1988, Bio / Technology 6: 1419-1422. Suitable methods for transforming Fusarium species are described by Malardier et al., 1989, Gene 78: 147156, and WO 96 / 00787. Yeast can be transformed using the procedures described by Becker and Guarente, in Abelson, JN and Simon, MI, editors, Guide to Yeast Genetics and Molecular Biology, Methods in Enzymology, Volume 194, pp. 182-187, Academic Press, Inc., New York; Ito et al., 1983, J. Bacteriol. 153: 163; and Hinnen et al., 1978, Proc. Natl. Petition 870210014734, dated 12 / 02 / 2021, pages 58 / 154 / 141 Acad. Sci. USA 75: 1920. Production Methods [000149] The present invention also relates to methods of producing a polypeptide of the present invention, comprising: (a) cultivating a cell, which in its wild-type form produces the polypeptide, under conditions conducive to the production of the polypeptide; and optionally (b) recovering the polypeptide. In one aspect, the cell is a Scytalidium cell. In another aspect, the cell is a Scytalidium thermophilum cell. In another aspect, the cell is a Penicillium cell. In another aspect, the cell is a Penicillium oxalicum cell. In another aspect, the cell is a Rhizomucor cell. In another aspect, the cell is a Rhizomucor pumillus cell. In another aspect, the cell is a Thermoascus cell. In another aspect, the cell is a Thermoascus aurantiacus cell. [000150] The present invention also relates to methods of producing a polypeptide of the present invention, comprising: (a) growing a recombinant host cell of the present invention under conditions conducive to the production of the polypeptide; and optionally (b) recovering the polypeptide. [000151] Host cells are cultured in a suitable nutrient medium for polypeptide production using methods known in the art. For example, cells can be cultured by shake flask culture, or small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid-state fermentations) in laboratory or industrial fermenters, in a suitable medium and conditions that allow the polypeptide to be expressed and / or isolated. Culture occurs in a suitable nutrient medium comprising carbon and nitrogen sources and inorganic salts, using procedures known in the art. Suitable media are available from commercial suppliers, Petition 870210014734, dated 12 / 02 / 2021, pp. 59 / 154 / 141, or they can be prepared according to published compositions (e.g., in catalogs of the American Type Culture Collection). If the polypeptide is secreted into the nutrient medium, the polypeptide can be recovered directly from the medium. If the polypeptide is not secreted, it can be recovered from cell lysates. [000152] The polypeptide can be detected using methods known in the art that are specific for polypeptides. These detection methods include, but are not limited to, the use of specific antibodies, the formation of an enzyme product, or the disappearance of an enzyme substrate. For example, an enzyme assay can be used to determine the activity of the polypeptide. [000153] The polypeptide can be recovered using methods known in the art. For example, the polypeptide can be recovered from the nutrient medium by conventional procedures including, but not limited to, collection, centrifugation, filtration, extraction, spray drying, evaporation or precipitation. In one aspect, the fermentation broth comprising a polypeptide of the present invention is recovered. [000154] The polypeptide can be purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, isoelectric focusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focusing), differential solubility (e.g., ammonium sulfate precipitation), SDS-PAGE, or extraction (see, for example, Protein Purification, Janson and Ryden, editors, VCH Publishers, New York, 1989) to obtain substantially pure polypeptides. [000155] In an alternative aspect, the polypeptide is not recovered, but a host cell of the present invention expressing the polypeptide is used as a source of the polypeptide. Petition 870210014734, dated 12 / 02 / 2021, pages 60 / 154 / 141 Plants [000156] The present invention also relates to isolated plants, for example, a transgenic plant, part of a plant or plant cell, comprising a polynucleotide of the present invention in order to express and produce a polypeptide in recoverable quantities. The polypeptide can be recovered from the plant or part of the plant. Alternatively, the plant or part of the plant containing the polypeptide can be used as such to improve the quality of a food or feed, for example, to improve nutritional value, palatability and rheological properties, or to destroy an antinutritional factor. [000157] The transgenic plant can be dicotyledonous (a dicotyledon) or monocotyledonous (a monocotyledon). Examples of monocotyledonous plants are grasses, such as meadow grass (bluegrass, Poa), forage grasses such as fescue, Lolium, temperate grasses such as Agrostis, and cereals, for example, wheat, oats, rye, barley, rice, sorghum and maize (corn kernel). [000158] Examples of dicotyledonous plants are tobacco, legumes such as lupins, potatoes, beets, peas, beans and soybeans, and cruciferous plants (family Brassicaceae) such as cauliflower, canola and the closely related model organism Arabidopsis thaliana. [000159] Examples of plant parts are stems, calluses, leaves, roots, fruits, seeds, and tubers, as well as the individual tissues comprising these parts, for example, epidermis, mesophyll, parenchyma, vascular tissues, meristems. Specific plant cell compartments, such as chloroplasts, apoplasts, mitochondria, vacuoles, peroxisomes, and cytoplasm, are also considered plant parts. Furthermore, any plant cell, regardless of tissue origin, is considered a plant part. Similarly, plant parts such as specific tissues and isolated cells to facilitate the use of the invention are also considered plant parts, for Petition 870210014734, dated 12 / 02 / 2021, page 61 / 154 / 141 example, embryos, endosperms, aleurone and seed coats. [000160] Also included within the scope of the present invention are the offspring of such plants, plant parts and plant cells. [000161] The transgenic plant or plant cell expressing the polypeptide can be constructed according to methods known in the technology. In summary, the plant or plant cell is constructed by incorporating one or more expression constructs that encode the polypeptide into the host plant genome or chloroplast genome, and propagating the resulting modified plant or plant cell into a transgenic plant or plant cell. [000162] The expression construct is conveniently a nucleic acid construct comprising a polynucleotide encoding the polypeptide operably linked to appropriate regulatory sequences required for the expression of the polynucleotide in the plant or plant part of choice. Furthermore, the expression construct may comprise a selectable marker used to identify plant cells into which the expression construct has been integrated and the DNA sequences required for the introduction of the construct into the plant in question (the latter depends on the method of DNA introduction to be used). [000163] The choice of regulatory sequences, such as promoter and terminator sequences and, optionally, signal or transit sequences, is determined, for example, based on where, when, and how the polypeptide is to be expressed. For example, the expression of the gene encoding a polypeptide may be constitutive or inducible, or it may be developmentally, stage-specific, or tissue-specific, and the gene product may be targeted to a specific tissue or plant part such as seeds or leaves. Regulatory sequences are, for example, described by Tague et al., 1988, Plant Physiology 86: 506. [000164] For constitutive expression, 35S-CaMV, maize ubiquitin 1 or rice actin 1 promoter can be used (Franck et al., Petition 870210014734, dated 12 / 02 / 2021, p. 62 / 154 / 141 1980, Cell 21: 285-294; Christensen et al., 1992, Plant Mol. Biol. 18:675689; Zhang et al., 1991, Plant Cell 3: 1155-1165). Organ-specific promoters can be, for example, a promoter for storage tissues such as seeds, potato tubers, and fruits (Edwards and Coruzzi, 1990, Ann. Rev. Genet. 24: 275-303), or for metabolic storage tissues such as meristems (Ito et al., 1994, Plant Mol. Biol. 24: 863-878), a seed-specific promoter such as the glutelin, prolamin, globulin, or rice albumin promoter (Wu et al., 1998, Plant Cell Physiol. 39: 885-889), a Vicia faba legume B4 promoter and the unknown Vicia faba seed protein gene (Conrad et al., 1998, J. Plant Physiol. 152: 708-711), a promoter for a seed oil body protein Chen et al., 1998, Plant Cell Physiol.39: 935-941), the napA storage protein promoter from Brassica napus, or any other seed-specific promoter known in the art, for example, in the manner described in WO 91 / 14772. Furthermore, the promoter may be a leaf-specific promoter such as the rbcs promoter of rice or tomato (Kyozuka et al., 1993, Plant Physiol. 102: 991-1000), the adenine methyltransferase gene promoter of chlorella virus (Mitra and Higgins, 1994, Plant Mol. Biol. 26: 85-93), the aldP gene promoter of rice (Kagaya et al., 1995, Mol. Gen. Genet. 248: 668-674), or a wound-inducible promoter such as the pin2 promoter of potato (Xu et al., 1993, Plant Mol. Biol. 22: 573-588).Similarly, the promoter can be induced by abiotic treatments, such as temperature, aridity, or changes in salinity, or induced by exogenously applied substances that activate the promoter, for example, ethanol, estrogen, plant hormones such as ethylene, abscisic acid and gibberellic acid, and heavy metals. [000165] A promoter enhancer element can also be used to achieve higher expression of a polypeptide in the plant. For example, the promoter enhancer element can be an intron that is placed between the Petition 870210014734, dated 12 / 02 / 2021, page 63 / 154 / 141 promoter and the polynucleotide that codes for a polypeptide. For example, Xu et al., 1993, supra, reveal the use of the first intron of the rice actin 1 gene to enhance expression. [000166] The selectable marker gene and any other parts of the expression construct can be chosen from those available in the technique. [000167] The nucleic acid construct is incorporated into the plant genome according to conventional techniques known in the art, including Agrobacterium-mediated transformation, virus-mediated transformation, microinjection, particle bombardment, biolistic transformation and electroporation (Gasser et al., 1990, Science 244: 1293; Potrykus, 1990, Bio / Technology 8: 535; Shimamoto et al., 1989, Nature 338: 274). [000168] Gene transfer mediated by Agrobacterium tumefaciens is a method for generating transgenic dicotyledons (for a review, see Hooykas and Schilperoort, 1992, Plant Mol. Biol. 19: 15-38) and for transforming monocotyledons, although other transformation methods may be used for these plants. One method for generating transgenic monocots is particle bombardment (microscopic gold or tungsten particles coated with transforming DNA) of embryonic calli or developing embryos (Christou, 1992, Plant J. 2: 275-281; ​​Shimamoto, 1994, Curr. Opin. Biotechnol. 5: 158-162; Vasil et al., 1992, Bio / Technology 10: 667-674). An alternative method for monocot transformation is based on protoplast transformation, as described by Omirulleh et al., 1993, Plant Mol. Biol. 21: 415-428. Additional transformation methods include those described in US patents 6,395,966 and 7,151.204 (both of which are incorporated herein by reference in full). [000169] After transformation, the transformants with the incorporated expression construct are selected and regenerated in the complete plants, according to methods well known in the art. In general, the Petition 870210014734, dated 12 / 02 / 2021, page 64 / 154 / 141. The transformation procedure is designed for the selective elimination of selection genes both during regeneration and after generations using, for example, cotransformation with two separate T-DNA constructs or site-specific excision of the selection gene by a specific recombinase. [000170] In addition to targeting the transformation of a particular plant genotype with a construct of the present invention, transgenic plants can be prepared by crossing a plant with the construct into a second plant that needs the construct. For example, a construct encoding a polypeptide can be introduced into a particular plant variety by crossing, without the need to directly transform a plant of that given variety. Therefore, the present invention includes not only a plant regenerated directly from cells that have been transformed according to the present invention, but also the progeny of such plants.As used herein, progeny may refer to the offspring of any generation of a mother plant prepared in accordance with the present invention. Such progeny may include a DNA construct prepared in accordance with the present invention. Crossbreeding results in the introduction of a transgene into a plant lineage by cross-pollinating an initial lineage with a donor plant lineage. Non-limiting examples of such steps are described in U.S. Patent 7,151,204. [000171] Plants can be generated through a backcross conversion process. For example, plants include plants referred to as a genotype, lineage, innate, or backcross-converted hybrid. [000172] Genetic markers can be used to assist in the introgression of one or more transgenes of the invention from one genetic ancestor into another. Marker-assisted selection offers advantages over conventional breeding, in that it can be used to avoid errors caused by phenotypic variations. Additionally, the Petition 870210014734, dated 12 / 02 / 2021, page 65 / 154 / 141: Genetic markers can provide data regarding the relative degree of elite germplasm in the individual progeny of a particular cross. For example, when a plant with a desired trait, which otherwise has an agronomically undesirable genetic background, is crossed with an elite mother, genetic markers can be used to select progeny that not only possess the trait of interest but also exhibit a relatively large proportion of the desired germplasm. In this way, the number of generations required to introgress one or more traits into a particular genetic background is minimized. [000173] The present invention also relates to methods of producing a polypeptide of the present invention comprising: (a) growing a transgenic plant or a plant cell comprising a polynucleotide encoding the polypeptide under conditions leading to the production of the polypeptide; and optionally (b) recovering the polypeptide. Removal or reduction of beta-xylosidase activity [000174] The present invention also relates to methods of producing a mutant of a mother cell, comprising interrupting or deleting a polynucleotide, or a portion thereof, encoding a polypeptide of the present invention, which results in the mutant cell producing less of the polypeptide than the mother cell when grown under the same conditions. [000175] The mutant cell can be constructed by reducing or eliminating the expression of the polynucleotide using methods well known in the art, for example, insertions, interruptions, substitutions, or deletions. In a preferred aspect, the polynucleotide is inactivated. The polynucleotide to be modified or inactivated may be, for example, the coding region, or a part thereof, essential for activity, or a regulatory element required for the expression of the coding region. An example of such a regulatory or control sequence may be a promoter sequence or a Petition 870210014734, dated 12 / 02 / 2021, page 66 / 154 / 141 functional part thereof, that is, a part that is sufficient to affect the expression of the polynucleotide. Other control sequences for possible modification include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, signal peptide sequence, transcription terminator, and transcriptional activator. [000176] Modification or inactivation of the polynucleotide can be achieved by subjecting the mother cell to mutagenesis and selecting mutant cells in which the expression of the polynucleotide has been reduced or eliminated. Mutagenesis, which can be specific or random, can be performed, for example, by using a suitable physical or chemical mutagenic agent, by using a suitable oligonucleotide, or by subjecting the DNA sequence to mutagenesis generated by PCR. Furthermore, mutagenesis can be performed by using any combination of these mutagenic agents. [000177] Examples of a suitable physical or chemical mutagenic agent for the present purpose include ultraviolet (UV) irradiation, hydroxylamine, N-methyl-N-nitro-N-nitrosoguanidine (MNNG), O-methyl hydroxylamine, nitrous acid, ethyl methane sulfonate (EMS), sodium bisulfite, formic acid, and nucleotide analogs. [000178] When such agents are used, mutagenesis is typically performed by incubating the mother cell to be mutagenized in the presence of the mutagenic agent of choice under suitable conditions, and screening and / or selecting mutant cells that exhibit reduced or no expression of the gene. [000179] Modification or inactivation of a polynucleotide can be achieved by inserting, substituting, or deleting one or more nucleotides in the gene, or a regulatory element required for its transcription or translation. For example, nucleotides can be inserted or removed in a way that results in the introduction of a stop codon, the removal of the start codon, or a change in the open reading frame. Such modification or inactivation can be achieved by site mutagenesis. Petition 870210014734, dated 12 / 02 / 2021, page 67 / 154 / 141 directed or mutagenesis generated by PCR according to methods known in the art. Although in principle the modification can be performed in vivo, that is, directly in the cell that expresses the polynucleotide to be modified, it is preferable that the modification be performed in vitro in the manner exemplified below. [000180] An example of a convenient way to eliminate or reduce the expression of a polynucleotide is based on gene replacement, gene deletion, or gene disruption techniques. For example, in the gene disruption method, a nucleic acid sequence corresponding to the endogenous polynucleotide is mutagenized in vitro to produce a defective nucleic acid sequence that is then transformed in the mother cell to produce a defective gene. By homologous recombination, the defective nucleic acid sequence replaces the endogenous polynucleotide. It may be desirable that the defective polynucleotide also encode a marker that can be used for the selection of transformants in which the polynucleotide has been modified or destroyed. In one aspect, the polynucleotide is disrupted with a selectable marker such as those described herein. [000181] The present invention also relates to methods of inhibiting the expression of a polypeptide with beta-xylosidase activity in a cell, comprising administering to the cell or expressing in the cell a double-stranded RNA (dsRNA) molecule, wherein the dsRNA comprises a subsequence of a polynucleotide of the present invention. In a preferred aspect, the dsRNA has about 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more duplex nucleotides in size. [000182] dsRNA is preferably a small interfering RNA (siRNA) or a microRNA (miRNA). In a preferred aspect, dsRNA is a small interfering RNA to inhibit transcription. In another preferred aspect, dsRNA is a microRNA to inhibit translation. Petition 870210014734, dated 12 / 02 / 2021, p. 68 / 154 / 141 [000183] The present invention also relates to such double-stranded RNA (dsRNA) molecules comprising a portion of the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7 or SEQ ID NO: 9 to inhibit the expression of the polypeptide in a cell. Although the present invention is not limited by any particular mechanism of action, dsRNA can enter a cell and cause the degradation of a single-stranded RNA (ssRNA) of similar or identical sequences, including endogenous mRNAs. When a cell is exposed to dsRNA, the mRNA of the homologous gene is selectively degraded by a process called RNA interference (RNAi). [000184] The RNAds of the present invention can be used in gene silencing. In one aspect, the invention provides methods for selectively degrading RNA using an RNAid of the present invention. The process can be carried out in vitro, ex vivo, or in vivo. In one aspect, the RNAds molecules can be used to generate a loss-of-function mutation in a cell, an organ, or an animal. Methods of preparing and using RNAds molecules to selectively degrade RNA are well known in the art; see, for example, US patents 6,489,127, 6,506,559, 6,511,824, and 6,515,109. [000185] The present invention further relates to a mutant cell of a mother cell comprising a disruption or deletion of a polynucleotide encoding the polypeptide, or a control sequence thereof, or a silenced gene encoding the polypeptide, which results in the mutant cell processing less or no polypeptide compared to the mother cell. [000186] Polypeptide-deficient mutant cells are particularly useful in host cells for the expression of natural and heterologous polypeptides. Therefore, the present invention further relates to methods of producing a heterologous or natural polypeptide. Petition 870210014734, dated 12 / 02 / 2021, pp. 69 / 154 / 141, which includes: (a) cultivating the mutant cell under conditions that lead to the production of the polypeptide; and optionally (b) recovering the polypeptide. The term heterologous polypeptides means polypeptides that are not natural to the host cell, for example, a variant of a natural protein. The host cell may contain more than one copy of a polynucleotide that codes for the heterologous or natural polypeptide. [000187] The methods used for cultivation and purification of the product of interest can be carried out by methods known in the art. [000188] The methods of the present invention for producing essentially beta-xylosidase-free products are of particular interest in the production of eukaryotic polypeptides, in particular fungal proteins such as enzymes. Betaxylosidase-deficient cells can also be used to express heterologous proteins of pharmaceutical interest such as hormones, growth factors, receptors and the like. The term eukaryotic polypeptides includes not only natural polypeptides but also those polypeptides, for example, enzymes, that have been modified by amino acid substitutions, deletions or additions, or other such modifications to improve activity, thermostability, pH tolerance and the like. [000189] In a further aspect, the present invention relates to a protein product essentially free of beta-xylosidase activity that is produced by a method of the present invention. Fermentation broth formulations or cell compositions [000190] The present invention also relates to a fermentation broth formulation or a cell composition comprising a polypeptide of the present invention. The fermentation broth product further comprises more ingredients used in the fermentation process, such as, for example, cells (including host cells containing the gene encoding the polypeptide of the present invention). Petition 870210014734, dated 12 / 02 / 2021, page 70 / 154 / 141 invention, which are used to produce the polypeptide of interest), cell debris, biomass, fermentation media and / or fermentation products. In some embodiments, the composition is a whole broth of dead cells containing organic acid(s), dead cells and / or cell debris, and culture medium. [000191] The term fermentation broth, as used herein, refers to a preparation produced by cell fermentation that undergoes minimal or no purification and / or recovery. For example, fermentation broths are produced when microbial cultures are grown in saturation, incubated under carbon-limiting conditions, to allow protein synthesis (e.g., enzyme expression by host cells) and secretion into a cell culture medium. The fermentation broth may contain unfractionated or fractionated contents from the fermentation materials derived at the end of fermentation. Typically, the fermentation broth is unfractionated and comprises the culture medium used and the cell debris present after the microbial cells (e.g., filamentous fungal cells) are removed, for example, by centrifugation.In some embodiments, the fermentation broth contains used cell culture medium, extracellular enzymes, and viable and / or non-viable microbial cells. [000192] In one embodiment, the fermentation broth formulation and cell compositions comprise a first organic acid component, comprising at least one 1-5 carbon organic acid and / or a salt thereof, and a second organic acid component comprising at least one 6 or more carbon organic acid and / or a salt thereof. In a specific embodiment, the first organic acid component is acetic acid, formic acid, propionic acid, a salt thereof, or a mixture of two or more of the foregoing, and the second organic acid component is benzoic acid. Petition 870210014734, dated 12 / 02 / 2021, page 71 / 154 / 141 cyclohexanecarboxylic acid, 4-methylvaleric acid, phenylacetic acid, a salt thereof, or a mixture of two or more of the preceding. [000193] In one aspect, the composition contains organic acid(s) and optionally contains additional dead cells and / or cellular debris. In one embodiment, the dead cells and / or cellular debris are removed from a whole broth containing dead cells to provide a composition that is free of these components. [000194] Fermentation broth formulations or cell compositions may additionally comprise a preservative and / or antimicrobial agent (e.g., bacteriostatic), including, but not limited to, sorbitol, sodium chloride, potassium sorbate, and others known in the art. [000195] Fermentation broth formulations or cell compositions may additionally comprise multiple enzymatic activities, such as one or more (e.g., several) enzymes selected from the group consisting of a cellulase, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swolenin.Fermentation broth formulations or cell compositions may also comprise one or more (e.g., several) enzymes selected from the group consisting of a hydrolase, an isomerase, a ligase, a lyase, an oxidoreductase, or a transferase, for example, an alpha-galactosidase, alpha-glucosidase, aminopeptidase, amylase, beta-galactosidase, beta-glucosidase, betaxylosidase, carbohydrase, carboxypeptidase, catalase, cellobiohydrolase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endoglucanase, esterase, glucoamylase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase. [000196] The broth or complete composition of dead cells can Petition 870210014734, dated 12 / 02 / 2021, page 72 / 154 / 141, containing the unfractionated contents of fermentation materials derived from the end of fermentation. Typically, the broth or complete dead cell composition contains the culture medium used and the cell debris present after the microbial cells (e.g., filamentous fungal cells) have grown to saturation, and is incubated under carbon-limiting conditions to allow protein synthesis (e.g., expression of cellulase and / or glucosidase enzyme(s)). In some embodiments, the broth or complete dead cell composition contains the culture medium used, extracellular enzymes, and dead filamentous fungal cells. In some embodiments, the microbial cells present in the broth or complete dead cell composition may be permeabilized and / or lysed using methods known in the art. [000197] A whole cell composition or broth, as described herein, is typically a liquid, but may contain insoluble components such as dead cells, cell debris, culture medium components, and / or insoluble enzyme(s). In some embodiments, the insoluble components may be removed to provide a clear liquid composition. [000198] The whole broth formulations and cell compositions of the present invention can be produced by a method described in WO 90 / 15861 or WO 2010 / 096673. [000199] The following examples are of preferred uses of the compositions of the present invention. The dosage of the composition and other conditions under which the composition is used can be determined based on methods known in the art. Enzyme compositions [000200] The present invention also relates to compositions comprising a polypeptide of the present invention. Preferably, the compositions are enriched in a polypeptide such as this. The term Petition 870210014734, dated 12 / 02 / 2021, page 73 / 154 / 141 enriched indicates that the beta-xylosidase activity of the composition has been improved, for example, with an enrichment factor of at least 1.1. [000201] The compositions may comprise a polypeptide of the present invention as the main enzymatic component, for example, a single-component composition. Alternatively, the compositions may comprise multiple enzymatic activities, such as one or more (for example, several) enzymes selected from the group consisting of a cellulase, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swolenin.The compositions may also comprise one or more (e.g., several) enzymes selected from the group consisting of a hydrolase, an isomerase, a ligase, a lyase, an oxidoreductase, or a transferase, for example, an alpha-galactosidase, alpha-glucosidase, aminopeptidase, amylase, beta-galactosidase, beta-glucosidase, betaxylosidase, carbohydrase, carboxypeptidase, catalase, cellobiohydrolase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endoglucanase, esterase, glucoamylase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase. The compositions can be prepared according to methods known in the art and can be in the form of a liquid or a dry composition. The compositions can be stabilized according to methods known in the art. [000202] The following examples are of preferred uses of the compositions of the present invention. The dosage of the composition and other conditions under which the composition is used can be determined based on methods known in the art. Uses [000203] The present invention also relates to the following processes Petition 870210014734, dated 12 / 02 / 2021, p. 74 / 154 / 141 to use polypeptides with beta-xylosidase activity, or compositions thereof. [000204] The present invention also relates to processes for degrading or converting a cellulosic or xylan-containing material, comprising: treating the cellulosic or xylan-containing material with an enzyme composition in the presence of a polypeptide with betaxylosidase activity of the present invention. In one aspect, the processes further comprise recovering the degraded or converted cellulosic or xylan-containing material. The soluble degradation or conversion products of the cellulosic or xylan-containing material can be separated from the insoluble cellulosic or xylan-containing material using a method known in the art such as, for example, centrifugation, filtration or gravity establishment. [000205] The present invention also relates to processes for producing a fermentation product, comprising: (a) saccharifying a cellulosic or xylan-containing material with an enzyme composition in the presence of a polypeptide with beta-xylosidase activity of the present invention; (b) fermenting the saccharified cellulosic or xylan-containing material with one or more (e.g., several) fermenting microorganisms to synthesize the fermentation product; and (c) recovering the fermentation product from the fermentation. [000206] The present invention also relates to processes for fermenting a cellulosic or xylan-containing material, comprising: fermenting the cellulosic or xylan-containing material with one or more (e.g., several) fermenting microorganisms, wherein the cellulosic or xylan-containing material is saccharified with an enzyme composition in the presence of a polypeptide with beta-xylosidase activity of the present invention. In one aspect, the fermentation of the cellulosic or xylan-containing material synthesizes a fermentation product. In another aspect, the processes further comprise recovering the fermentation product by Petition 870210014734, dated 12 / 02 / 2021, page 75 / 154 / 141 from fermentation. [000207] The processes of the present invention can be used to saccharify cellulosic or xylan-containing material into fermentable sugars and to convert the fermentable sugars into many usable fermentation products, for example, fuel, potable ethanol, and / or platform chemicals (e.g., acids, alcohols, ketones, gases, and the like). The production of a desired fermentation product from cellulosic or xylan-containing material typically involves pretreatment, enzymatic hydrolysis (saccharification), and fermentation. [000208] The processing of cellulosic or xylan-containing material according to the present invention can be carried out using conventional methods in the art. Furthermore, the processes of the present invention can be implemented using any conventional biomass processing apparatus configured to operate according to the invention. [000209] Hydrolysis (saccharification) and fermentation, separate or simultaneous, include, but are not limited to, separate hydrolysis and fermentation (SHF); simultaneous saccharification and fermentation (SSF); simultaneous saccharification and co-fermentation (SSCF); hybrid hydrolysis and fermentation (HHF); separate hydrolysis and co-fermentation (SHCF); hybrid hydrolysis and co-fermentation (HHCF) and direct microbial conversion (DMC), sometimes also referred to as consolidated bioprocessing (CBP).SHF uses separate process steps to first enzymatically hydrolyze cellulosic material into fermentable sugars, for example, glucose, cellobiose, and pentose-type monomers, and then ferment the fermentable sugars into ethanol. In SSF, the enzymatic hydrolysis of cellulosic material and the fermentation of sugars into ethanol are combined into one step (Philippidis, GP, 1996, Cellulose bioconversion technology, in Handbook on Bioethanol: Production and Utilization, Wyman, CE, ed., Taylor & Francis, Washington, DC, 179-212). SSCF involves the co-fermentation of... Petition 870210014734, dated 12 / 02 / 2021, p. 76 / 154 / 141 multiple sugars (Sheehan, J. and Himmel, M., 1999, Enzymes, energy and the environment: A strategic perspective on the US Department of Energy's research and development activities for bioethanol, Biotechnol. Prog. 15: 817-827). HHF involves a separate hydrolysis step and, in addition, a simultaneous saccharification and hydrolysis step that can be carried out in the same reactor. The steps in an HHF process can be carried out at different temperatures, i.e., enzymatic saccharification at high temperature followed by SSF at a temperature lower than the fermentation strain can tolerate. DMC combines all three processes (production, hydrolysis, and enzymatic fermentation) into one or more (e.g., multiple) steps, where the same organism is used to produce the enzymes for converting cellulosic material into fermentable sugars and to convert the fermentable sugars into a final product (Lynd, LR, Weimer, PJ)., van Zyl, WH, and Pretorius, IS, 2002, Utilization of microbial cellulose: Fundamentals and biotechnology, Microbiol. Mol. Biol. Reviews 66: 506-577). It is understood here that any method known in the art comprising pretreatment, enzymatic hydrolysis (saccharification), fermentation, or a combination thereof, may be used in the practice of the processes of the present invention. [000210] A conventional apparatus may include a fed-batch stirred reactor, a batch stirred reactor, a continuous flow stirred reactor with ultrafiltration and / or a continuous plug flow column reactor (Fernanda de Castilhos Corazza, Flávio Faria de Moraes, Gisella Maria Zanin and Ivo Neitzel, 2003, Optimal control in fed-batch reactor for the cellobiose hydrolysis, Acta Scientiarum. Tecnologia 25: 33-38; Gusakov, AV, and Sinitsyn, AP, 1985, Kinetics of enzymatic hydrolysis of cellulose: 1. A mathematical model for a batch reactor process, Enz. cellulose from waste using a friction bioreactor, Biotechnol. Bioeng. Petition 870210014734, dated 12 / 02 / 2021, p. 77 / 154 / 141 (Gusakov, AV, Sinitsyn, AP, Davydkin, IY, Davydkin, VY, Protas, OV, 1996, Enhancement of enzymatic cellulose hydrolysis using a novel type of bioreactor with intensive stirring induced by electromagnetic field, Appl. Biochem. Biotechnol. 56: 141-153). Additional reactor types include: fluidized bed, upflow blanket, immobilized, and extruded reactors for hydrolysis and / or fermentation. [000211] Pre-treatment. In practice, the processes of the present invention can be used to break down the cell wall components of plant cellulosic or xylan-containing material (Chandra et al., 2007, Substrate pretreatment: The key to effective enzymatic hydrolysis of lignocellulosics? Adv. Biochem. Engin. / Biotechnol. 108: 67-93; Galbe and Zacchi, 2007, Pretreatment of lignocellulosic materials for efficient bioethanol production, Adv. Biochem. Engin. / Biotechnol. 108: 41-65; Hendriks and Zeeman, 2009, Pretreatments to enhance the digestibility of lignocellulosic biomass, Bioresource Technol. 100: 10-18; Mosier et al., 2005, Features of promising technologies for pretreatment of lignocellulosic biomass, Bioresource Technol. 96: 673-686; Taherzadeh and Karimi, 2008, Pretreatment of lignocellulosic wastes to improve ethanol and biogas production: A review, Int. J. de Mol. Sci.9: 1621-1651; Yang and Wyman, 2008, Pretreatment: The key to unlocking low-cost cellulosic ethanol, Biofuels Bioproducts and Biorefining-Biofpr. 2: 26-40). [000212] Cellulosic or xylan-containing material may also be subjected to particle size reduction, sieving, pre-soaking, humidification, washing and / or conditioning prior to pretreatment using methods known in the art. [000213] Conventional pretreatments include, but are not limited to, steam pretreatment (with or without explosion), dilute acid pretreatment, hot water pretreatment, alkaline pretreatment, pre Petition 870210014734, dated 12 / 02 / 2021, pp. 78 / 154 / 141, mentions lime treatment, wet oxidation, wet blasting, ammonia fiber blasting, organosolv pretreatment, and biological pretreatment. Additional pretreatments include ammonia percolation, ultrasound, electroporation, microwaves, supercritical CO2, supercritical H2O, ozone, ionic liquid, and gamma irradiation. [000214] Cellulosic or xylan-containing material can be pretreated before hydrolysis and / or fermentation. Pretreatment is preferably carried out before hydrolysis. Alternatively, pretreatment can be carried out simultaneously with enzymatic hydrolysis to release fermentable sugars such as glucose, xylose and / or cellobiose. In many cases, the pretreatment step itself results in some conversion of biomass into fermentable sugars (even in the absence of enzymes). [000215] Steam pretreatment. In steam pretreatment, cellulosic or xylan-containing material is heated to break down the components of plant cell walls, including lignin, hemicellulose, and cellulose, to make cellulose and other fractions, for example, hemicellulose, accessible to enzymes. The cellulosic or xylan-containing material passes through a reaction vessel where steam is injected to raise the temperature to the required temperature and pressure and is held there for the desired reaction time. Steam pretreatment is preferably carried out at 140-250°C, for example, 160-200°C or 170-190°C, where the ideal temperature range depends on the addition of a chemical catalyst. The dwell time for steam pretreatment is preferably 1-60 minutes, for example, 1-30 minutes, 1-20 minutes, 3-12 minutes or 4-10 minutes, where the ideal dwell time depends on the temperature range and the addition of a chemical catalyst.Steam pretreatment allows for relatively high solids loadings, such that the cellulosic or xylan-containing material is generally only wet during the pretreatment process. Steam pretreatment is often combined with... Petition 870210014734, dated 12 / 02 / 2021, pp. 79 / 154 / 141, describes an explosive discharge of the material after pretreatment, known as a steam explosion, i.e., rapid burning at atmospheric pressure and turbulent flow of the material to increase the surface area accessible by fragmentation (Duff and Murray, 1996, Bioresource Technology 855: 1-33; Galbe and Zacchi, 2002, Appl. Microbiol. Biotechnol. 59: 618-628; US patent application 20020164730). During steam pretreatment, acetyl hemicellulose groups are cleaved, and the resulting acid autocatalyzes the partial hydrolysis of hemicellulose into monosaccharides and oligosaccharides. Lignin is removed to only a limited extent. [000216] Chemical pretreatment: The term “chemical treatment” refers to any chemical pretreatment that promotes the separation and / or release of cellulose, hemicellulose, and / or lignin. Such a pretreatment can convert crystalline cellulose into amorphous cellulose. Examples of suitable chemical pretreatment processes include, for example, dilute acid pretreatment, lime pretreatment, wet oxidation, ammonia fiber explosion / freeze-drying (AFEX), ammonia percolation (APR), ionic liquid, and organosolv pretreatments. [000217] A catalyst, such as H2SO4 or SO2 (typically 0.3 to 5% w / w), is generally added to the steam pretreatment which decreases time and temperature, increases recovery and improves enzymatic hydrolysis (Ballesteros et al., 2006, Appl. Biochem. Biotechnol. 129-132: 496-508; Varga et al., 2004, Appl. Biochem. Biotechnol. 113-116: 509-523; Sassner et al., 2006, Enzyme Microb. Technol. 39: 756-762). In dilute acid pretreatment, cellulosic or xylan-containing material is mixed with dilute acid, typically H2SO4, and water to form a slurry, heated by steam to the desired temperature, and after a residence time is burned off at atmospheric pressure. Dilute acid pretreatment can be carried out with numerous reactor designs, for example, plug flow reactors, counter-current reactors, or counter-stirred bed reactors. Petition 870210014734, dated 12 / 02 / 2021, pp. 80 / 154 / 141 direct current (Duff and Murray, 1996, supra; Schell et al., 2004, Bioresource Technol. 91: 179-188; Lee et al., 1999, Adv. Biochem. Eng. Biotechnol. 65: 93-115). [000218] Various pretreatment methods under alkaline conditions can also be used. These alkaline pretreatments include, but are not limited to, sodium hydroxide, lime, wet oxidation, ammonia percolation (APR), and ammonia fiber explosion / freezing (AFEX). [000219] Lime pretreatment is carried out with calcium oxide or calcium hydroxide at temperatures of 85-150 °C and residence times of 1 hour to several days (Wyman et al., 2005, Bioresource Technol. 96: 1959-1966; Mosier et al., 2005, Bioresource Technol. 96: 673-686). WO 2006 / 110891, WO 2006 / 110899, WO 2006 / 110900, and WO 2006 / 110901 disclose pretreatment methods that use ammonia. [000220] Wet oxidation is a thermal pretreatment typically carried out at 180-200 °C for 5-15 minutes with the addition of an oxidizing agent, such as hydrogen peroxide or super-pressurized oxygen (Schmidt and Thomsen, 1998, Bioresource Technol. 64: 139-151; Palonen et al., 2004, Appl. Biochem. Biotechnol. 117: 1-17; Varga et al., 2004, Biotechnol. Bioeng. 88: 567-574; Martin et al., 2006, J. Chem. Technol. Biotechnol. 81: 1669-1677). Pretreatment is preferably carried out on 1-40% dry material, for example, 2-30% dry material or 5-20% dry material, and often the initial pH is increased by the addition of alkali, such as sodium carbonate. [000221] A modification of the wet oxidation pretreatment method, known as wet blasting (a combination of wet oxidation blasting and steam), can handle material that is up to 30% dry. In wet blasting, the oxidizing agent is introduced during pretreatment after a certain residence time. The pretreatment is then completed by burning at atmospheric pressure (WO 2006 / 032282). Petition 870210014734, dated 12 / 02 / 2021, page 81 / 154 / 141 [000222] Ammonia fiber explosion (AFEX) involves treating cellulosic or xylan-containing material with liquid or gaseous ammonia at moderate temperatures, such as 90-150 °C, and high pressure, such as 17-20 bar, for 5-10 minutes, where the dry matter content can be as high as 60% (Gollapalli et al., 2002, Appl. Biochem. Biotechnol. 98: 23-35; Chundawat et al., 2007, Biotechnol. Bioeng. 96: 219-231; Alizadeh et al., 2005, Appl. Biochem. Biotechnol. 121: 1133-1141; Teymouri et al., 2005, Bioresource Technol. 96: 2014-2018). During pretreatment with AFEX, cellulose and hemicellulose remain relatively intact. Lignin-carbohydrate complexes are cleaved. [000223] Organosolv pretreatment delignifies cellulosic or xylan-containing material by extraction using aqueous ethanol (40-60% ethanol) at 160-200 °C for 30-60 minutes (Pan et al., 2005, Biotechnol. Bioeng. 90: 473-481; Pan et al., 2006, Biotechnol. Bioeng. 94: 851-861; Kurabi et al., 2005, Appl. Biochem. Biotechnol. 121: 219-230). Sulfuric acid is generally added as a catalyst. In organosolv pretreatment, most of the hemicellulose and lignin is removed. [000224] Other examples of suitable pretreatment methods are described by Schell et al., 2003, Appl. Biochem. and Biotechnol. Vol. 105-108, p. 69-85, and Mosier et al., 2005, Bioresource Technology 96: 673-686, and published application US 2002 / 0164730. [000225] In one aspect, the chemical pretreatment is preferably carried out as a dilute acid treatment, and more preferably as a continuous dilute acid treatment. The acid is typically sulfuric acid, but other acids may also be used, such as acetic acid, citric acid, nitric acid, phosphoric acid, tartaric acid, succinic acid, hydrogen chloride, or mixtures thereof. The weak acid treatment is conducted in the pH range of preferably 1-5, for example, 1-4 or 1-2.5. In one aspect, the acid concentration is in the range of Petition 870210014734, dated 12 / 02 / 2021, p. 82 / 154 / 141 preferably 0.01 to 10% by weight of acid, for example, 0.05 to 5% by weight of acid or 0.1 to 2% by weight of acid. The acid is placed in contact with the cellulosic or xylan-containing material and maintained at a temperature in the range of preferably 140-200 °C, for example, 165-190 °C, for periods ranging from 1 to 60 minutes. [000226] In another aspect, the pretreatment takes place in an aqueous slurry. In preferred aspects, the cellulosic or xylan-containing material is present during the pretreatment in amounts preferably between 10-80% by weight, for example, 20-70% by weight or 30-60% by weight, such as around 40% by weight. The pretreated cellulosic or xylan-containing material may be unwashed or washed using any method known in the art, for example, washed with water. [000227] Mechanical pretreatment or physical pretreatment: The term “mechanical pretreatment” or “physical pretreatment” refers to any pretreatment that promotes a reduction in particle size. For example, such pretreatment may involve various types of crushing or grinding (e.g., dry grinding, wet grinding, or vibratory ball grinding). [000228] Cellulosic or xylan-containing material can be pretreated both physically (mechanically) and chemically. Mechanical or physical pretreatment can be coupled with steam / vapor explosion, hydrothermolysis, weak or dilute acid treatment, high temperature, high pressure treatment, irradiation (e.g., microwave irradiation), or combinations thereof. In one aspect, high pressure means pressure in the range of preferably about 100 to about 400 psi, for example, about 150 to about 250 psi. In another aspect, high temperature means temperatures in the range of about 100 to about 300 °C, for example, about 140 to about 200 °C. In a preferred aspect, the mechanical or physical pretreatment is carried out in a batch process using a steam gun hydrolyzer system that uses high pressure. Petition 870210014734, dated 12 / 02 / 2021, page 83 / 154 / 141 and high temperature in the manner defined above, for example, a Sunds hydrolyzer available from Sunds Defibrator AB, Sweden. Chemical or physical pretreatments may be carried out sequentially or simultaneously, if desired. [000229] In this way, in a preferred aspect, the cellulosic or xylan-containing material is subjected to physical (mechanical) or chemical pretreatment, or any combination thereof, to promote the separation and / or release of cellulose, hemicellulose and / or lignin. [000230] Biological pretreatment: The term “biological pretreatment” refers to any biological pretreatment that promotes the separation and / or release of cellulose, hemicellulose, and / or lignin from cellulosic material or material containing xylan. Biological pretreatment techniques may involve applying microorganisms and / or enzymes that solubilize lignin (see, for example, Hsu, T.-A., 1996, Pretreatment of biomass, in Handbook on Bioethanol: Production and Utilization, Wyman, CE, ed., Taylor & Francis, Washington, DC, 179-212; Ghosh and Singh, 1993, Physicochemical and biological treatments for enzymatic / microbial conversion of cellulose biomass, Adv. Appl. Microbiol. 39: 295-333; Symposium Series 566, American Chemical Society, Washington, DC, chapter 15;T., 1999, Ethanol production from renewable resources, em Advances in Biochemical Engineering / Biotechnology, Scheper, T., ed., Springer-Verlag Berlin Heidelberg, Alamanha, 65: 207-241; Olsson e Hahn-Hagerdal, 1996, Fermentation of lignocellulosic hydrolysates for ethanol production, Enz. Microb. Tech. 18: 312-331; e Vallander e Eriksson, 1990, Production of ethanol from material lignocelullosics: State do art, Adv. Biochem. Eng. / Biotechnol. 42: 63-95). Petição 870210014734, de 12 / 02 / 2021, pág. 84 / 154 / 141 [000231] Saccharification. In the hydrolysis step, also known as saccharification, the cellulosic or xylan-containing material, for example, pretreated, is hydrolyzed to break down cellulose and / or hemicellulose into fermentable sugars, such as glucose, cellobiose, xylose, xylulose, arabinose, mannose, galactose, and / or soluble oligosaccharides. The hydrolysis is carried out enzymatically by an enzyme composition, as described herein, in the presence of a polypeptide with beta-xylosidase activity of the present invention. The enzyme components of the compositions can be added simultaneously or sequentially. [000232] Enzymatic hydrolysis is preferably carried out in a suitable aqueous environment, under conditions that can be easily determined by those skilled in the art. In one aspect, hydrolysis is carried out under conditions suitable for the activity of the enzyme components, i.e., ideal for the enzyme components. Hydrolysis can be carried out as a fed-batch or continuous process, where the cellulosic or xylan-containing material is fed gradually, for example, by a hydrolysis solution containing enzyme. [000233] Saccharification is generally carried out in reactors or stirred tank fermenters under controlled pH, temperature, and mixing conditions. The appropriate process time, temperature, and pH conditions can be easily determined by those skilled in the art. For example, saccharification can last up to 200 hours, but is typically carried out preferably for about 12 to about 120 hours, for example, about 16 to about 72 hours or about 24 to about 48 hours. The temperature is in the range of preferably about 25°C to about 70°C, for example, about 30°C to about 65°C, about 40°C to about 60°C, or about 50°C to about 55°C. The pH is preferably in the range of about 3 to about 8, for example, about 3.5 to about 7, about 4 to about 6, or about 5.0 to about 5.5. The dry solids content is in the range of Petition 870210014734, dated 12 / 02 / 2021, p. 85 / 154 / 141 preferably about 5 to about 50% by weight, for example, about 10 to about 40% by weight or about 20 to about 30% by weight. [000234] Enzyme compositions may comprise any protein used in the degradation of cellulosic material or that contains xylan. [000235] In one aspect, the enzyme composition comprises or additionally includes one or more (e.g., several) proteins selected from the group consisting of a cellulase, a polypeptide with enhanced cellulolytic activity, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swolenin. In another aspect, the cellulase is preferably one or more (e.g., several) enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase, and a beta-glucosidase. In another aspect, the hemicellulase is preferably one or more (e.g., several) enzymes selected from the group consisting of an acetylmannan esterase, an acetylxylan esterase, an arabinanase, an arabinofuranosidase, a coumaric acid esterase, a feruloyl esterase, a galactosidase, a glucuronidase, a glucuronoyl esterase, a mannanase, a mannosidase, a xylanase, and a xylosidase. [000236] In another aspect, the enzymatic composition comprises one or more (e.g., several) cellulolytic enzymes. In another aspect, the enzymatic composition comprises or additionally includes one or more (e.g., several) hemicellulolytic enzymes. In another aspect, the enzymatic composition comprises one or more (e.g., several) cellulolytic enzymes and one or more (e.g., several) hemicellulolytic enzymes. In another aspect, the enzymatic composition comprises one or more (e.g., several) enzymes selected from the group of cellulolytic enzymes and hemicellulolytic enzymes. In another aspect, the enzymatic composition comprises an endoglucanase. In another aspect, the enzymatic composition comprises Petition 870210014734, dated 12 / 02 / 2021, page 86 / 154 / 141 a cellobiohydrolase. In another aspect, the enzymatic composition comprises a beta-glucosidase. In another aspect, the enzymatic composition comprises a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises an endoglucanase and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises a cellobiohydrolase and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises a beta-glucosidase and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises an endoglucanase and a cellobiohydrolase. In another aspect, the enzymatic composition comprises an endoglucanase and a beta-glucosidase. In another aspect, the enzymatic composition comprises a cellobiohydrolase and a beta-glucosidase.In another aspect, the enzymatic composition comprises an endoglucanase, a cellobiohydrolase, and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises an endoglucanase, a beta-glucosidase, and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises a cellobiohydrolase, a beta-glucosidase, and a polypeptide with improved cellulolytic activity. In another aspect, the enzymatic composition comprises an endoglucanase, a cellobiohydrolase, and a beta-glucosidase. In another aspect, the enzymatic composition comprises an endoglucanase, a cellobiohydrolase, a beta-glucosidase, and a polypeptide with improved cellulolytic activity. [000237] In another aspect, the enzymatic composition comprises an acetylmannan esterase. In another aspect, the enzymatic composition comprises an acetylxylan esterase. In another aspect, the enzymatic composition comprises an arabinanase (e.g., alpha-L-arabinanase). In another aspect, the enzymatic composition comprises a Petition 870210014734, dated 12 / 02 / 2021, p. 87 / 154 / 141 arabinofuranosidase (e.g., alpha-L-arabinofuranosidase). In another aspect, the enzymatic composition comprises a coumaric acid esterase. In another aspect, the enzymatic composition comprises a feruloyl esterase. In another aspect, the enzymatic composition comprises a galactosidase (e.g., alpha-galactosidase and / or beta-galactosidase). In another aspect, the enzymatic composition comprises a glucuronidase (e.g., alpha-D-glucuronidase). In another aspect, the enzymatic composition comprises a glucuronyl esterase. In another aspect, the enzymatic composition comprises a mannanase. In another aspect, the enzymatic composition comprises a mannosidase (e.g., beta-mannosidase). In another aspect, the enzymatic composition comprises a xylanase. In a preferred aspect, the xylanase is a xylanase from family 10.In another aspect, the enzymatic composition includes a xylosidase (for example, beta-xylosidase). [000238] In another aspect, the enzymatic composition comprises an esterase. In another aspect, the enzymatic composition comprises an expansin. In another aspect, the enzymatic composition comprises a laccase. In another aspect, the enzymatic composition comprises a lignolytic enzyme. In a preferred aspect, the lignolytic enzyme is a manganese peroxidase. In another preferred aspect, the lignolytic enzyme is a lignin peroxidase. In another preferred aspect, the lignolytic enzyme is a water-producing enzyme. In another aspect, the enzymatic composition comprises a pectinase. In another aspect, the enzymatic composition comprises a peroxidase. In another aspect, the enzymatic composition comprises a protease. In another aspect, the enzymatic composition comprises a swolenin. [000239] In the processes of the present invention, the enzyme(s) may be added before or during saccharification, saccharification and fermentation, or fermentation. Petition 870210014734, dated 12 / 02 / 2021, pages 88 / 154 / 141 [000240] One or more (e.g., several) components of the enzyme composition may be wild-type proteins, recombinant proteins, or a combination of wild-type and recombinant proteins. For example, one or more (e.g., several) components may be natural proteins of a cell, which are used as a host cell to recombinantly express one or more (e.g., several) other components of the enzyme composition. One or more (e.g., several) components of the enzyme composition may be produced as monocomponents, which are then combined to form the enzyme composition. The enzyme composition may be a combination of multicomponent and monocomponent protein preparations. [000241] The enzymes used in the processes of the present invention may be in any suitable form for use, such as, for example, a fermentation broth formulation or a cell composition, a cell lysate with or without cell debris, a semi-purified or purified enzyme preparation, or a host cell as a source of the enzymes. The enzyme composition may be a dry powder or granules, a granules that are not in powder form, a liquid, a stabilized liquid, or a stabilized protected enzyme. Liquid enzyme preparations, for example, may be stabilized by adding stabilizers such as a sugar, a sugar alcohol or another polyol, and / or lactic acid or another organic acid, according to the established processes. [000242] The ideal quantities of enzymes and polypeptides with beta-xylosidase activity depend on several factors including, but not limited to, the mixture of cellulolytic and / or hemicellulolytic enzyme components, the cellulosic or xylan-containing material, the concentration of cellulosic or xylan-containing material, the pretreatment(s) of the cellulosic or xylan-containing material, temperature, time, pH, and inclusion of fermenting organism (e.g., yeast for Saccharification and Petition 870210014734, dated 12 / 02 / 2021, pages 89 / 154 / 141 Simultaneous Fermentation). [000243] In one aspect, an efficient amount of cellulolytic or hemicellulolytic enzyme for cellulosic or xylan-containing material is about 0.5 to about 50 mg, for example, about 0.5 to about 40 mg, about 0.5 to about 25 mg, about 0.75 to about 20 mg, about 0.75 to about 15 mg, about 0.5 to about 10 mg, or about 2.5 to about 10 mg per g of cellulosic or xylan-containing material. [000244] In another aspect, an efficient amount of a polypeptide with beta-xylosidase activity for cellulosic or xylan-containing material is about 0.01 to about 50.0 mg, for example, about 0.01 to about 40 mg, about 0.01 to about 30 mg, about 0.01 to about 20 mg, about 0.01 to about 10 mg, about 0.01 to about 5 mg, about 0.025 to about 1.5 mg, about 0.05 to about 1.25 mg, about 0.075 to about 1.25 mg, about 0.1 to about 1.25 mg, about 0.15 to about 1.25 mg, or about 0.25 to about 1.0 mg per gram of material cellulosic or containing xylan. [000245] In another aspect, an efficient amount of a polypeptide with beta-xylosidase activity for the cellulolytic or hemicellulolytic enzyme is about 0.005 to about 1.0 g, for example, about 0.01 to about 1.0 g, about 0.15 to about 0.75 g, about 0.15 to about 0.5 g, about 0.1 to about 0.5 g, about 0.1 to about 0.25 g, or about 0.05 to about 0.2 g per gram of cellulolytic or hemicellulolytic enzyme. [000246] Polypeptides with cellulolytic enzyme activity or hemicellulolytic enzyme activity, as well as other proteins / polypeptides used in the degradation of cellulosic material or containing xylan, for example, GH61 polypeptides with improved cellulolytic activity (collectively hereafter “polypeptides with enzymatic activity”), may be derived from or obtained from any suitable source, including bacterial, fungal, yeast, plant or mammalian origin. The Petition 870210014734, dated 12 / 02 / 2021, p. 90 / 154 / 141 The term “obtained” also means here that the enzyme may have been recombinantly produced in a host organism using methods described herein, wherein the recombinantly produced enzyme is either natural or foreign to the host organism, or has a modified amino acid sequence, for example, with one or more (e.g., several) amino acids that are eliminated, inserted and / or substituted, i.e., a recombinantly produced enzyme that is a mutant and / or a fragment of a natural amino acid sequence, or an enzyme produced by nucleic acid scrambling processes known in the art. Natural variants are included in the meaning of a natural enzyme, and recombinant variants, such as site-directed mutagenesis or scrambling, are included in the meaning of a foreign enzyme. [000247] A polypeptide with enzymatic activity may be a bacterial polypeptide. For example, the polypeptide may be a polypeptide from a Gram-positive bacterium, such as a polypeptide with enzymatic activity from Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, Caldicellulosiruptor, Acidothermus, Thermobifidia, or Oceanobacillus, or a polypeptide from a Gram-negative bacterium such as a polypeptide with enzymatic activity from E. coli, Pseudomonas, Salmonella, Campylobacter, Helicobacter, Flavobacterium, Fusobacterium, Ilyobacter, Neisseria, or Ureaplasma. [000248] In one aspect, the polypeptide is a polypeptide with enzymatic activity from Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus subtilis or Bacillus thuringiensis. Petition 870210014734, of 12 / 02 / 2021, p. 91 / 154 / 141 [000249] In another aspect, the polypeptide is a polypeptide with enzymatic activity from Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberi, or Streptococcus equi subsp. Zooepidemic. [000250] In another aspect, the polypeptide is a polypeptide with enzymatic activity from Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus or Streptomyces lividans. [000251] The polypeptide with enzymatic activity may also be a fungal polypeptide, and more preferably a yeast polypeptide such as a polypeptide with enzymatic activity from Candida, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces or Yarrowia; or more preferably a filamentous fungal polypeptide such as a polypeptide with enzymatic activity from Acremonium, Agaricus, Alternaria, Aspergillus, Aureobasidium, Botryospaeria, Ceriporiopsis, Chaetomidium, Chrysosporium, Claviceps, Cochliobolus, Coprinopsis, Coptotermes, Corynascus, Cryphonectria, Cryptococcus, Diplodia, Exidia, Filibasidium, Fusarium, Gibberella, Holomastigotoides, Humicola, Irpex, Lentinula, Leptospaeria, Magnaporthe, Melanocarpus, Meripilus, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Piromyces, Poitrasia, Pseudoplectania, Pseudotrichonympha, Rhizomucor, Schizophyllum, Scytalidium, Talaromyces, Thermoascus, Thielavia, Tolypocladium, Trichoderma, Trichophaea, Verticillium, Volvariella or Xylaria. [000252] In one aspect, the polypeptide is a polypeptide with enzymatic activity from Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces norbensis or Saccharomyces oviformis. [000253] In another aspect, a polypeptide is a polypeptide with Petition 870210014734, of 12 / 02 / 2021, p. 92 / 154 / 141 enzymatic activity of Acremonium cellulolxlicus, Aspergillus aculeatus, Aspergillus awamori, Aspergillus fumigatus, Aspergillus foetidus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Chrysosporium keratinophilum, Chrysosporium lucknowense, Chrysosporium tropicum, Chrysosporium merdarium, Chrysosporium inops, Chrysosporium pannicola, Chrysosporium queenslandicum, Chrysosporium zonatum, Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusarium venenatum, Humicola grisea, Humicola insolens, Humicola lanuginosa, Irpex lacteus, Mucor miehei, Myceliophthora thermophila, Neurospora thick,Penicillium funiculosum, Penicillium purpurogenum, Phanerochaete chrysosporium, Thielavia achromatica, Thielavia albomyces, Thielavia albopilosa, Thielavia australeinsis, Thielavia fimeti, Thielavia microspora, Thielavia ovispora, Thielavia peruviana, Thielavia spededonium, Thielavia setosa, Thielavia subthermophila, Thielavia terrestris, Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, Trichoderma viride or Trichophaea saccata. [000254] Chemically modified or protein-engineered mutants can also be used. [000255] One or more (several) components of the enzyme composition may be a recombinant component, that is, produced by cloning a DNA sequence that encodes the single component and subsequently transforming the cell with the DNA sequence and expressing it in a host (see, for example, WO 91 / 17243 and WO 91 / 17244). The host is preferably a heterologous host (the enzyme is foreign to the host). Petition 870210014734, dated 12 / 02 / 2021, p. 93 / 154 / 141 host), but the host can also, under certain conditions, be a homologous host (the enzyme is natural to the host). Single-component cellulolytic proteins can also be prepared by purifying such a protein from a fermentation broth. [000256] In one aspect, one or more (e.g., several) cellulolytic enzymes comprise a commercial cellulolytic enzyme preparation. Examples of commercial cellulolytic enzyme preparations suitable for use in the present invention include, for example, CELLIC® CTec (Novozymes A / S), CELLIC® CTec2 (Novozymes A / S), CELLUCLAST™ (Novozymes A / S), NOVOZYM™ 188 (Novozymes A / S), CELLUZYME™ (Novozymes A / S), CEREFLO™ (Novozymes A / S), and ULTRAFLO™ (Novozymes A / S), ACCELERASE™ (Genencor Int.), LAMINEX™ (Genencor Int.), SPEZYME™ CP (Genencor Int.), FILTRASE® NL (DSM); METHAPLUS® S / L 100 (DSM), ROHAMENT™ 7069 W (Rohm GmbH), FIBREZYME® LDI (Dyadic International, Inc.), FIBREZYME® LBR (Dyadic International, Inc.), or VISCOSTAR® 150L (Dyadic International, Inc.). Cellulase enzymes are added in effective amounts of about 0.001 to about 5.0% by weight of solids, for example, about 0.025 to about 4.0% by weight of solids, or about 0.005 to about 2.0% by weight of solids. [000257] Examples of bacterial endoglucanases that can be used in the methods of the present invention include, but are not limited to, an endoglucanase from Acidothermus cellulolyticus (WO 91 / 05039; WO 93 / 15186; US patent 5,275,944; WO 96 / 02551; US ​​patent 5,536,655, WO 00 / 70031, WO 05 / 093050); endoglucanase III from Thermobifida fusca (WO 05 / 093050) and endoglucanase V from Thermobifida fusca (WO 05 / 093050). [000258] Examples of fungal endoglucanases that can be used in the present invention include, but are not limited to, an endoglucanase I from Trichoderma reesei (Penttila et al., 1986, Gene 45: 253-263, endoglucanase I Petition 870210014734, dated 12 / 02 / 2021, p. 94 / 154 / 141 from Trichoderma reesei Cel7B (GENBANK™ accession number M15665), endoglucanase II from Trichoderma reesei (Saloheimo, et al., 1988, Gene 63:11-22), endoglucanase II from Trichoderma reesei Cel5A (GENBANK™ accession number M19373), endoglucanase III from Trichoderma reesei (Okada et al., 1988, Appl. Environ. Microbiol. 64: 555-563, GENBANK™ accession number AB003694), endoglucanase V from Trichoderma reesei (Saloheimo et al., 1994, Molecular Microbiology 13: 219-228, accession number AB003694). GENBANK™ number Z33381), endoglucanase from Aspergillus aculeatus (Ooi et al., 1990, Nucleic Acids Research 18: 5884), endoglucanases from Aspergillus kawachii (Sakamoto et al., 1995, Current Genetics 27: 435-439), endoglucanase from Erwinia carotovara (Saarilahti et al., 1990, Gene 90: 9-14), endoglucanase from Fusarium oxysporum (GENBANK™ accession number L29381), endoglucanase from Humicola grisea var.thermoidea (GENBANK™ accession number AB003107), endoglucanases from Melanocarpus albomyces (GENBANK™ accession number MAL515703), endoglucanases from Neurospora crassa (GENBANK™ accession number XM_324477), endoglucanase V from Humicola insolens, endoglucanases from Myceliophthora thermophila CBS 117.65, endoglucanases from basidiomycete CBS 495.95, endoglucanases from basidiomycete CBS 494.95, endoglucanases from Thielavia terrestris NRRL 8126 CEL6B, endoglucanases from Thielavia terrestris NRRL 8126 CEL6C, endoglucanases from Thielavia terrestris NRRL 8126 CEL7C, endoglucanases from Thielavia terrestris NRRL 8126 CEL7E, endoglucanases from Thielavia terrestris NRRL 8126 CEL7F, endoglucanases from Cladorrhinum foecundissimum ATCC 62373 CEL7A and endoglucanase from Trichoderma reesei strain number VTT-D-80133 (GENBANK™ accession number M15665). [000259] Examples of cellobiohydrolases used in the present invention include, but are not limited to, cellobiohydrolase II from Aspergillus aculeatus (WO 2011 / 059740), cellobiohydrolase I from Chaetomium Petition 870210014734, dated 12 / 02 / 2021, page. 95 / 154 / 141 thermophilum, cellobiohydrolase II from Chaetomium thermophilum, cellobiohydrolase I from Humicola insolens, cellobiohydrolase II from Myceliophthora thermophila (WO 2009 / 042871), cellobiohydrolase II from Thielavia hyrcanie (WO 2010 / 141325), cellobiohydrolase II from Thielavia terrestris (CEL6A, WO 2006 / 074435), cellobiohydrolase I from Trichoderma reesei, cellobiohydrolase II from Trichoderma reesei and cellobiohydrolase II from Trichophaea saccata (WO 2010 / 057086). [000260] Examples of beta-glucosidases used in the present invention include, but are not limited to, beta-glucosidases from Aspergillus aculeatus (Kawaguchi et al., 1996, Gene 173: 287-288), Aspergillus fumigatus (WO 2005 / 047499), Aspergillus niger (Dan et al., 2000, J. Biol. Chem. 275: 49734980), Aspergillus oryzae (WO 2002 / 095014), Penicillium brasilianum IBT 20888 (WO 2007 / 019442 and WO 2010 / 088387), Thielavia terrestris (WO 2011 / 035029) and Trichophaea saccata (WO 2007 / 019442). [000261] Beta-glucosidase may be a fusion protein. In one aspect, beta-glucosidase is a BG variant fusion protein of Aspergillus oryzae beta-glucosidase (WO 2008 / 057637) or a fusion protein of Aspergillus oryzae beta-glucosidase (WO 2008 / 057637). [000262] Other endoglucanases, cellobiohydrolases and beta-glucosidases used are revealed in several glycosyl hydrolase families, using the classification according to Henrissat, B., 1991, A classification of glycosyl hydrolases based on amino-acid sequence similarities, Biochem. J. 280: 309-316, and Henrissat, B., and Bairoch, A., 1996, Updating the sequence-based classification of glycosyl hydrolases, Biochem. J. 316: 695-696. [000263] Other cellulolytic enzymes that can be used in the present invention are described in WO 98 / 13465, WO 98 / 015619, WO 98 / 015633, WO 99 / 06574, WO 99 / 10481, WO 99 / 025847, WO 99 / 031255, WO 2002 / 101078, WO 2003 / 027306, WO 2003 / 052054, WO 2003 / 052055, WO 2003 / 052056, WO 2003 / 052057, WO 2003 / 052118, WO 2004 / 016760, WO Petition 870210014734, dated 12 / 02 / 2021, pages 96 / 154 / 141 2004 / 043980, WO 2004 / 048592, WO 2005 / 001065, WO 2005 / 028636, WO 2005 / 093050, WO 2005 / 093073, WO 2006 / 074005, WO 2006 / 117432, WO 2007 / 071818, WO 2007 / 071820, WO 2008 / 008070, WO 2008 / 008793, US patent 5,457,046, US patent 5,648,263 and US patent 5,686,593. [000264] In the processes of the present invention, any GH61 polypeptide with improved cellulolytic activity can be used as a component of the enzyme composition. [000265] Examples of GH61 polypeptides with improved cellulolytic activity used in the processes of the present invention include, but are not limited to, GH61 polypeptides from Thielavia terrestris (WO 2005 / 074647, WO 2008 / 148131, and WO 2011 / 035027), Thermoascus aurantiacus (WO 2005 / 074656 and WO 2010 / 065830), Trichoderma reesei (WO 2007 / 089290), Myceliophthora thermophila (WO 2009 / 085935, WO 2009 / 085859, WO 2009 / 085864, WO 2009 / 085868), Aspergillus fumigatus (WO 2010 / 138754), GH61 polypeptides from Penicillium pinophilum (WO 2011 / 005867), Thermoascus sp. (WO 2011 / 039319), Penicillium sp. (WO 2011 / 041397), and Thermoascus crustaceous (WO 2011 / 041504). [000266] In one aspect, the GH61 polypeptide with improved cellulolytic activity is used in the presence of a soluble divalent metal activation cation, according to WO 2008 / 151043, for example, manganese or copper. [000267] In another aspect, the GH61 polypeptide with improved cellulolytic activity is used in the presence of a dioxy compound, a bicyclic compound, a heterocyclic compound, a nitrogen-containing compound, a quinone compound, a sulfur-containing compound, or a liquor obtained from a pre-treated cellulosic material, such as pre-treated corn residue (PCS). [000268] The dioxy compound may include any suitable compound containing two or more oxygen atoms. In some respects, dioxy compounds contain a substituted aryl moiety, as described herein. The Petition 870210014734, dated 12 / 02 / 2021, page 97 / 154 / 141 Dioxy compounds may comprise one or more (e.g., several) hydroxyl groups and / or hydroxyl derivatives, but also include substituted aryl moieties that do not contain a hydroxyl group and hydroxyl derivatives.Non-limiting examples of dioxy compounds include pyrocatechol or catechol; caffeic acid; 3,4-dihydroxybenzoic acid; 4-tert-butyl-5-methoxy-1,2-benzenediol; pyrogallol; gallic acid; methyl-3,4,5-trihydroxybenzoate; 2,3,4-trihydroxybenzophenone; 2,6-dimethoxyphenol; sinapinic acid; 3,5-dihydroxybenzoic acid; 4-chloro-1,2-benzenediol; 4-nitro-1,2-benzenediol; tannic acid; ethyl gallate; methyl glycolate; dihydroxyfumaric acid; 2-butyne-1,4-diol; (croconic acid; 1,3-propanediol; tartaric acid; 2,4-pentanediol; 3-ethoxy-1,2-propanediol; 2,4,4'-trihydroxybenzophenone; cis-2-butene-1,4-diol; 3,4-dihydroxy-3-cyclobutene-1,2-dione; dihydroxyacetone; acrolein acetal; methyl-4-hydroxybenzoate; 4-hydroxybenzoic acid and methyl-3,5-dimethoxy-4-hydroxybenzoate, or a salt or solvate thereof. [000269] The bicyclic compound may include any suitable substituted fused ring system, as described herein. The compounds may comprise one or more (e.g., multiple) additional rings, and are not limited to a specific number of rings unless otherwise stated. In one aspect, the bicyclic compound is a flavonoid. In another aspect, the bicyclic compound is an optionally substituted isoflavonoid. In yet another aspect, the bicyclic compound is an optionally substituted flavylium ion, such as an optionally substituted anthocyanidin or anthocyanin, or derivatives thereof. Non-limiting examples of bicyclic compounds include epicatechin; quercetin; myricetin; taxifolin; kaempferol; morin; acacetin; naringenin; isorhamnetin; apigenin; cyanidin; cyanin; curomanin; ceracyanin or a salt or solvate thereof. [000270] The heterocyclic compound can be any suitable compound, such as an aromatic or optionally non-aromatic ring. Petition 870210014734, dated 12 / 02 / 2021, p. 98 / 154 / 141 substituted comprising a heteroatom, as described herein. In one aspect, the heterocyclic compound is a compound comprising an optionally substituted heterocycloalkyl moiety, or an optionally substituted heteroaryl moiety. In another aspect, the optionally substituted heterocycloalkyl moiety, or optionally substituted heteroaryl moiety, is an optionally substituted 5-membered heterocycloalkyl moiety or an optionally substituted 5-membered heteroaryl moiety.In another aspect, the optionally substituted heterocycloalkyl or optionally substituted heteroaryl moiety is an optionally substituted moiety selected from pyrazolyl, furanyl, imidazolyl, isoxazolyl, oxadiazolyl, oxazolyl, pyrrolyl, pyridyl, pyrimidinyl, pyridazinyl, thiazolyl, triazolyl, tienyl, dihydrothienopyrazolyl, tianaftenyl, carbazolyl, benzimidazolyl, benzothienyl, benzofuranyl, indolyl, quinolinyl, benzotriazolyl, benzothiazolyl, benzooxazolyl, benzimidazolyl, isoquinolinyl, isoindolyl, acridinyl, benzoisazolyl, dimethylhydantoin, pyrazinyl, tetrahydrofuranyl, pyrrolinyl, pyrrolidinyl, morpholinyl, indolyl, diazepinyl, azepinyl, tiepinyl, piperidinyl, and oxepinil. In another aspect, the optionally substituted heterocycloalkyl moiety, or optionally substituted heteroaryl moiety, is an optionally substituted furanyl.Non-limiting examples of heterocyclic compounds include (1,2-dihydroxyethyl)-3,4-dihydroxyfuran-2(5H)-one; 4-hydroxy-5-methyl-3-furanone; 5-hydroxy-2(5H)-furanone; [1,2-dihydroxyethyl]furan-2,3,4(5H)trione; α-hydroxy-γ-butyrolactone; ribonic γ-lactone; aldoexuronic acid γ-lactone; gluconic acid δ-lactone; 4-hydroxycoumarin; dihydrobenzofuran; 5-(hydroxymethyl)furfural; furoin; 2(5H)-furanone; 5,6-dihydro-2H-pyran-2-one; and 5,6-dihydro-4-hydroxy-6-methyl-2H-pyran-2-one; or a salt or solvate thereof. [000271] The nitrogen-containing compound can be any suitable compound with one or more nitrogen atoms. In one aspect, the compound Petition 870210014734, dated 12 / 02 / 2021, page 99 / 154 / 141 containing nitrogen comprises an amine, imine, hydroxylamine or nitroxide fraction. Non-limiting examples of nitrogen-containing compounds include acetone oxime; violuric acid; pyridine-2-aldoxime; 2-aminophenol; 1,2-benzenediamine; 2,2,6,6-tetramethyl-1-piperidinyloxy; 5,6,7,8-tetrahydrobiopterin; 6,7-dimethyl-5,6,7,8-tetrahydropterin and maleamic acid; or a salt or solvate thereof. [000272] The quinone compound may be any suitable compound comprising a quinone moiety in the manner described herein. Non-limiting examples of quinone compounds include 1,4-benzoquinone; 1,4-naphthoquinone; 2-hydroxy-1,4-naphthoquinone; 2,3-dimethoxy-5-methyl-1,4-benzoquinone or coenzyme Q0; 2,3,5,6-tetramethyl-1,4-benzoquinone or duroquinone; 1,4-dihydroxyanthraquinone; 3-hydroxy-1-methyl-5,6-indolinedione or adrenochrome; 4-tert-butyl-5-methoxy-1,2-benzoquinone; pyrroloquinoline quinone; or a salt or solvate thereof. [000273] The sulfur-containing compound may be any suitable compound comprising one or more sulfur atoms. In one aspect, the sulfur-containing compound comprises a selected fraction of thionyl, thioether, sulfinyl, sulfonyl, sulfonamide, sulfonamide, sulfonic acid, and sulfonic ester. Non-limiting examples of sulfur-containing compounds include ethanethiol; 2-propanethiol; 2-propene-1-thiol; 2-mercaptoethanesulfonic acid; benzenethiol; benzene-1,2-dithiol; cysteine; methionine; glutathione; cystine; or a salt or solvate thereof. [000274] In one aspect, an efficient amount of a compound such as that described above for cellulosic material as a molar ratio in cellulose glucosyl units is about 10⁻⁶ to about 10, for example, about 10⁻⁶ to about 7.5, about 10⁻⁶ to about 5, about 10⁻⁶ to about 2.5, about 10⁻⁶ to about 1, about 10⁻⁵ to about 1, about 10⁻⁵ to about 10⁻¹, about 10⁻⁴ to about 10⁻¹, about 10⁻³ to about 10⁻¹, or about 10⁻³ to about 10⁻². In another aspect, an amount Petition 870210014734, dated 02 / 12 / 2021, page. 100 / 154 / 141 efficient of a compound as described above is about 0.1 μM to about 1 M, for example, about 0.5 μM to about 0.75 M, about 0.75 μM to about 0.5 M, about 1 μM to about 0.25 M, about 1 μM to about 0.1 M, about 5 μM to about 50 mM, about 10 μM to about 25 mM, about 50 μM to about 25 mM, about 10 μM to about 10 mM, about 5 μM to about 5 mM, or about 0.1 mM to about 1 mM. [000275] The term “liquor” means the solution phase, whether aqueous, organic, or a combination thereof, that arises from the treatment of a material with lignocellulose and / or hemicellulose in a slurry, or monosaccharides thereof, for example, xylose, arabinose, mannose, etc., under conditions as described herein, and the soluble contents thereof. A liquor for cellulolytic enhancement of a GH61 polypeptide can be produced by treating a material with lignocellulose or hemicellulose (or raw material), applying heat and / or pressure, optionally in the presence of a catalyst, for example, acid, optionally in the presence of an organic solvent, and optionally in combination with physical disruption of the material, and then separating the solution from the residual solids. Such conditions determine the degree of cellulolytic enhancement obtained by combining liquor and a GH61 polypeptide during the hydrolysis of a cellulosic substrate by a cellulase preparation.The liquor can be separated from the treated material using a standard method in the art, such as filtration, sedimentation, or centrifugation. [000276] In one aspect, an efficient amount of liquor for cellulose is about 10-6a about 10 g per g of cellulose, for example, about 10-6a about 7.5 g, about 10-6a about 5, about 10-6a about 2.5 g, about 10-6a about 1 g, about 10-5a about 1 g, about 10-5a about 10-1 g, about 10-4 about 10-1 g, about 10-3a about 10-1 g, or about 10-3a about 10-2 g per g of cellulose. [000277] In one aspect, to one or more (e.g., several) enzymes Petition 870210014734, dated 12 / 02 / 2021, page 101 / 154 / 141 hemicellulolytic enzymes comprise a commercial preparation of hemicellulolytic enzyme. Examples of commercial hemicellulolytic enzyme preparations suitable for use in the present invention include, for example, SHEARZYME™ (Novozymes A / S), CELLIC® HTec (Novozymes A / S), CELLIC® HTec2 (Novozymes A / S), VISCOZYME® (Novozymes A / S), ULTRAFLO® (Novozymes A / S), PULPZYME® HC (Novozymes A / S), MULTIFECT® Xylanase (Genencor), ACCELLERASE® XY (Genencor), ACCELLERASE® XC (Genencor), ECOPULP® TX-200A (AB Enzimas), HSP 6000 Xylanase (DSM), DEPOL™ 333P (Biocatalysts Limited, Wales, UK), DEPOL™ 740L. (Biocatalysts Limit, Wales, UK), and DEPOL™ 762P (Biocatalysts Limit, Wales, UK). [000278] Examples of xylanases used in the processes of the present invention include, but are not limited to, xylanases from Aspergillus aculeatus (GeneSeqP:AAR63790; WO 94 / 21785), Aspergillus fumigatus (WO 2006 / 078256), Penicillium pinophilum (WO 2011 / 041405), Penicillium sp. (WO 2010 / 126772), Thielavia terrestris NRRL 8126 (WO 2009 / 079210) and Trichophaea saccata GH10 (WO 2011 / 057083). [000279] Examples of beta-xylosidases used in the processes of the present invention include, but are not limited to, beta-xylosidases from Neurospora crassa (SwissProt accession number Q7SOW4), Trichoderma reesei (UniProtKB / TrEMBL accession number Q92458), and Talaromyces emersonii (SwissProt accession number Q8X212). [000280] Examples of acetylxylan esterases used in the processes of the present invention include, but are not limited to, acetylxylan esterases from Aspergillus aculeatus (WO 2010 / 108918), Chaetomium globosum (UniProt accession number Q2GWX4), Chaetomium gracile (GeneSeqP accession number AAB82124), Humicola insolens DSM 1800 (WO 2009 / 073709), Hypocrea jecorina (WO 2005 / 001036), Myceliophtera thermophila (WO 2010 / 014880), Neurospora crassa (UniProt accession number q7s259), Petition 870210014734, dated 12 / 02 / 2021, pages 102 / 154 / 141 Phaeosphaeria nodorum (Uniprot accession number Q0UHJ1) and Thielavia terrestris NRRL 8126 (WO 2009 / 042846). [000281] Examples of feruloyl esterases (ferulic acid esterases) used in the processes of the present invention include, but are not limited to, feruloyl esterases from Humicola insolens DSM 1800 (WO 2009 / 076122), Neosartorya fischeri (UniProt accession number A1D9T4), Neurospora crassa (UniProt accession number Q9HGR3), Penicillium aurantiogriseum (WO 2009 / 127729) and Thielavia terrestris (WO 2010 / 053838 and WO 2010 / 065448). [000282] Examples of arabinofuranosidases used in the processes of the present invention include, but are not limited to, arabinofuranosidases from Aspergillus niger (GeneSeqP accession number AAR94170), Humicola insolens DSM 1800 (WO 2006 / 114094 and WO 2009 / 073383) and M. giganteus (WO 2006 / 114094). [000283] Examples of alpha-glucuronidases used in the processes of the present invention include, but are not limited to, alpha-glucuronidases from Aspergillus clavatus (UniProt accession number alcc12), Aspergillus fumigatus (SwissProt accession number Q4WW45), Aspergillus niger (UniProt accession number Q96WX9), Aspergillus terreus (SwissProt accession number Q0CJP9), Humicola insolens (WO 2010 / 014706), Penicillium aurantiogriseum (WO 2009 / 068565), Talaromyces emersonii (UniProt accession number Q8X211) and Trichoderma reesei (UniProt accession number Q99024). [000284] The polypeptides with enzymatic activity, used in the processes of the present invention, can be produced by fermentation of the microbial strains mentioned above in a nutrient medium containing suitable sources of carbon and nitrogen and inorganic salts, using procedures known in the art (see, for example, Bennett, JW and LaSure, L. (eds.), More Gene Manipulations in Fungi, Academic Press, CA, Petition 870210014734, dated 12 / 02 / 2021, pages 103 / 154 / 141 (1991). Suitable media are available from commercial suppliers, or can be prepared according to published compositions (e.g., in catalogs of the American Type Culture Collection). The temperature ranges and other conditions suitable for growth and enzyme production are known in the art (see, for example, Bailey, JE, and Ollis, DF, Biochemical Engineering Fundamentals, McGraw-Hill Book Company, NY, 1986). [000285] Fermentation can be any method of culturing a cell that results in the expression or isolation of an enzyme or protein. Therefore, fermentation can be understood as that which comprises shake flask cultivation, or small- or large-scale fermentation (including continuous, batch, fed-batch, or solid-state fermentations) in laboratory or industrial fermenters, carried out in a suitable medium and under conditions that allow the enzyme to be expressed or isolated. The resulting enzymes produced by the methods described above can be recovered from the fermentation medium and purified by conventional procedures. [000286] Fermentation. Fermentable sugars obtained from cellulosic material or containing hydrolyzed xylan can be fermented by one or more (e.g., several) fermenting microorganisms capable of fermenting the sugars directly or indirectly into a desired fermentation product. “Fermentation” or “fermentation process” refers to any fermentation process or any process comprising a fermentation step. Fermentation processes also include fermentation processes used in the alcohol consumption industry (e.g., beer and wine), the baking industry (e.g., fermented bakery products), the leather industry, and the tobacco industry. Fermentation conditions depend on the desired fermentation product and the fermenting organism, and can be easily determined by those skilled in the art. Petition 870210014734, dated 12 / 02 / 2021, pages 104 / 154 / 141 [000287] In the fermentation stage, the sugars, released from the cellulosic or xylan-containing material as a result of the pretreatment and enzymatic hydrolysis stages, are fermented into a product, for example, ethanol, by a fermenting organism such as yeast. Hydrolysis (saccharification) and fermentation can be separate or simultaneous, as described herein. [000288] Any suitable cellulosic material or material containing hydrolyzed xylan can be used in the fermentation step in the practice of the present invention. The material is generally selected based on the desired fermentation product, i.e., the substance to be obtained from the fermentation, and the process employed, in the manner well known in the art. [000289] It is understood here that the term “fermentation medium” refers to a medium before the fermenting microorganism(s) is / are added, such as a medium resulting from a saccharification process, as well as a medium used in a simultaneous saccharification and fermentation (SSF) process. [000290] “Fermenting microorganism” refers to any microorganism, including bacterial and fungal organisms, suitable for use in a desired fermentation process to produce a fermentation product. The fermenting organism may be hexose and / or pentose fermenting organisms, or a combination thereof. Both hexose and pentose fermenting organisms are well known in the art. Suitable fermenting microorganisms are capable of fermenting, that is, converting sugars, such as glucose, xylose, xylulose, arabinose, maltose, mannose, galactose and / or oligosaccharides, directly or indirectly into the desired fermentation product.Examples of bacterial and fungal fermenting organisms that produce ethanol are described by Lin et al., 2006, Appl. Microbiol. Biotechnol. 69: 627-642. [000291] Examples of fermenting microorganisms that can ferment hexose sugars include bacterial and fungal organisms, such as Petition 870210014734, dated 12 / 02 / 2021, pages 105 / 154 / 141, refers to yeast. Preferred yeasts include strains of Candida, Kluyveromyces, and Saccharomyces, for example, Candida sonorensis, Kluyveromyces marxianus, and Saccharomyces cerevisiae. [000292] Examples of fermenting organisms that can ferment pentose sugars in their natural state include bacterial and fungal organisms, such as some yeasts. Preferred xylose-fermenting yeasts include Candida strains, preferably C. sheatae or C. sonorensis; and Pichia strains, preferably P. stipitis, such as P. stipitis CBS 5773. Preferred pentose-fermenting yeasts include Pachysolen strains, preferably P. tannophilus. Organisms that are not capable of fermenting pentose sugars, such as xylose and arabinose, can be genetically modified to do so by methods known in the art. [000293] Examples of bacteria that can efficiently ferment hexose and pentose into ethanol include, for example, Bacillus coagulans, Clostridium acetobutilicum, Clostridium thermocellum, Clostridium phytofermentans, Geobacillus sp., Thermoanaerobacter saccharolyticum and Zymomonas mobilis (Philippidis, 1996, supra). [000294] Other fermenting organisms include strains of Bacillus, such as Bacillus coagulans; Candida, such as C. sonorensis, C. methanosorbosa, C. diddensiae, C. parapsilosis, C. naedodendra, C. blankii, C. entomophilia, C. brassicae, C. pseudotropicalis, C. boidinii, C. utilis and C. scehatae; Clostridium, such as C. acetobutilicum, C. thermocellum and C. phytofermentans; E. coli, especially strains of E. coli that have been genetically modified to improve ethanol yield; Geobacillus sp.; Hansenula, such as Hansenula anomala; Klebsiella, such as K. oxytoca; Kluyveromyces, such as K. marxianus, K. lactis, K. thermotolerans and K. fragilis; Schizosaccharomyces, such as S. pombe; Thermoanaerobacter, such as Thermoanaerobacter saccharolyticum and Zymomonas, such as Zymomonas mobilis. Petition 870210014734, dated 12 / 02 / 2021, pp. 106 / 154 / 141 [000295] In a preferred aspect, the yeast is Bretannomyces. In a more preferred aspect, the yeast is Bretannomyces clausenii. In another preferred aspect, the yeast is Candida. In another more preferred aspect, the yeast is Candida sonorensis. In another more preferred aspect, the yeast is Candida boidinii. In another more preferred aspect, the yeast is Candida blankii. In another more preferred aspect, the yeast is Candida brassicae. In another more preferred aspect, the yeast is Candida diddensii. In another more preferred aspect, the yeast is Candida entomophiliia. In another more preferred aspect, the yeast is Candida pseudotropicalis. In another more preferred aspect, the yeast is Candida scehatae. In another more preferred aspect, the yeast is Candida utilis. In another preferred aspect, the yeast is Clavispora. In another more preferred aspect, the yeast is Clavispora lusitaniae.In another preferred aspect, the yeast is Clavispora opuntiae. In another preferred aspect, the yeast is Kluyveromyces. In another preferred aspect, the yeast is Kluyveromyces fragilis. In another preferred aspect, the yeast is Kluyveromyces marxianus. In another preferred aspect, the yeast is Kluyveromyces thermotolerans. In another preferred aspect, the yeast is Pachysolen. In another preferred aspect, the yeast is Pachysolen tannophilus. In another preferred aspect, the yeast is Pichia. In another preferred aspect, the yeast is Pichia stipitis. In another preferred aspect, the yeast is Saccharomyces spp. In another preferred aspect, the yeast is Saccharomyces cerevisiae. In another preferred aspect, the yeast is Saccharomyces distaticus. In another preferred aspect, the yeast is Saccharomyces uvarum. [000296] In a preferred aspect, the bacterium is a Bacillus. In a more preferred aspect, the bacterium is Bacillus coagulans. In another preferred aspect, the bacterium is a Clostridium. In yet another preferred aspect, the Petition 870210014734, dated 12 / 02 / 2021, pp. 107 / 154 100 / 141 The bacterium is Clostridium acetobutilicum. In another more preferred aspect, the bacterium is Clostridium phytofermentans. In another more preferred aspect, the bacterium is Clostridium thermocellum. In another more preferred aspect, the bacterium is Geobacillus sp. In another more preferred aspect, the bacterium is a Thermoanaerobacter. In another more preferred aspect, the bacterium is Thermoanaerobacter saccharolyticum. In another preferred aspect, the bacterium is a Zymomonas. In another more preferred aspect, the bacterium is Zymomonas mobilis. [000297] Commercially available yeasts suitable for ethanol production include, for example, BIOFERM™ AFT and XR (NABC North American Bioproducts Corporation, GA, United States), ETHANOL RED™ yeast (Fermentis / Lesaffre, United States), FALI™ (Fleischmann's Yeast, United States), FERMIOL™ (DSM Specialties), GERT STRAND™ (Gert Strand AB, Sweden), and fresh SUPERSTART™ and THERMOSACC™ yeast (Ethanol Technology, WI, United States). [000298] In a preferred aspect, the fermenting microorganism was genetically modified to provide the ability to ferment pentose sugars, such as microorganisms that utilize xylose, that utilize arabinose, and that co-utilize xylose and arabinose. [000299] Cloning heterologous genes in several fermenting microorganisms has led to the construction of organisms capable of converting hexoses and pentoses into ethanol (co-fermentation) (Chen and Ho, 1993, Cloning and improving the expression of Pichia stipitis xylose reductase gene in Saccharomyces cerevisiae, Appl. Biochem. Biotechnol. 39-40: 135-147; Ho et al., 1998, Genetically engineered Saccharomyces yeast capable of effectively co-fermenting glucose and xylose, Appl. Environ. Microbiol. 64: 1852-1859; Kotter and Ciriacy, 1993, Xylose fermentation by Saccharomyces cerevisiae, Appl. Microbiol. Biotechnol. 38: 776-783; Walfridsson et al., 1995, Xylosemetabolizing Saccharomyces cerevisiae strains overexpressing the TKL1 and Petition 870210014734, dated 12 / 02 / 2021, pages 108 / 154 101 / 141 TAL1 genes encoding the pentose fosfato pathway enzymes transketolase and transaldolase, Appl. Environ. Microbiol. 61: 4184-4190; Kuyper et al., 2004, Minimal metabolic engineering of Saccharomyces cerevisiae for efficient anaerobic xylose fermentation: a proof of principle, FEMS Yeast Research 4: 655-664; Beall et al., 1991, Parametric studies of ethanol production from xylose and other sugars by recombinant Escherichia coli, Biotech. Bioeng. 38: 296-303; Ingram et al., 1998, Metabolic engineering of bacteria for ethanol production, Biotechnol. Bioeng. 58: 204-214; Zhang et al., 1995, Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis, Science 267: 240-243; Deanda et al., 1996, Development of an arabinose-fermenting Zymomonas mobilis strain by metabolic pathway engineering, Appl. Environ. Microbiol. 62: 4465-4470; WO 2003 / 062430, xilose isomerase). [000300] In a preferred aspect, the genetically modified fermenting microorganism is Candida sonorensis. In another preferred aspect, the genetically modified fermenting microorganism is Escherichia coli. In another preferred aspect, the genetically modified fermenting microorganism is Klebsiella oxytoca. In another preferred aspect, the genetically modified fermenting microorganism is Kluyveromyces marxianus. In another preferred aspect, the genetically modified fermenting microorganism is Saccharomyces cerevisiae. In another preferred aspect, the genetically modified fermenting microorganism is Zymomonas mobilis. [000301] It is well known in the art that the organisms described above can also be used to produce other substances, in the manner described herein. [000302] The fermenting microorganism is typically added to cellulosic material containing degraded or hydrolyzed xylan, and fermentation is carried out for approximately 8 to 96 hours, for example, Petition 870210014734, dated 12 / 02 / 2021, pp. 109 / 154 102 / 141 approximately 24 to approximately 60 hours. The temperature is typically between approximately 26°C and approximately 60°C, for example, approximately 32°C or 50°C, and the pH is approximately 3 to approximately pH 8, for example, pH 4-5, 6, or 7. [000303] In one aspect, yeast and / or another microorganism is applied to the degraded cellulosic material, and fermentation is carried out for about 12 to about 96 hours, such as typically 24-60 hours. In another aspect, the temperature is preferably between about 20 °C to about 60 °C, for example, about 25 °C to about 50 °C, about 32 °C to about 50 °C, or about 32 °C to about 50 °C, and the pH is generally about pH 3 to about pH 7, for example, about pH 4 to about pH 7. However, some fermenting organisms, for example, bacteria, have a higher ideal fermentation temperature. Yeast or another microorganism is preferably applied in quantities of approximately 10⁵ to 10¹², more preferably approximately 10⁷ to 10¹⁰, essentially approximately counts of 2 x 10⁸ viable cells per mL of fermentation broth.Further guidance regarding the use of yeast for fermentation can be found in, for example, “The Alcohol Textbook” (Editors K. Jacques, TP Lyons and DR Kelsall, Nottingham University Press, UK 1999), which is incorporated here by reference. [000304] A fermentation enhancer can be used in combination with any of the processes described herein to further improve the fermentation process and, in particular, the performance of the fermenting microorganism, such as improving the rate and yield of ethanol. A “fermentation enhancer” refers to stimulators for the growth of fermenting microorganisms, in particular, yeasts. Preferred fermentation enhancers for growth include vitamins and minerals. Examples of vitamins include multivitamins, biotin, pantothenate, nicotinic acid, meso-inositol, thiamine, pyridoxine, para-aminobenzoic acid, folic acid, riboflavin, and vitamins A, B, C, D, and E. See, for example. Petition 870210014734, dated 12 / 02 / 2021, pp. 110 / 154 103 / 141 example, Alfenore et al., Improving ethanol production and viability of Saccharomyces cerevisiae by a vitamin feeding strategy during the fed-batch process, Springer-Verlag (2002), which is incorporated here by reference. Examples of minerals include minerals and mineral salts that can supply nutrients comprising P, K, Mg, S, Ca, Fe, Zn, Mn and Cu. [000305] Fermentation products: A fermentation product may be any substance derived from fermentation. The fermentation product may be, without limitation, an alcohol (e.g., arabinitol, n-butanol, isobutanol, ethanol, glycerol, methanol, ethylene glycol, 1,3-propanediol [propylene glycol], butanediol, glycerin, sorbitol and xylitol); an alkane (e.g., pentane, hexane, heptane, octane, nonane, decane, undecane, and dodecane), a cycloalkane (e.g., cyclopentane, cyclohexane, cycloheptane and cyclooctane), an alkene (e.g., pentene, hexene, heptene and octene); an amino acid (e.g., aspartic acid, glutamic acid, glycine, lysine, serine and threonine); a gas (for example, methane, hydrogen (H2), carbon dioxide (CO2) and carbon monoxide (CO)); isoprene; a ketone (for example, acetone);an organic acid (e.g., acetic acid, acetonic acid, adipic acid, ascorbic acid, citric acid, 2,5-diketo-D-gluconic acid, formic acid, fumaric acid, glucaric acid, gluconic acid, glucuronic acid, glutaric acid, 3-hydroxypropionic acid, itaconic acid, lactic acid, malic acid, malonic acid, oxalic acid, oxaloacetic acid, propionic acid, succinic acid, and xylonic acid) and polyketide. The fermentation product may also be protein as a high-value product. [000306] In a preferred aspect, the fermentation product is an alcohol. It will be well understood that the term "alcohol" includes a substance containing one or more hydroxyl moieties. In a more preferred aspect, the alcohol is n-butanol. In another more preferred aspect, the alcohol is isobutanol. In another more preferred aspect, the alcohol is ethanol. In another aspect Petition 870210014734, dated 12 / 02 / 2021, pp. 111 / 154 104 / 141 more preferred, the alcohol is methanol. In another more preferred aspect, the alcohol is arabinitol. In another more preferred aspect, the alcohol is butanediol. In another more preferred aspect, the alcohol is ethylene glycol. In another more preferred aspect, the alcohol is glycerin. In another more preferred aspect, the alcohol is glycerol. In another more preferred aspect, the alcohol is 1,3-propanediol. In another more preferred aspect, the alcohol is sorbitol. In another more preferred aspect, the alcohol is xylitol. See, for example, Gong, CS, Cao, NJ, Du, J., and Tsao, GT, 1999, Ethanol production from renewable resources, in Advances in Biochemical Engineering / Biotechnology, Scheper, T., ed., Springer-Verlag Berlin Heidelberg, Germany, 65: 207-241; Silveira, MM, and Jonas, R., 2002, The biotechnological production of sorbitol, Appl. Microbiol. Biotechnol. 59: 400-408; Nigam, P. and Singh, D., 1995, Processs for fermentative production of xilitol - a sugar substitute, Process Biochemistry 30 (2): 117-124; Ezeji, T.C., Qureshi, N., and Blaschek, H. P., 2003, Production of acetone, butanol and ethanol by Clostridium beijerinckii BA101 e in situ recovery by gas stripping, World Journal of Microbiology and Biotechnology 19 (6): 595-603. [000307] In another preferred aspect, the fermentation product is an alkane. The alkane may be an unbranched or branched alkane. In another more preferred aspect, the alkane is pentane. In another more preferred aspect, the alkane is hexane. In another more preferred aspect, the alkane is heptane. In another more preferred aspect, the alkane is octane. In another more preferred aspect, the alkane is nonane. In another more preferred aspect, the alkane is decane. In another more preferred aspect, the alkane is undecane. In another more preferred aspect, the alkane is dodecane. [000308] In another preferred aspect, the fermentation product is a cycloalkane. In another more preferred aspect, the cycloalkane is cyclopentane. In another more preferred aspect, the cycloalkane is cyclohexane. In another more preferred aspect, the cycloalkane is cycloheptane. Petition 870210014734, dated 12 / 02 / 2021, pp. 112 / 154 105 / 141 In another, more preferred aspect, the cycloalkane is cyclooctane. [000309] In another preferred aspect, the fermentation product is an alkene. The alkene may be an unbranched or branched alkene. In another more preferred aspect, the alkene is pentene. In another more preferred aspect, the alkene is hexene. In another more preferred aspect, the alkene is heptene. In another more preferred aspect, the alkene is octene. [000310] In another preferred aspect, the fermentation product is an amino acid. In another more preferred aspect, the organic acid is aspartic acid. In another more preferred aspect, the amino acid is glutamic acid. In another more preferred aspect, the amino acid is glycine. In another more preferred aspect, the amino acid is lysine. In another more preferred aspect, the amino acid is serine. In another more preferred aspect, the amino acid is threonine. See, for example, Richard, A. and Margaritis, A., 2004, Empirical modeling of batch fermentation kinetics for the production of poly(glutamic acid) and other microbial biopolymers, Biotechnology and Bioengineering 87 (4): 501-515. [000311] In another preferred aspect, the fermentation product is a gas. In another more preferred aspect, the gas is methane. In another more preferred aspect, the gas is H2. In another more preferred aspect, the gas is CO2. In another more preferred aspect, the gas is CO. See, for example, Kataoka, N., A. Miya, and K. Kiriyama, 1997, Studies on hydrogen production by continuous culture system of anaerobic hydrogen-producing bacteria, Water Science and Technology 36 (6-7): 41-47; and Gunaseelan VN, in Biomass and Bioenergy, 13 (1-2): 83-114, 1997, Anaerobic digestion of biomass for methane production: A review. [000312] In another preferred aspect, the fermentation product is isoprene. [000313] In another preferred aspect, the fermentation product is a ketone. It will be well understood that the term “ketone” includes a substance Petition 870210014734, dated 12 / 02 / 2021, pp. 113 / 154 106 / 141 containing one or more ketone fractions. In another, more preferred aspect, the ketone is acetone. See, for example, Qureshi and Blaschek, 2003, supra. [000314] In another preferred aspect, the fermentation product is an organic acid. In another more preferred aspect, the organic acid is acetic acid. In another more preferred aspect, the organic acid is acetonic acid. In another more preferred aspect, the organic acid is adipic acid. In another more preferred aspect, the organic acid is ascorbic acid. In another more preferred aspect, the organic acid is citric acid. In another more preferred aspect, the organic acid is 2,5-diketo-D-gluconic acid. In another more preferred aspect, the organic acid is formic acid. In another more preferred aspect, the organic acid is fumaric acid. In another more preferred aspect, the organic acid is glucaric acid. In another more preferred aspect, the organic acid is gluconic acid. In another more preferred aspect, the organic acid is glucuronic acid. In another more preferred aspect, the organic acid is glutaric acid.In another preferred aspect, the organic acid is 3-hydroxypropionic acid. In another more preferred aspect, the organic acid is itaconic acid. In another more preferred aspect, the organic acid is lactic acid. In another more preferred aspect, the organic acid is malic acid. In another more preferred aspect, the organic acid is malonic acid. In another more preferred aspect, the organic acid is oxalic acid. In another more preferred aspect, the organic acid is propionic acid. In another more preferred aspect, the organic acid is succinic acid. In another more preferred aspect, the organic acid is xylonic acid. See, for example, Chen, R., and Lee, YY, 1997, Membrane-mediated extractive fermentation for lactic acid production from cellulosic biomass, Appl. Biochem. Biotechnol. 63-65: 435-448. [000315] In another preferred aspect, the fermentation product is Petition 870210014734, dated 12 / 02 / 2021, pp. 114 / 154 107 / 141 polyketide. [000316] Recovery. The fermentation product(s) may optionally be recovered from the fermentation medium using any method known in the art including, but not limited to, chromatography, electrophoretic procedures, differential solubility, distillation or extraction. For example, alcohol is separated from the fermented cellulosic or xylan-containing material and purified by conventional distillation methods. Ethanol with a purity of up to about 96% by vol can be obtained, which can be used, for example, as fuel ethanol, ethanol for beverages, i.e., neutral potable spirits or industrial ethanol. Signal peptides [000317] The present invention also relates to an isolated polynucleotide encoding a signal peptide comprising or consisting of amino acids 1 to 19 of SEQ ID NO: 2, amino acids 1 to 19 of SEQ ID NO: 4, amino acids 1 to 19 of SEQ ID NO: 6, amino acids 1 to 21 of SEQ ID NO: 8 or amino acids 1 to 20 of SEQ ID NO: 10. The polynucleotide may further comprise a gene encoding a protein, which is operably linked to the signal peptide. The protein is preferably foreign to the signal peptide. In one aspect, the polynucleotide encoding the signal peptide has nucleotides 1 to 57 with SEQ ID NO: 1. In another aspect, the polynucleotide encoding the signal peptide has nucleotides 1 to 57 with SEQ ID NO: 3. In another aspect, the polynucleotide encoding the signal peptide has nucleotides 1 to 57 with SEQ ID NO: 5. In another aspect, the polynucleotide encoding the signal peptide has nucleotides 1 to 63 with SEQ ID NO: 7.In another aspect, the polynucleotide that encodes the signal peptide has nucleotides 1 to 60 with SEQ ID NO: 9. [000318] The present invention also relates to nucleic acid constructs, expression vectors and recombinant host cells. Petition 870210014734, dated 12 / 02 / 2021, pages 115 / 154 108 / 141 comprising such polynucleotides. [000319] The present invention also relates to methods of producing a protein, comprising (a) growing a recombinant host cell comprising a polynucleotide such as this operably linked to a gene encoding the protein; and optionally (b) recovering the protein. [000320] A protein can be natural or heterologous to a host cell. The term “protein” here does not mean that it refers to a specific size of the encoded product and therefore includes peptides, oligopeptides, and polypeptides. The term “protein” also includes two or more polypeptides combined to form the encoded product. Proteins also include hybrid polypeptides and fused polypeptides. [000321] Preferably, the protein is a hormone, enzyme, receptor or portion thereof, antibody or portion thereof, or reporter. For example, the protein may be a hydrolase, isomerase, ligase, lyase, oxidoreductase, or transferase, for example, an alpha-galactosidase, alpha-glucosidase, aminopeptidase, amylase, beta-galactosidase, beta-glucosidase, betaxylosidase, carbohydrase, carboxypeptidase, catalase, cellobiohydrolase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endoglucanase, esterase, glucoamylase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase. [000322] The gene can be obtained from any proarrhythmic, eukaryotic, or other source. [000323] The present invention is further described by the following examples, which should not be construed as limiting the scope of the invention. Examples Petition 870210014734, dated 12 / 02 / 2021, pp. 116 / 154 109 / 141 Strains [000324] A fungal strain identified as NN047338 was isolated from a soil sample collected from Hunan Province, China, by dilution on PDA plates at 45 °C, and subsequently purified by transferring a single conidium to a YG agar plate. The NN047338 strain was identified as Scytalidium thermophilum, based on both its morphological characteristics and its ITS rDNA sequence. [000325] A fungal strain identified as NN051380 was isolated from a soil sample collected in China by dilution on PDA plates at 25 °C and subsequently purified by transferring a single conidium to a PDA plate. The NN051380 strain was identified as Penicillium oxalicum based on both its morphological characteristics and its ITS rDNA sequence. [000326] A fungal strain identified as NN046782 was isolated from a soil sample collected from China by dilution on PDA plates at 45 °C and subsequently purified by transferring a single conidium to a YG agar plate. The strain NN046872 was identified as Rhizomucor pusillus, based on both its morphological characteristics and its ITS rDNA sequence. [000327] A fungal strain identified as NN044936 was isolated from a soil sample collected from Yunnan Province, China, by dilution on PDA plates at 45 °C and subsequently purified by transferring a single conidium to a YG agar plate. The NN044936 strain was identified as Thermoascus aurantiacus, based on both its morphological characteristics and its ITS rDNA sequence. Means [000328] The PDA plates were composed of 39 grams of potato dextrose agar and deionized water per 1 liter. [000329] The YG agar plates were composed of 5 g of yeast extract, 10 g of glucose, 20 g of agar, and deionized water to make 1 liter. [000330] The YPG medium was composed of 0.4% yeast extract, Petition 870210014734, dated 12 / 02 / 2021, pp. 117 / 154 110 / 141 0.1% KH2PO4, 0.05% MgSO4-7H2O, and 1.5% glucose in deionized water. [000331] The YPM medium consisted of 1% yeast extract, 2% peptone, and 2% maltose in deionized water. [000332] Czapek's medium was composed of 30 g of sucrose, 3 g of NaNÜ3, 0.5 g of MgSÜ4-7H2Ü, 0.01 g of FeSÜ4-7H2Ü, 1 g of K2HPO4, 0.5 g of KCl, and deionized water to make 1 liter. The pH was adjusted to pH 4 with 1 M HCl. [000333] The FG4 medium was composed of 30 g of soy flour, 15 g of maltose, 5 g of Bacto peptone, and deionized water for 1 liter. [000334] The plates with minimal medium were composed of 342 g of sucrose, 20 mL of salt solution, 20 g of agar, and deionized water to make 1 liter. The salt solution was composed of 2.6% KCl, 2.6% MgSO4-7H2O, 7.6% KH2PÜ4, 2 ppm Na2B4Ü7-10H2Ü, 20 ppm CuSÜ4-5H2Ü, 40 ppm FeSÜ4-7H2Ü, 40 ppm MnSÜ4-2H2Ü, 40 ppm Na2MoÜ4-2H2Ü, and 400 ppm ZnSO4-7H2Ü in deionized water. Example 1: Genomic DNA extraction [000335] The Scytalidium thermophilum NN047338 strain was inoculated onto a PDA plate and incubated for 3 days at 45°C in the dark. Several PDA-mycelial plugs were inoculated into 500 mL shaker flasks containing 100 mL of May YPG. The flasks were incubated for 3 days at 45°C with shaking at 160 rpm. The mycelia were collected by filtration using MIRACLÜTH® (Calbiochem, La Jolla, CA, USA) and frozen in liquid nitrogen. The frozen mycelia were ground, using a mortar and pestle, into a fine powder, and genomic DNA was isolated using a DNEASY® Plant Maxi kit (QIAGEN Inc., Valencia, CA, USA) following the manufacturer's instructions. [000336] The Penicillium oxalicum NN051380 strain was inoculated onto a PDA plate and incubated for 5 days at 25°C in the dark. Several plugs of Petition 870210014734, dated 12 / 02 / 2021, pages 118 / 154 111 / 141 PDA mycelia were inoculated into 500 mL shaker flasks containing 100 mL of Czapek's medium. The flasks were incubated for 3 days at 30°C with shaking at 160 rpm. The mycelia were collected by filtration using MIRACLOTH® and frozen in liquid nitrogen. The frozen mycelia were ground, using a mortar and pestle, into a fine powder, and genomic DNA was isolated using a DNEASY® Plant Maxi kit following the manufacturer's instructions. [000337] The Rhizomucor pusillus NN046782 strain was inoculated onto a PDA plate and incubated for 3 days at 45°C in the dark. Several PDA-mycelial plugs were inoculated into 500 mL shaker flasks containing 100 mL of FG4 medium. The flasks were incubated for 3 days at 45°C with shaking at 160 rpm. Mycelia were collected by filtration using MIRACLOTH® and frozen in liquid nitrogen. The frozen mycelia were ground, using a mortar and pestle, into a fine powder, and genomic DNA was isolated using a DNEASY® Plant Maxi kit following the manufacturer's instructions. [000338] The Thermoascus aurantiacus NN044936 strain was inoculated onto a PDA plate and incubated for 3 days at 45°C in the dark. Several PDA-mycelial plugs were inoculated into 500 mL shaker flasks containing 100 mL of May YPG. The flasks were incubated for 3 days at 45°C with shaking at 160 rpm. Mycelia were collected by filtration using MIRACLOTH® and frozen in liquid nitrogen. The frozen mycelia were ground, using a mortar and pestle, into a fine powder, and genomic DNA was isolated using a DNEASY® Plant Maxi kit following the manufacturer's instructions. Example 2: Genome sequencing, assembly, and annotation of the strains Scytalidium thermophilum NN047338, Penicillium oxalicum NN051380, Rhizomucor pusillus NN046782, and Thermoascus aurantiacus NN044936 Petition 870210014734, dated 12 / 02 / 2021, pp. 119 / 154 112 / 141 [000339] The extracted genomic DNA samples were sent to the Beijing Genome Institute (BGI, Shenzhen, China) for genome sequencing using an ILLUMINA® GA2 System (Illumina, Inc., San Diego, CA, United States). The raw reads were assembled in BGI using the SOAPdenovo program (Li et al., 2010, Genome Research 20(2): 265-72). The assembled sequences were analyzed using standard bioinformatics methods for gene finding and functional prediction. GeneID (Parra et al., 2000, Genome Research 10(4): 511-515) was used for gene prediction. Blastall version 2.2.10 (Altschul et al., 1990, J. Mol. Biol. 215 (3): 403-410, National Center for Biotechnology Information (NCBI), Bethesda, MD, United States) and HMMER version 2.1.1 (National Center for Biotechnology Information (NCBI), Bethesda, MD, United States) were used to predict function based on structural homology. Beta-xylosidases were directly identified by analysis of Blast results.The Agene program (Munch and Krogh, 2006, BMC Bioinformatics 7: 263) and the SignalP program (Nielsen et al., 1997, Protein Engineering 10: 1-6) were used to identify the starting codons. The SignalP program was additionally used to predict the signal peptides. Pepstats (Rice et al., 2000, Trends Genet. 16(6): 276-277) was used to predict the isoelectric points and molecular weights of the deduced amino acid sequences. Example 3: Cloning the coding sequences of beta-xylosidase GH3 from Scytalidium thermophilum genomic DNA [000340] Based on DNA information (SEQ ID NOs: 1 and 3) obtained from genome sequencing in example 2, the oligonucleotide primers shown below were designed to amplify the beta-xylosidase genes GH3, GH3_ZY577211_92 and GH3_ZY577202_22, from the genomic DNA of Scytalidium thermophilum NN047338. The oligonucleotide primers were synthesized by Invitrogen, Beijing, China. Petition 870210014734, dated 12 / 02 / 2021, pages 120 / 154 113 / 141 oligonucleotide primer SEQID1_direct: 5'-ACACAACTGGGGATCCACCatgaccaggctgaccagcatc-3' (SEQ ID NO: 11) oligonucleotide primer SEQID1_reverse: 5'-GTCACCCTCTAGATCTcgtaccccactgccgttattg-3' (SEQ ID NO: 12) oligonucleotide primer SEQID3_direct: 5'-ACACAACTGGGGATCCACCatgaaggccctgactagaagg-3' (SEQ ID NO: 13) oligonucleotide primer SEQID3_reverse: 5'-GTCACCCTCTAGATCTtaccggacatgaacatgacagtagg-3' (SEQ ID NO: 14) [000341] Lowercase letters represent the coding regions of the genes in the forward oligonucleotide primers and the flanking region of the gene in the reverse oligonucleotide primers, while uppercase letters represent regions homologous to the pPFJO355 plasmid insertion sites (WO 2011 / 005867). [000342] For each gene, 20 picomoles of each forward and reverse primer oligonucleotide pair were used in a PCR reaction composed of 2 pL of Scytalidium thermophilum NN047338 genomic DNA, 10 pL of GC buffer [000343] 5X (Finnzymes Oy, Espoo, Finland), 1.5 pL of DMSO, 2.5 mM each of dATP, dTTP, dGTP, and dCTP, and 0.6 units of high-fidelity DNA polymerase PHUSION™ (Finnzymes Oy, Espoo, Finland) in a total volume of 50 μL. Amplifications were performed using a Peltier thermocycler (MJ Research Inc., South San Francisco, CA, United States) programmed to denature at 98°C for 1 minute; 6 cycles of denaturation at 98°C for 15 seconds, annealing at 65°C for 30 seconds, decreasing by 1°C per cycle, and stretching at 72°C for 3 minutes; 23 cycles each at 98°C for 15 seconds, 62°C for 30 seconds, and 72°C for 3 minutes; and a final extension at 72°C for 5 minutes. The heated block was then left in an immersion cycle at 4°C. [000344] PCR products were isolated by gel electrophoresis of Petition 870210014734, dated 12 / 02 / 2021, pages 121 / 154 114 / 141 agarose at 1.0% using 90 mM Tris-borate and 1 mM EDTA buffer (TBE), where a single 3 kb product band for each PCR reaction was visualized under UV light. The PCR products were then purified from a solution using an ILLUSTRA® GFX® PCR and Gel Band Purification Kit (GE Healthcare, Buckinghamshire, UK) according to the manufacturer's instructions. [000345] Plasmid pPFJO355 was digested with Bam HI and Bgl II, isolated by 1.0% agarose gel electrophoresis using TBE buffer, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification Kit, according to the manufacturer's instructions. Table 1: Plasmids Gene Plasmid DNA Map GH3_ZY577211_92 pGH3_ZY577211_92 Figure 1 GH3_ZY577202_22 pGH3_ZY577202_22 Figure 2 [000346] Each PCR product and the digested vector were ligated together using an IN-FUSION® CF Dry-down cloning kit (Clontech Laboratories, Inc., Mountain View, CA, United States), resulting in the plasmids shown in Table 1: pGH3_ZY577211_92 (Figure 1) and pGH3_ZY577202_22 (Figure 2) in which transcription of the beta-xylosidase GH3 coding sequences from Scytalidium thermophilum was in control of an alpha-amylase promoter gene from Aspergillus oryzae. In summary, 30 ng of pPFJO355, digested with BamHI and Bgl II, and 60 ng of each purified beta-xylosidase GH3 PCR product from Scytalidium thermophilum were added to reaction flasks and resuspended in a total volume of 10 μL by adding deionized water. The reactions were incubated at 37°C for 15 minutes and then at 50°C for 15 minutes. Three μL of the reactions were used to transform competent E. coli TOP10 cells (TIANGEN Biotech (Beijing) Co. Ltd., Beijing, China). The E. transformants...E. coli containing expression constructs were detected by colony PCR. Colony PCR is a method for screening. Petition 870210014734, dated 12 / 02 / 2021, pages 122 / 154 115 / 141 rapidly inserted plasmid DNA directly into E. coli colonies. Briefly, in an aliquot of PCR solution premixed in each PCR tube, including PCR buffer, MgCl2, dNTPs, and primer oligonucleotide pairs from which the PCR fragment was generated, a single colony was added by picking it out with a sterile loop and moving the loop in the reaction solution. In general, 7-10 colonies were selected. After PCR, the reactions were analyzed by electrophoresis on a 1.0% agarose gel using TBE buffer. Plasmid DNA was prepared from colonies exhibiting insertions of the expected sizes using a QIAPREP® Spin Miniprep kit (QIAGEN GmbH, Hilden, Germany). The beta-xylosidase GH3 coding sequences from Scytalidium thermophilum inserted into pGH3_ZY577211_92 and pGH3_ZY577202_22 were confirmed by DNA sequencing using a 3730XL DNA analyzer (Applied Biosystems Inc., Foster City, CA, United States). Example 4: Expression of GH3 beta-xylosidase coding sequences from Scytalidium thermophilum in Aspergillus oryzae [000347] Protoplasts of Aspergillus oryzae HowB101 (WO 95 / 035385) prepared according to the method of Christensen et al., 1988, Bio / Technology 6: 1419-1422, were transformed with 3 μg of pGH3_ZY577211_92 or pGH3_ZY577202_22. Each transformation yielded approximately 50 transformants. Eight transformants from each transformation were isolated onto individual minimal medium plates. [000348] Four transformants from each transformation were inoculated separately into 3 mL of YPM medium in a 24-well plate and incubated at 30°C with shaking at 150 rpm. After 3 days of incubation, 20 μL of supernatant from each culture were analyzed by SDS-PAGE using a NUPAGE® NOVEX® 4-12% Bis-Tris Gel with 50 mM 2-(N-morpholino)ethanesulfonic acid (MES) (Invitrogen Corporation, Carlsbad, Petition 870210014734, dated 12 / 02 / 2021, pages 123 / 154 116 / 141 (CA, United States) according to the manufacturer's instructions. The resulting gel was stained with INSTANTBLUE® (Expedeon Ltd., Babraham Cambridge, United Kingdom). SDS-PAGE profiles of the cultures showed transformants of pGH3_ZY577211_92 and pGH3_ZY577202_22 with a main protein band at 90 kDa and 95 kDa, respectively (Table 2). One transformant from each transformation was selected as expression strains and determined to be Aspergillus oryzae O5JAC and Aspergillus oryzae O5JA9, respectively. Table 2: Expression Plasmid Expression strain Recombinant protein size (KD) pGH3_ZY577211_92 O5JAC 90 pGH3_ZY577202_22 O5JA9 95 [000349] A scraping of each expression strain, Aspergillus oryzae O5JAC and Aspergillus oryzae O5JA9, was washed with 10 mL of YPM and inoculated into 2-liter flasks containing 400 mL of YPM medium. Cultures were collected on day 3 and filtered using a 0.45 μm DURAPORE® membrane (Millipore, Bedford, MA, United States). Example 5: Purification of recombinant beta-xylosidase GH3 from Scytalidium thermophilum using Aspergillus oryzae O5JAC [000350] A volume of 3200 mL of filtered Aspergillus oryzae O5JAC broth (example 4) was precipitated with ammonium sulfate (80% saturation), re-dissolved in 50 mL of 20 mM sodium acetate pH 5.0, dialyzed against the same buffer, and filtered through a 0.45 µm filter. The total volume was 80 mL. The solution was fed into a 40 mL Q SEPHAROSE® fast-flow column (GE Healthcare, Buckinghamshire, UK) equilibrated with 20 mM sodium acetate pH 5.0. Proteins were eluted with a linear gradient of 0-0.5 M NaCl. The fractions were collected, pooled, and fed into a 40 mL SP SEPHAROSE® fast-flow column (GE Healthcare, Buckinghamshire, UK) equilibrated with 20 mM sodium acetate pH 5.0. The proteins were eluted with a Petition 870210014734, dated 12 / 02 / 2021, pages 124 / 154 117 / 141 linear gradient of 0.2-0.5 M NaCl. The fractions were evaluated by SDSPAGE using a NUPAGE® NOVEX® 4-12% Bis-Tris Gel with 50 mM MES. Fractions containing a band of approximately 90 kDa were pooled and concentrated by ultrafiltration. Example 6: Cloning a GH3 xylosidase coding sequence from Penicillium oxalicum genomic DNA [000351] Based on gene information (SEQ ID NO: 5) obtained by genome sequencing in example 2, the oligonucleotide primers shown below were designed to amplify a GH3 xylosidase gene, GH3_ZY569167_685, from Penicillium oxalicum genomic DNA. Direct primer oligonucleotide: 5'-ACACAACTGGGGATCCACCatgctggccctggcatc-3' (SEQ ID NO: 15) reverse primer oligonucleotide: 5'-GTCACCCTCTAGATCTtcaaaatcctcttgtgctacctctcaagaa-3' (SEQ ID NO: 16) [000352] Lowercase letters represent the gene DNA sequence in the forward primer oligonucleotide and the gene flanking region in the reverse primer oligonucleotide, while uppercase letters represent regions homologous to the pPFJO355 plasmid insertion sites. [000353] Twenty picomoles of each of the previous oligonucleotide primers were used in a PCR reaction composed of 2 pL of Penicillium oxalicum genomic DNA, 10 pL of GC 5X buffer, 1.5 pL of DMSO, 2.5 mM each of dATP, dTTP, dGTP, and dCTP, and 0.6 units of high-fidelity DNA polymerase PHUSION™ in a total volume of 50 μL. Amplification was performed using a Peltier thermocycler programmed to denature at 98°C for 1 minute; 6 cycles of denaturation at 98°C for 15 seconds, annealing at 65°C for 30 seconds, decreasing by 1°C per cycle, and elongation at 72°C for 3 minutes; 25 cycles each at 98°C for 15 seconds, 62°C for 30 seconds, and 72°C for 3 seconds. Petition 870210014734, dated 12 / 02 / 2021, pp. 125 / 154 118 / 141 minutes; and a final extension at 72°C for 5 minutes. The heated block was then left in an immersion cycle at 4°C. [000354] The reaction products were isolated by electrophoresis on 1.0% agarose gel using TBE buffer, where a product band of approximately 3 kb was excised from the gel, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification kit according to the manufacturer's instructions. [000355] Plasmid pPFJO355 was digested with Bam HI and Bgl II, isolated by 1.0% agarose gel electrophoresis using TBE buffer, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification kit according to the manufacturer's instructions. [000356] The 3 kb PCR product and the digested vector were ligated together using an IN-FUSION® CF Dry-down PCR cloning kit resulting in pGH3_ZY569167_685 (Figure 3), where the transcription of the GH3 xylosidase coding sequence from Penicillium oxalicum was in control of an alpha-amylase promoter gene from Aspergillus oryzae. In summary, 30 ng of pPFJO355, digested with Bam HI and Bgl II, and 60 ng of the purified beta-xylosidase GH3 PCR product from purified Penicillium oxalicum were added to a reaction flask and resuspended in a total volume of 10 µL by adding deionized water. The reaction was incubated at 37°C for 15 minutes and then at 50°C for 15 minutes. Three μL of the reaction were used to transform competent E. coli TOP10 cells. An E. coli transformant containing pGH3_ZY569167_685 was detected by colony PCR as described in Example 3. Plasmid DNA was prepared using a QIAPREP® Spin Miniprep kit.The coding sequence for beta-xylosidase GH3 from Penicillium oxalicum inserted into pGH3_ZY569167_685 was confirmed by DNA sequencing using a 3730XL DNA analyzer. Example 7: Expression of the coding sequence for beta-xylosidase GH3 Petition 870210014734, dated 12 / 02 / 2021, pages 126 / 154 119 / 141 of Penicillium oxalicum in Aspergillus oryzae [000357] Protoplasts of Aspergillus oryzae HowB101 (WO 95 / 035385) prepared according to the method of Christensen et al., 1988, supra, were transformed with 3 μg of pGH3_ZY569167_685. The transformation yielded approximately 50 transformants. Four transformants were isolated on individual minimal medium plates. [000358] The four transformants were inoculated separately into 3 mL of YPM medium in a 24-well plate and incubated at 30°C with shaking at 150 rpm. After 3 days of incubation, 20 μL of supernatant from each culture were analyzed by SDS-PAGE using a NUPAGE® NOVEX® 4-12% Bis-Tris Gel with 50 mM MES. The resulting gel was stained with INSTANTBLUE®. The SDS-PAGE profiles of the cultures showed that most transformants exhibited a band of approximately 98 kDa. One transformant was selected as an expression strain and determined to be Aspergillus oryzae O4S4Q. [000359] A scraping of Aspergillus oryzae O4S4Q was washed with 10 mL of YPM medium and inoculated into five 2-liter flasks containing 400 mL of YPM medium. Cultures were collected on day 3 and filtered using a 0.45 μm DURAPORE® membrane. Example 8: Cloning the coding sequence of beta-xylosidase GH3 from Rhizomucorpusillus from genomic DNA. [000360] Based on DNA information (SEQ ID NO: 7) obtained from genome sequencing, the oligonucleotide primers shown below were designed to amplify a betaxylosidase gene GH3, GH3_ZY654890_6424, from the genomic DNA of Rhizomucor pusillus NN046782. The oligonucleotide primers were synthesized by Invitrogen, Beijing, China. Direct primer oligonucleotide: 5'-ACACAACTGGGGATCCACCatggcgtttatcaagcagagc-3' (SEQ ID NO: 17) Petition 870210014734, dated 12 / 02 / 2021, pages 127 / 154 120 / 141 reverse primer oligonucleotide: 5'-GTCACCCTCTAGATCTaccgtggaaacagcagcag-3' (SEQ ID NO: 18) [000361] Lowercase letters represent the gene coding regions in the forward primer oligonucleotide and the gene flanking region in the reverse primer oligonucleotide, while uppercase letters represent regions homologous to the pPFJO355 plasmid insertion sites. [000362] Twenty picomoles of each of the previous oligonucleotide primers were used in a PCR reaction composed of 2 pL of Rhizomucor pusillus genomic DNA, 10 μL of GC 5X buffer, 1.5 gL of DMSO, 2.5 mM each of dATP, dTTP, dGTP, and dCTP, and 0.6 units of high-fidelity DNA polymerase PHUSION™ in a total volume of 50 μL. Amplification was performed using a Peltier thermocycler programmed to denature at 98°C for 1 minute; 6 cycles of denaturation at 98°C for 30 seconds, annealing at 63°C for 30 seconds, decreasing by 1°C per cycle, and elongation at 72°C for 2.5 minutes; 24 cycles each at 94°C for 30 seconds, 58°C for 30 seconds, and 72°C for 2.5 minutes; and a final extension at 72°C for 5 minutes. The heated block was then left in an immersion cycle at 4°C. [000363] The reaction products were isolated by electrophoresis on 1.0% agarose gel using TBE buffer, where a band of the product of approximately 2.6 kb was excised from the gel, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification kit, according to the manufacturer's instructions. [000364] Plasmid pPFJO355 was digested with Bam HI and Bgl II, isolated by 1.0% agarose gel electrophoresis using TBE buffer, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification kit according to the manufacturer's instructions. [000365] An IN-FUSION® CF Dry-down cloning kit was used to clone each of the 2.6 kb PCR fragments directly into the vector. Petition 870210014734, dated 12 / 02 / 2021, pages 128 / 154 121 / 141 pPFJO355 expression, without the need for restriction digestion and ligation. [000366] The PCR product and the digested vector were ligated together using an IN-FUSION® CF Dry-down PCR cloning kit, resulting in pGH3_ZY654890_6424 (Figure 4) in which the transcription of the GH3 xylosidase coding sequence from Rhizomucor pusillus was in control of an alpha-amylase promoter gene from Aspergillus oryzae. In summary, 30 ng of pPFJO355, digested with Bam HI and Bgl II, and 60 ng of the purified beta-xylosidase GH3 PCR product gene from Rhizomucor pusillus were added to a reaction flask, and resuspended in a total volume of 10 pL by adding deionized water. The reaction was incubated at 37°C for 15 minutes and then at 50°C for 15 minutes. Three μL of the reaction were used to transform competent E. coli TOP10 cells. An E. coli transformant containing pGH3_ZY654890_6424 was detected by colony PCR as described in Example 3.Plasmid DNA was prepared using a QIAPREP® Spin Miniprep kit. The coding sequence of beta-xylosidase GH3 from Rhizomucor pusillus inserted into pGH3_ZY654890_6424 was confirmed by DNA sequencing using a 3730XL DNA analyzer. Example 9: Cloning a coding sequence of beta-xylosidase GH3 from Thermoascus aurantiacus genomic DNA [000367] Based on gene information (SEQ ID NO: 9) obtained by genome sequencing in example 2, the oligonucleotide primers shown below were designed to amplify a betaxylosidase GH3 gene, PE04100001596, from the genomic DNA of Thermoascus aurantiacus. Oligonucleotide primers were synthesized by Invitrogen, Beijing, China. Direct primer oligonucleotide: 5'-ACACAACTGGGGATCCACCatggccaccctcaagtcagttct-3' (SEQ ID NO: 19) Reverse primer oligonucleotide: Petition 870210014734, dated 12 / 02 / 2021, pages 129 / 154 122 / 141 5'-GTCACCCTCTAGATCTtcgctcactcactcactgagaagc-3' (SEQ ID NO: 20) [000368] Lowercase letters represent the gene DNA sequence in the forward primer oligonucleotide and the gene flanking region in the reverse primer oligonucleotide, while uppercase letters represent regions homologous to the pPFJO355 plasmid insertion sites. [000369] Twenty picomoles of each of the previous oligonucleotide primers were used in a PCR reaction composed of 2 pL of Thermoascus aurantiacus genomic DNA, 10 pL of GC 5X buffer, 1.5 pL of DMSO, 2.5 mM each of dATP, dTTP, dGTP, and dCTP, and 0.6 units of high-fidelity DNA polymerase PHUSION™ in a total volume of 50 μL. Amplification was performed using a Peltier thermocycler programmed to denature at 98°C for 1 minute; 8 cycles of denaturation at 98°C for 15 seconds, annealing at 65°C for 30 seconds, decreasing by 1°C per cycle, and elongation at 72°C for 3.25 minutes; 22 cycles each at 98°C for 15 seconds, 58°C for 30 seconds, and 72°C for 3.25 minutes; and a final extension at 72°C for 10 minutes. The heated block was then left in an immersion cycle at 4°C. [000370] The reaction products were isolated by electrophoresis on 1.0% agarose gel using TBE buffer where a product band of approximately 2.4 kb was excised from the gel, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification kit. [000371] Plasmid pPFJO355 was digested with Bam HI and Bgl II, isolated by 1.0% agarose gel electrophoresis using TBE buffer, and purified using an ILLUSTRA® GFX® PCR and Gel Band Purification Kit. [000372] The 2.4 kb PCR product and the digested vector were ligated together using an IN-FUSION® CF Dry-down PCR cloning kit resulting in pGH3_PE04100001596 (Figure 5), in which the transcription of the beta-xylosidase GH3 coding sequence from Thermoascus aurantiacus Petition 870210014734, dated 12 / 02 / 2021, pages 130 / 154 123 / 141 was in control of an alpha-amylase promoter gene from Aspergillus oryzae. In summary, 30 ng of pPFJO355, digested with BamHI and Bgl II, and 60 ng of the purified beta-xylosidase GH3 PCR product from Thermoascus aurantiacus were added to a reaction flask and resuspended in a total volume of 10 μL by adding deionized water. The reaction was incubated at 37°C for 15 minutes and then at 50°C for 15 minutes. Three μL of the reaction were used to transform competent E. coli TOP10 cells. An E. coli transformant containing pGH3_PE04100001596 was detected by colony PCR as described in Example 3. Plasmid DNA was prepared using a QIAPREP® Spin Miniprep kit. The coding sequence for beta-xylosidase GH3 from Thermoascus aurantiacus inserted in pGH3_PE04100001596 was confirmed by DNA sequencing using a 3730XL DNA analyzer. Example 10: Expression of the Thermoascus aurantiacus beta-xylosidase GH3 coding sequence in Aspergillus oryzae [000373] Protoplasts of Aspergillus oryzae HowB101 (WO 95 / 035385) prepared according to the method of Christensen et al., 1988, supra, were transformed with 3 μg of pGH3_PE04100001596. The transformation yielded approximately 50 transformants. Four transformants were isolated on individual minimal medium plates. [000374] The four transformants were inoculated separately into 3 mL of YPM medium in a 24-well plate and incubated at 30°C with shaking at 150 rpm. After 3 days of incubation, 20 μL of supernatant from each culture were analyzed by SDS-PAGE using a NUPAGE® NOVEX® 4-12% Bis-Tris Gel with 50 mM MES. The resulting gel was stained with INSTANTBLUE®. The SDS-PAGE profiles of the cultures showed that most transformants exhibited a band of approximately 90 kDa. One transformant was selected as an expression strain and determined to be Aspergillus oryzae O6YKQ. Petition 870210014734, dated 12 / 02 / 2021, pages 131 / 154 124 / 141 [000375] A scraping of Aspergillus oryzae O6YKQ was washed with 10 mL of YPM medium and inoculated into five 2-liter flasks containing 400 mL of YPM medium. Cultures were collected on day 3 and filtered using a 0.45 μm DURAPORE® membrane. [000376] A volume of 2,400 mL of filtered Aspergillus oryzae O6YKQ broth was precipitated with ammonium sulfate (80% saturation), redissolved in 50 mL of 20 mM Tris-HCl pH 6.5, dialyzed against the same buffer, and filtered through a 0.45 μm filter. The total volume was 75 mL. The solution was applied to a 40 mL Q SEPHAROSE® fast-flow column equilibrated in 20 mM Tris-HCl pH 6.5. The fractions eluted with 0.08–0.1 M NaCl were collected and further purified on a 40 mL Q SEPHAROSE® fast-flow column with a linear NaCl gradient (0.03–0.11 M). The fractions were evaluated by SDS-PAGE using a NUPAGE® NOVEX® 4-12% Bis-Tris Gel with 50 mM MES. Fractions containing a band of approximately 84 kDa were pooled. Subsequently, the pooled solution was concentrated by ultrafiltration. Example 11: Characterization of genomic DNAs encoding GH3 betaxylosidases [000377] The genomic DNA sequence and the deduced amino acid sequence of a beta-xylosidase GH3 coding sequence from Scytalidium thermophilum are shown in SEQ ID NO: 1 (D822K1) and SEQ ID NO: 2 (P244Y5), respectively. The coding sequence is 2,402 bp long including the stop codon, which is interrupted by a 68 bp intron (nucleotides 192 to 259). The predicted encoded protein has 777 amino acids. Using the SignalP program (Nielsen et al., 1997, Protein Engineering 10: 1-6), a 19-residue signal peptide was predicted. The predicted mature protein contains 758 amino acids with a predicted molecular mass of 83.06 kDa and a predicted isoelectric point of 6.15. [000378] A global pairwise comparative alignment of sequences Petition 870210014734, dated 12 / 02 / 2021, pages 132 / 154 The amino acid sequence 125 / 141 was determined using the Needleman and Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) with a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 matrix. Alignment showed that the deduced amino acid sequence from the genomic DNA of Scytalidium thermophilum encoding a beta-xylosidase GH3 shares 62.96% sequence identity (excluding gaps) with the deduced amino acid sequence of a beta-xylosidase GH3 from Pyrenophora tritici-repentis (UNIPROT B2W9Y0). [000379] The genomic DNA sequence and the deduced amino acid sequence of a beta-xylosidase GH3 coding sequence from Scytalidium thermophilum are shown in SEQ ID NO: 3 (D822JZ) and SEQ ID NO: 4 (P244Y4), respectively. The coding sequence is 2671 bp long including the stop codon, which is interrupted by three introns of 68 bp (nucleotides 192 to 259), 62 bp (nucleotides 564 to 625), and 63 bp (nucleotides 1001 to 1063). The predicted encoded protein is 825 amino acids long. Using the SignalP program (Nielsen et al., 1997, supra), a 19-residue signal peptide was predicted. The predicted mature protein contains 806 amino acids with a predicted molecular mass of 86.94 kDa and a predicted isoelectric point of 5.35. [000380] A comparative global pairwise alignment of amino acid sequences was determined using the Needleman and Wunsch algorithm (Needleman and Wunsch, 1970, supra) with a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 matrix. The alignment showed that the deduced amino acid sequence from the genomic DNA of Scytalidium thermophilum encoding a beta-xylosidase GH3 shares 70.39% identity (excluding gaps) with the deduced amino acid sequence of a beta-xylosidase GH3 from Chaetomium globosum (UNIPROT Q2HEP1). Petition 870210014734, dated 12 / 02 / 2021, pages 133 / 154 126 / 141 [000381] The genomic DNA sequence and the deduced amino acid sequence of a coding sequence of beta-xylosidase GH3 from Penicillium oxalicum are shown in SEQ ID NO: 5 (D72UE7) and SEQ ID NO: 6 (P241KM), respectively. The coding sequence is 2832 bp long including the stop codon, which is interrupted by two introns of 82 bp (nucleotides 222 to 303) and 194 bp (nucleotides 418 to 611). The predicted encoded protein has 851 amino acids. Using the SignalP program (Nielsen et al., 1997, supra), a 19-residue signal peptide was predicted. The predicted mature protein contains 832 amino acids with a predicted molecular mass of 90.45 kDa and a predicted isoelectric point of 4.83. [000382] A global pairwise alignment of amino acid sequences was determined using the Needleman and Wunsch algorithm (Needleman and Wunsch, 1970, supra) with a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 matrix. The alignment showed that the deduced amino acid sequence from the Penicillium oxalicum genomic DNA encoding a beta-xylosidase GH3 shares 47.51% identity (excluding gaps) with the deduced amino acid sequence of a GH3 enzyme from Fusarium verticillioides (GENESEQP AZG45438). [000383] The genomic DNA sequence and the deduced amino acid sequence of a beta-xylosidase GH3 coding sequence from Rhizomucor pusillus are shown in SEQ ID NO: 7 (D13874) and SEQ ID NO: 8 (P24QRU), respectively. The coding sequence is 2637 bp long including the stop codon, which is interrupted by five introns of 51 bp (nucleotides 288 to 338), 58 bp (nucleotides 444 to 501), 58 bp (nucleotides 540 to 597), 59 bp (nucleotides 707 to 765), and 107 bp (nucleotides 1618 to 1724). The predicted encoded protein is 767 amino acids long. Using the SignalP program (Nielsen et al., 1997, supra), a 21-residue signal peptide was predicted. The predicted mature protein contains Petition 870210014734, dated 12 / 02 / 2021, pages 134 / 154 127 / 141 746 amino acids with a predicted molecular mass of 82.03 kDa and a predicted isoelectric point of 5.02. [000384] A global pairwise alignment of amino acid sequences was determined using the Needleman and Wunsch algorithm (Needleman and Wunsch, 1970, supra) with a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 matrix. The alignment showed that the deduced amino acid sequence from the Rhizomucor pusillus genomic DNA encoding a beta-xylosidase GH3 shares 43.44% identity (excluding gaps) with the deduced amino acid sequence of a beta-glucosidase from Dictyostelium discoideum (GENESEQP AYM76588). [000385] The genomic DNA sequence and the deduced amino acid sequence of a beta-xylosidase GH3 coding sequence from Thermoascus aurantiacus are shown in SEQ ID NO: 9 (D82RN1) and SEQ ID NO: 10 (P24GP2), respectively. The coding sequence is 2403 bp long including the stop codon, with no introns. The predicted encoded protein has 800 amino acids. Using the SignalP program (Nielsen et al., 1997, supra), a 20-residue signal peptide was predicted. The predicted mature protein contains 780 amino acids with a predicted molecular mass of 84.58 kDa and a predicted isoelectric point of 5.03. [000386] A global pairwise comparative alignment of amino acid sequences was determined using the Needleman and Wunsch algorithm (Needleman and Wunsch, 1970, supra) with a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 matrix. The alignment showed that the deduced amino acid sequence from the Thermoascus aurantiacus genomic DNA encoding a beta-xylosidase GH3 shares 70.5% identity (excluding gaps) with the deduced amino acid sequence of a beta-xylosidase from Trichoderma reesei (GENESEQP ARZ21779). Petition 870210014734, dated 12 / 02 / 2021, pp. 135 / 154 128 / 141 Example 12: Hydrolysis test of pre-treated corn cobs [000387] Corn cobs were pretreated with NaOH (0.08 g / g dry weight of cobs) at 120°C for 60 minutes, at 15% total dry weight solids (TS). The resulting material was washed with water until pH 8.2 was achieved, resulting in alkaline washed pretreated corn cobs (APCC). Ground and sieved alkaline pretreated corn cobs (GS-APCC) were prepared by adjusting the pH of APCC to 5.0 by adding 6 M HCl and water with thorough mixing, grinding APCC in a Cosmos ICMG 40 wet multipurpose grinder (EssEmm Corporation, Tamil Nadu, India), and autoclaving for 45 minutes at 121°C, with a final TS of 3.33%. The hydrolysis of GSAPCC was conducted using 2.2 mL of deep well plates (Axygen, Union City, CA, United States), with a final reaction volume of 1.0 mL. [000388] Hydrolysis was performed with 10 mg of total GSAPCC solids per mL of 50 mM sodium acetate buffer pH 5.0 containing 1 mM manganese sulfate, and various protein loadings of various enzymatic compositions (expressed as mg of protein per gram of cellulose). The enzymatic compositions were then prepared and added simultaneously to all wells, in volumes ranging from 50 pL to 200 pL, for a total volume of 1 mL in each reaction. The plate was then sealed using an ALPS-300™ plate heat sealer (Abgene, UK), thoroughly mixed, and incubated at a specific temperature for 72 hours. All reported experiments were performed in triplicate. [000389] After hydrolysis, the samples were filtered using a 96-well plate with a 0.45 µm MULTISCREEN® filter (Millipore, Bedford, MA, USA) and the filtrates were analyzed for sugar content as described below. When not used immediately, the filtered aliquots were frozen at -20°C. The sugar concentrations of the samples diluted in 0.005 M H2SO4 were measured using a 4.6 x 250 mm AMINEX® HPX-87H column (Bio-Rad Laboratories, Inc., Hercules, Petition 870210014734, dated 12 / 02 / 2021, pages 136 / 154 129 / 141 (CA, United States) by elution with 0.05% w / w benzoic acid-H2SO4 0.005 M at 65°C at a flow rate of 0.6 mL per minute, and quantification by integration of glucose, cellobiose, and xylose signals from refractive index detection (CHEMSTATION®, AGILENT® 1100 HPLC, Agilent Technologies, Santa Clara, CA, United States) was calibrated using pure sugar samples. The resulting glucose equivalents were used to calculate the percentage conversion of cellulose for each reaction. The resulting xylose equivalents were used to calculate the percentage conversion of xylo-oligosaccharide for each reaction. [000390] Glucose, cellobiose, and xylose were evaluated individually. Measured sugar concentrations were adjusted for the appropriate dilution factor. All HPLC data processing was performed using MICROSOFT EXCEL™ software (Microsoft, Richland, WA, United States). [000391] The degree of conversion of xylo-oligosaccharide to xylose was calculated using the following equation: % xylose conversion = xylose concentration / xylose concentration at a limit digestion. In order to calculate the % conversion, a conversion point of 100% was set based on a control of cellulase (100 mg of Trichoderma reesei cellulase supplemented with P. emersonii polypeptide GH61A (WO 2011 / 041397)), A. fumigatus xylanase GH10 (xyn3) (WO 2006 / 078256), and T. emersonii beta-xylosidase GH3 (WO 2003 / 070956) per gram of cellulose), and all values ​​were divided by this number and then multiplied by 100. The data points in triplicate had their mean calculated and the standard deviation was calculated. Example 13: Preparation of GH10 xylanase from Penicillium sp. strain NN51602 [000392] Penicillium sp. strain NN51602 GH10 xylanase (SEQ ID NO: 21 [DNA sequence] and SEQ ID NO: 22 [derived amino acid sequence]) was recombinantly prepared according to WO Petition 870210014734, dated 12 / 02 / 2021, pp. 137 / 154 130 / 141 2010 / 126772. The filtered broth was concentrated and the buffer was replaced with 20 mM Tris pH 8.0 using a tangential flow concentrator (Pall Filtron, Northborough, MA, USA) equipped with a 10 kDa polyethersulfone membrane (Pall Filtron, Northborough, MA, USA). The desalinated filtrate was placed on a Q SEPHAROSE® High Performance column (GE Healthcare, Piscataway, NJ, USA) equilibrated in 20 mM Tris pH 8.0, and bound proteins were eluted with a linear gradient of 0-1000 mM sodium chloride. The fractions were analyzed by SDS-PAGE using an 8-16% Tris HCl CRITERION STAIN FREE™ gel and a CRITERION STAIN FREE™ Imaging System SDS-PAGE (Bio-Rad Laboratories, Inc., Hercules, CA, United States). Fractions containing a band of approximately 50 kDa were pooled.Protein concentration was determined using a Microplate BCA™ protein assay kit (Thermo Fisher Scientific, Waltham, MA, United States), in which bovine serum albumin was used as a protein standard. Example 14: Preparation of beta-xylosidase GH3 from Talaromyces emersonii CBS 393.64 (P4UE) [000393] A beta-xylosidase from Talaromyces emersonii CBS 393.64 (SEQ ID NO: 23 [DNA sequence] and SEQ ID NO: 24 [derived amino acid sequence]) was recombinantly prepared according to Rasmussen et al., 2006, Biotechnology and Bioengineering 94: 869-876, using Aspergillus oryzae JaL355 as a host (WO 2003 / 070956). The filtered broth was concentrated and desalted with 50 mM sodium acetate pH 5.0, using a tangential flow concentrator equipped with a 10 kDa polyethersulfone membrane. Protein concentration was determined using a Microplate BCA™ protein assay kit, in which bovine serum albumin was used as a protein standard. Example 15: Gel quantification of beta-xylosidase GH3 Petition 870210014734, dated 12 / 02 / 2021, pages 138 / 154 131 / 141 Thermoascus aurantiacus (P24GP2) [000394] The total protein content of beta-xylosidase GH3 of Thermoascus aurantiacus was determined by gel quantification. Protein concentration was determined by SDS-PAGE using an 8-16% Tris HCl CRITERION STAIN FREE™ gel and a CRITERION STAIN FREE™ Imaging System SDS-PAGE (Bio-Rad Laboratories, Inc., Hercules, CA, United States), in which Talaromyces emersonii beta-xylosidase GH3 was used as a protein standard. Example 16: Effect of beta-xylosidase GH3 from Thermoascus aurantiacus (P24GP2) when supplemented with xylanase GH10 from Penicillium sp. using APCC at pH 4.0 to 7.0 [000395] Beta-xylosidase GH3 from Thermoascus aurantiacus (P24GP2) supplemented with xylanase GH10 from Penicillium sp. (Example 13) was evaluated at 50 °C and 60 °C at pH 4.0 to 7.0 using pretreated washed and alkaline corn cobs (APCC) as a substrate. As a comparison, beta-xylosidase GH3 from Talaromyces emersonii (P4UE) supplemented with xylanase GH10 from Penicillium sp. was added to APCC. Beta-xylosidases were added to the hydrolysis of APCC at 0.025 mg of total protein per g of cellulose supplemented with xylanase at 4.0 mg of total protein per g of cellulose, and the hydrolysis results were compared with the results containing only xylanase at 4.0 mg of total protein per g of cellulose. [000396] The assay was performed as described in Example 12. Reactions of 1 mL with APCC (1% total solids) were conducted for 72 hours in 50 mM sodium acetate buffer (pH 4.0 to 5.5) or 50 mM Tris buffer (pH 6.0 to 7.0) containing 1 mM manganese sulfate. All reactions were performed in triplicate and involved simple mixing at the beginning of hydrolysis. [000397] The results at 50°C are shown in Figure 6, and the results at 60°C are shown in Figure 7. As shown in Figure Petition 870210014734, dated 12 / 02 / 2021, pages 139 / 154 132 / 141 1. Beta-xylosidase GH3 from T. aurantiacus significantly increased the hydrolysis of xylan to xylose compared to xylanase GH10 from Penicillium sp. alone at 50°C and pH 4.0 to 7.0. At 50°C, beta-xylosidase GH3 from T. aurantiacus showed optimal activity at pH 4.0 to 5.5. Furthermore, beta-xylosidase GH3 from T. aurantiacus increased hydrolysis compared to beta-xylosidase GH3 from T. emersonii at pH 5.0 to 7.0 and 50°C. Beta-xylosidase GH3 from T. aurantiacus supplemented with xylanase increased the hydrolysis of xylan to xylose 3.19 times more than beta-xylosidase GH3 from T. emersonii supplemented with xylanase at pH 7.0 and 50°C. [000398] As shown in Figure 7, the beta-xylosidase GH3 from T. aurantiacus significantly increased the hydrolysis of xylan to xylose compared to the xylanase GH10 from Penicillium sp. alone at 60°C and pH 4.0 to 6.0. At 60°C, the beta-xylosidase GH3 from T. aurantiacus showed optimal activity at pH 4.0 to 5.0. Furthermore, the beta-xylosidase GH3 from T. aurantiacus increased hydrolysis compared to the beta-xylosidase GH3 from T. emersonii at pH 5.5 to 6.0 and 60°C. Beta-xylosidase GH3 from T. aurantiacus supplemented with xylanase increased the hydrolysis of xylan to xylose 1.95 times more than beta-xylosidase GH3 from T. emersonii supplemented with xylanase at pH 6.0 and 60°C. [000399] The present invention is further described by the following numbered paragraphs: [1] A polypeptide isolate with beta-xylosidase activity, selected from the group consisting of: (a) a polypeptide exhibiting at least 60% sequence identity with the mature polypeptide of SEQ ID NO: 6 or SEQ ID NO: 8; at least 65% sequence identity with the mature polypeptide of SEQ ID NO: 2; or at least 75% sequence identity with the mature polypeptide of SEQ ID NO: 4 or SEQ ID NO: 10; (b) a polypeptide encoded by a polynucleotide that hybridizes under at least medium-high severity conditions to (i) the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID Petition 870210014734, dated 12 / 02 / 2021, pages 140 / 154 133 / 141 NO: 5, SEQ ID NO: 7, or SEQ ID NO: 9, (ii) the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 7, or (iii) the full-size complement of (i) or (ii); (c) a polypeptide encoded by a polynucleotide that has at least 60% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 5 or SEQ ID NO: 7, or the cDNA sequences thereof; at least 65% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 1 or the cDNA sequence thereof; or at least 75% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 3 or the cDNA sequence thereof or SEQ ID NO: 9; (d) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10 comprising a substitution, deletion, and / or insertion at one or more (e.g., multiple) positions;and (e) a fragment of the polypeptide from (a), (b), (c), or (d) that exhibits beta-xylosidase activity.; [2] The polypeptide according to claim 1, which has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the mature polypeptide of SEQ ID NO: 6 or SEQ ID NO: 8; at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the Petition 870210014734, dated 12 / 02 / 2021, pages 141 / 154 134 / 141 mature polypeptide of SEQ ID NO: 2; or at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the mature polypeptide of SEQ ID NO: 4 or SEQ ID NO: 10. [3] The polypeptide according to claim 1, which is encoded by a polynucleotide that hybridizes under medium-high, high or very high severity conditions to (i) the sequence encoding the mature polypeptide of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, or SEQ ID NO: 9, (ii) the cDNA sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 7, or (iii) the full-size complement of (i) or (ii).[4] The polypeptide according to claim 1, which is encoded by a polynucleotide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 5 or SEQ ID NO: 7 or the cDNA sequences thereof;at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity; Petition 870210014734, dated 12 / 02 / 2021, pages 142 / 154 135 / 141 sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 1 or its cDNA sequence; or at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the sequence encoding the mature polypeptide of SEQ ID NO: 3 or its cDNA sequence or SEQ ID NO: 9. [5] The polypeptide of paragraph 1, comprising or consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10 or the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10. [6] The polypeptide of paragraph 5, wherein the mature polypeptide has amino acids 20 to 777 of SEQ ID NO: 2, amino acids 20 to 825 of SEQ ID NO: 4, amino acids 20 to 851 of SEQ ID NO: 6, amino acids 22 to 767 of SEQ ID NO: 8, or amino acids 21 to 800 of SEQ ID NO: 10. [7] The polypeptide of paragraph 1, which is a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10 comprising a substitution, deletion, and / or insertion at one or more (e.g., multiple) positions. [8] The polypeptide of any of paragraphs 1-7, which is a fragment of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, or SEQ ID NO: 10, in which the fragment exhibits betaxylosidase activity. [9] A composition comprising the polypeptide of any of paragraphs 1-8.

[10] An isolated polynucleotide that codes for the polypeptide Petition 870210014734, dated 12 / 02 / 2021, pages 143 / 154 136 / 141 of any of paragraphs 1-8.

[11] A nucleic acid construct or expression vector comprising the paragraph 10 polynucleotide operably linked to one or more control sequences that direct the production of the polypeptide in an expression host.

[12] A recombinant host cell comprising the paragraph 10 polynucleotide operably linked to one or more control sequences directing the production of the polypeptide.

[13] A method of producing the polypeptide of any of paragraphs 1-8, comprising: cultivating a cell, which in its wild-type form produces the polypeptide, under conditions that lead to the production of the polypeptide.

[14] The method in paragraph 13, additionally comprising recovering the polypeptide.

[15] A method of producing a polypeptide with xylanase activity, comprising: cultivating the host cell of paragraph 12 under conditions leading to the production of the polypeptide.

[16] The method in paragraph 15, additionally comprising recovering the polypeptide.

[17] A transgenic plant, part of a plant or plant cell transformed with a polynucleotide encoding the polypeptide from any of paragraphs 1-8.

[18] A method of producing a polypeptide with xylanase activity, comprising: cultivating the transgenic plant or plant cell of paragraph 17 under conditions leading to the production of the polypeptide.

[19] The method in paragraph 18, additionally comprising recovering the polypeptide.

[20] A method of producing a mutant from a cell Petition 870210014734, dated 12 / 02 / 2021, pages 144 / 154 137 / 141 precursor, comprising inactivating a polynucleotide encoding the polypeptide from any of paragraphs 1-8, resulting in the mutant producing less of the polypeptide than the precursor cell.

[21] A mutant cell produced by the method of paragraph 20.

[22] The mutant cell of paragraph 21, additionally comprising a gene encoding a natural or heterologous protein.

[23] A method of producing a protein, comprising: growing the mutant cell of paragraph 21 or 22 under conditions that lead to the production of the protein.

[24] The method in paragraph 23, additionally comprising recovering the protein.

[25] An inhibitory double-stranded RNA (dsRNA) molecule comprising a polynucleotide subsequence of paragraph 10, wherein optionally the dsRNA is an siRNA or miRNA molecule.

[26] The inhibitory double-stranded RNA (dsRNA) molecule of paragraph 25, which has approximately 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more duplex nucleotides in size.

[27] A method of inhibiting the expression of a polypeptide with xylanase activity in a cell, comprising administering to the cell or expressing in the cell the inhibitory double-stranded RNA (dsRNA) molecule of paragraph 25 or 26.

[28] A cell produced by the method of paragraph 27.

[29] The cell in paragraph 28, additionally comprising a gene encoding a natural or heterologous protein.

[30] A method of producing a protein, comprising: cultivating the cell of paragraph 28 or 29 under conditions that lead to the production of the protein.

[31] The method in paragraph 30, additionally comprising recovering the polypeptide. Petition 870210014734, dated 12 / 02 / 2021, pages 145 / 154 138 / 141

[32] An isolated polynucleotide encoding a signal peptide comprising or consisting of amino acids 1 to 19 of SEQ ID NO: 2, amino acids 1 to 19 of SEQ ID NO: 4, amino acids 1 to 19 of SEQ ID NO: 6, amino acids 1 to 21 of SEQ ID NO: 8, or amino acids 1 to 20 of SEQ ID NO: 10.

[33] A nucleic acid construct or expression vector comprising a gene encoding a protein operably linked to the polynucleotide of paragraph 32, wherein the gene is foreign to the polynucleotide encoding the signal peptide.

[34] A recombinant host cell comprising a gene encoding a protein operably linked to the polynucleotide of paragraph 32, wherein the gene is foreign to the polynucleotide encoding the signal peptide.

[35] A method of producing a protein, comprising: cultivating a recombinant host cell comprising a gene encoding a protein operably linked to the polynucleotide of paragraph 32, wherein the gene is foreign to the polynucleotide encoding the signal peptide, under conditions leading to the production of the protein.

[36] The method in paragraph 35, additionally comprising recovering the protein.

[37] A process for degrading a cellulosic or xylan-containing material, comprising: treating the cellulosic or xylan-containing material with an enzymatic composition in the presence of the polypeptide with xylanase activity from any of paragraphs 1-8.

[38] The process in paragraph 37, in which cellulosic or xylan-containing material is pre-treated.

[39] The process in paragraph 37 or 38, wherein the enzymatic composition comprises one or more (e.g., several) enzymes selected from the group consisting of a cellulase, a polypeptide with Petition 870210014734, dated 12 / 02 / 2021, pages 146 / 154 139 / 141 best cellulolytic activity, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swollenin.

[40] The process of paragraph 39, in which cellulase is one or more enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase, and a beta-glucosidase.

[41] The process of paragraph 39, wherein hemicellulase is one or more enzymes selected from the group consisting of a xylanase, an acetylxylan esterase, a feruloyl esterase, an arabinofuranosidase, a xylosidase, and a glucuronidase.

[42] The process of any of paragraphs 37-41, additionally comprising recovering degraded cellulosic or xylan-containing material.

[43] The process in paragraph 42, in which the degraded cellulosic or xylan-containing material is a sugar.

[44] The process in paragraph 43, in which sugar is selected from the group consisting of glucose, xylose, mannose, galactose, and arabinose.

[45] A process for synthesizing a fermentation product, comprising: (a) saccharifying a cellulosic or xylan-containing material with an enzymatic composition in the presence of the xylanase-active polypeptide of any of paragraphs 1-8; (b) fermenting the saccharified or xylan-containing cellulosic material with one or more fermenting microorganisms to synthesize the fermentation product; and (c) recovering the fermentation product from the fermentation.

[46] The process in paragraph 45, in which cellulosic or xylan-containing material is pre-treated.

[47] The process in paragraph 45 or 46, where the enzymatic composition comprises one or more (e.g., several) enzymes Petition 870210014734, dated 12 / 02 / 2021, pages 147 / 154 140 / 141 selected from the group consisting of a cellulase, a polypeptide with improved cellulolytic activity, a hemicellulase, an esterase, an expansin, a laccase, a lignolytic enzyme, a pectinase, a peroxidase, a protease, and a swollenin.

[48] ​​The process of paragraph 47, in which cellulase is one or more enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase, and a beta-glucosidase.

[49] The process of paragraph 47, wherein hemicellulase is one or more enzymes selected from the group consisting of a xylanase, an acetylxylan esterase, a feruloyl esterase, an arabinofuranosidase, a xylosidase, and a glucuronidase.

[50] The process of any of paragraphs 45-49, in which steps (a) and (b) are carried out simultaneously in a simultaneous saccharification and fermentation.

[51] The process in any of paragraphs 45-50, wherein the fermentation product is an alcohol, an alkane, a cycloalkane, an alkene, an amino acid, a gas, isoprene, a ketone, an organic acid, or a polyketide.

[52] A process for fermenting a cellulosic or xylan-containing material, comprising: fermenting the cellulosic or xylan-containing material with one or more (e.g., several) fermenting microorganisms, wherein the cellulosic or xylan-containing material is saccharified with an enzymatic composition in the presence of the polypeptide with xylanase activity of any of paragraphs 1-8.

[53] The process in paragraph 52, in which fermentation of cellulosic or xylan-containing material synthesizes a fermentation product.

[54] The process in paragraph 53, additionally comprising recovering the fermentation product from fermentation.

[55] The process of paragraph 53 or 54, in which the product of Petition 870210014734, dated 12 / 02 / 2021, pages 148 / 154 141 / 141 fermentation is an alcohol, an alkane, a cycloalkane, an alkene, an amino acid, a gas, isoprene, a ketone, an organic acid, or a polyketide.

[56] The process in any of paragraphs 52-55, in which cellulosic or xylan-containing material is pre-treated before saccharification.

[57] The process of any of paragraphs 52-56, wherein the enzymatic composition comprises one or more (e.g., several) enzymes selected from the group consisting of a cellulase, a polypeptide with improved cellulolytic activity, a hemicellulase, an esterase, an expansin, a laccase, a ligninolytic enzyme, a pectinase, a peroxidase, a protease, and a swolenin.

[58] The process of paragraph 57, in which cellulase is one or more enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase, and a beta-glucosidase.

[59] The process of paragraph 57, wherein hemicellulase is one or more enzymes selected from the group consisting of a xylanase, an acetylxylan esterase, a feruloyl esterase, an arabinofuranosidase, a xylosidase, and a glucuronidase.

[60] A whole broth formulation or cell culture composition comprising the polypeptide of any of paragraphs 1-8. [000400] The invention described and claimed herein shall not be limited in scope by the specific aspects disclosed herein, as these aspects are intended as illustrations of various aspects of the invention. Any equivalent aspects are intended to be within the scope of this invention. In fact, various modifications of the invention, in addition to those shown and described herein, will become apparent to those skilled in the art from the preceding description. Such modifications are also intended to be within the scope of the appended claims. In case of conflict, the present disclosure, including the definitions, shall prevail. Petition 870210014734, dated 12 / 02 / 2021, pp. 149 / 154

Claims

1 / 2 CLAIMS 1. Method for producing a polypeptide with beta-xylosidase activity, characterized in that it comprises: (a) culturing a host cell comprising the polynucleotide having the sequence encoding the mature polypeptide of SEQ ID NO: 9 or the cDNA sequence thereof; under conditions leading to the production of an isolated polypeptide; and optionally (b) recovering the polypeptide.

2. Method according to claim 1, characterized in that said polypeptide comprises or consists of SEQ ID NO: 10 or the mature polypeptide of SEQ ID NO:

10.

3. Process for degrading or converting a cellulosic or xylan-containing material, characterized in that it comprises: treating the cellulosic or xylan-containing material with an enzymatic composition in the presence of the polypeptide comprising or consisting of SEQ ID NO: 10 or the mature polypeptide of SEQ ID NO:

10.

4. Process for synthesizing a fermentation product, characterized in that it comprises: (a) saccharifying a cellulosic or xylan-containing material with the polypeptide comprising or consisting of SEQ ID NO: 10 or the mature polypeptide of SEQ ID NO: 10; (b) fermenting the saccharified or xylan-containing cellulosic material with one or more fermenting microorganisms to synthesize the fermentation product; and (c) recovering the fermentation product from the fermentation.

5. Process for fermenting a cellulosic or xylan-containing material, characterized in that it comprises: fermenting the cellulosic or xylan-containing material with one or more fermenting microorganisms, wherein the cellulosic or xylan-containing material is saccharified with the polypeptide comprising or consisting of SEQ ID NO: 10 or the mature polypeptide of SEQ ID NO: 10.

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