Title - METHODS TO INCREASE THE STARCH AND / OR GLUTEN YIELD OF CORN GRAINS IN A WET MILLING PROCESS

Abstract

The present application provides a method for increasing the starch and / or gluten yield of corn kernels in a wet milling process, comprising contacting a fiber-rich fraction of milled kernels with an effective amount of SO2 and an effective amount of one or more hydrolytic enzymes, wherein at least one of said hydrolytic enzymes is selected from xylanase and / or cellulase enzymes, during a fiber washing step.

Description

IMPROVED FIBER WASHING IN WET MILLING OF CORN FIELD OF INVENTION. The present invention relates to a method for improving or increasing the yield of starch and / or gluten from corn kernels in a wet milling process, by contacting said corn kernels with an enzymatic composition comprising xylanases and / or cellulases, preferably during fiber washing. BACKGROUND OF THE INVENTION. Conventional wet milling of corn is a process designed for the recovery and purification of starch and various byproducts, including germ, gluten (protein), and fiber. Fiber is the least valuable byproduct, so the industry has made a substantial effort to increase the yield of the more valuable products, such as starch and gluten, while simultaneously decreasing the fiber fraction. High-quality starch is valuable because it can be used for a variety of commercial purposes after further processing to yield products such as dry starch, modified starch, dextrins, sweeteners, and alcohol. Gluten is generally used for animal feed, as corn gluten meal (approximately 60% protein) or corn gluten feed (approximately 20% protein). The wet milling process can vary significantly depending on the specific milling equipment used, but it generally includes: grain cleaning, soaking, milling, germ separation, a second milling, fiber separation, gluten separation, and starch separation. After cleaning the corn kernels, they are typically softened by soaking them in water or a dilute SO2 solution under controlled time and temperature conditions. The kernels are then milled to break the pericarp, and the germ is separated from the rest of the grain. The remaining slurry, consisting mainly of fiber, starch, and gluten, is finely milled and sieved in a fiber washing process to separate the fiber from the starch and gluten. The gluten and starch are then separated, and the starch is purified in a washing / filtration process. The use of enzymes has been suggested in several steps of the wet milling process, such as the use of enzymes for the soaking step of milling processes in 237873 1433329 of 42 wet. The commercial enzyme product Steepzyme® (available from Novozymes A / S) has been shown to be suitable for the first step in wet milling processes, i.e., the soaking step in which the corn kernels are soaked in water. More recently, “enzymatic milling” has been developed, a modified wet milling process that uses proteases to significantly reduce the total processing time during wet milling of corn and eliminates the need for sulfur dioxide as a processing agent. Johnston et al., Cereal Chem, 81, pp. 626-632 (2004). US patent 6,566,125 describes a method for obtaining corn starch, which involves soaking corn kernels in water to produce soaked corn kernels, grinding the soaked corn kernels to produce a ground corn suspension, and incubating the ground corn suspension with enzyme (e.g., protease). US patent 5,066,218 describes a method for grinding grain, especially corn, comprising cleaning the grain, soaking it in water to soften it, and then grinding the grain with a cellulase enzyme. Document WO 2002 / 000731 describes a process for treating crop grains, comprising soaking the grains in water for 1-12 hours, wet grinding the soaked grains, and treating the grains with one or more enzymes, including an acid protease. Document WO 2002 / 000911 describes a process for separating starch and gluten, which comprises subjecting milled starch to an acid protease. WO 2002 / 002644 describes a washing process for a starch suspension obtained from the starch and gluten separation step of a milling process, comprising washing the starch suspension with an aqueous solution comprising an effective amount of acid protease. Documents WO 2014 / 082566 and WO 2014 / 082564 describe cellulolytic compositions for use in wet milling. Document WO2016 / 095856 describes compositions comprising xylanases and arabinofuranosidases and the use of these compositions in fiber washing in a wet milling process of corn. 237873 1433329 of 42 Document WO2019 / 023222 describes a wet milling process that applies GH5 xylanases and GH30 xylanases in combination with cellulases in the fiber washing step. WO2017 / 088820 describes a process for improving starch release in wet milling of corn from fiber, by adding an alpha-L-arabinofuranosidase (GH62) alone or in combination with a xylanase (GH10) in a fiber washing step. Document WO2018 / 053220 describes a fiber washing system as part of a wet milling process optimized to apply enzymes in the fiber washing step by using a dedicated space / tank for enzyme incubation. While the technique has investigated the effect of using enzymes in wet milling of corn, during soaking / soaking of corn kernels, during milling of corn kernels, and in the separation of starch and gluten, there is still a need for improved technology that can reduce energy expenditure and costs associated with wet milling of corn, and provide a higher yield of starch and gluten. SUMMARY OF THE INVENTION. In a first aspect, the present invention relates to a method for increasing the starch yield and / or gluten yield of corn kernels in a wet milling process, comprising contacting a fiber-rich fraction of milled kernels with an effective amount of SO2 and an effective amount of one or more hydrolytic enzymes, wherein at least one of said hydrolytic enzymes is selected from xylanase and / or cellulase enzymes, during a fiber washing step. DEFINITIONS. Definition of enzymes: Arabinofuranosidases / Arabinofuranosidase-containing polypeptide: The term arabinofuranosidase means an alpha-L-arabinofuranoside arabinofuranohydrolase (EC 3.2.1.55) that catalyzes the hydrolysis of terminal residues of non-reducing alpha-L-arabinofuranosides to alpha-L-arabinosides. The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3) and / or (1,2) and / or (1,5) linkages, arabinoxylans, and 237873 1433329 of 42 arabinogalactans. Alpha-L arabinofuranosidase is also known as arabinosidase, alpha-arabinosidase, alpha-L-arabinosidase, alpha-arabinofuranosidase, polysaccharide alpha-Larabinofuranosidase, alpha-L-arabinofuranoside hydrolase, L-arabinosidase, or alpha-Larabinanase. Arabinofuranosidase activity can be 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 μL for 30 minutes at 40°C, followed by arabinose analysis by AMINEX® HPX-87H column chromatography (Bio-Rad Laboratories, Inc., Hercules, CA, USA). Arabinofuranosidases can be found, for example, in the GH43, GH62, and GH51 families according to Henrissat, 1991, A classification of glycosyl hydrolases on the basis of amino acid sequence similarities, Biochem. J., 280: 309-316, and Henrissat and Bairoch, 1996, Update of the classification based on glycosyl hydrolase sequences, Biochem. J. 316: 695-696. Beta-glucosidase / polypeptide with beta-glucosidase activity: The term beta-glucosidase means a beta-D-glucoside glucohydrolase (EC 3.2.1.21) that catalyzes the hydrolysis of non-reducing terminal beta-D-glucose residues with the release of beta-D-glucose. Beta-glucosidase activity can be determined using p-nitrophenyl-beta-D-glucopyranoside as a substrate according to the procedure of Venturi et al., 2002, J. Basic Microbiol. 42: 55-66. One unit of beta-glucosidase is defined as 1.0 μmol of p-nitrophenolate anion produced per minute at 25°C, pH 4.8, from p-nitrophenyl-beta-D-glucopyranoside, 1 mM, as substrate in sodium citrate, 50 mM, containing 0.01% TWEEN® 20. Beta-xylosidase / polypeptide with beta-xylosidase activity: The term beta-xylosidase means a beta-D-xyloside xylohydrolase (EC 3.2.1.37) that catalyzes the exohydrolysis of short beta(1⁴)-xylooligosaccharides to remove successive D-xylose residues from the non-reducing ends. Beta-xylosidase activity can be determined using 1 mM p-nitrophenyl-beta-D-xyloside as a substrate in 100 mM sodium citrate containing 0.01% TWEEN® 20 at pH 5, 40°C. One unit of beta-xylosidase is defined as 1.0 μmol of p-nitrophenolate anion produced per minute at 40°C, pH 5, from p-nitrophenyl-beta-D-xyloside, 1 mM, in sodium citrate, 100 mM, containing 0.01% TWEEN® 20. Cellobiohydrolase / polypeptide with cellobiohydrolase activity: 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 bonds in cellulose, 237873 1433329 of 42 cellooligosaccharides or any polymer containing glucose with beta-1,4 linkages, which releases cellobiose from the reducing end (cellobiohydrolase I) or the non-reducing end (cellobiohydrolase II) of the chain (Teeri, 1997, Trends in Biotechnology, 15: 160-167; Teeri et al., 1998, Biochem. Soc. Trans. 26: 173-178). Cellobiohydrolase activity can be determined according to the procedures described by 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. Cellulolytic enzyme or cellulase / polypeptide with cellulase activity or cellulolytic activity: The term cellulolytic enzyme or cellulase means one or more (for example, several) enzymes that hydrolyze a cellulosic material, comprising any material containing cellulose, such as fiber. Cellulolytic enzymes include endoglucanase(s) (EC 3.2.1.4), cellobiohydrolase(s) (EC 3.2.1.91 and EC 3.2.1.150), beta-glucosidase(s) (EC 3.2.1.21), or combinations thereof. The two basic approaches to measuring cellulolytic enzyme activity include: (1) measuring total cellulolytic enzyme activity and (2) measuring individual cellulolytic enzyme activities (endoglucanases, cellobiohydrolases, and beta-glucosidases), as reviewed in Zhang et al., 2006, Biotechnology Advances 24: 452-481.Total cellulolytic enzyme activity can be measured using insoluble substrates, including Whatman Ns1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common assay for total cellulolytic activity is the filter paper assay using Whatman N1 filter paper as the substrate. This assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Pure Appl. Chem. 59: 257-68). Cellulolytic enzyme activity can be determined by measuring the increase in sugar production and release during the hydrolysis of a cellulosic material by cellulolytic enzyme(s) under the following conditions: 1-50 mg of cellulolytic enzyme protein / g of cellulose in pretreated corn stover (PCS) (or other pretreated cellulosic material) for 3-7 days at a suitable temperature such as 40°C-80°C, for example, 40°C, 45°C, 50°C, 55°C, 60°C, 65°C, 70°C, 75°C or 80°C, and a suitable pH, such as 4-9, for example, 4.0, 4.5, 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, 8.5. or 9.0, compared to a control hydrolysis without the addition of cellulolytic enzyme protein. Typical conditions are reactions of 1 ml, washed or unwashed PCS, 5% insoluble solids (dry weight), 50 mM sodium acetate pH 5, 1 mM MnSO4, 50°C, 55°C 237873 1433329 at 42 or 60°C, 72 hours, sugar analysis by column chromatography AMINEX® HPX-87H (Bio-Rad Laboratories, Inc., Hercules, CA, USA). Endoglucanase: The term endoglucanase refers to 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), lichenin, beta-1,4 linkages in beta-1,3 mixed glucans, such as beta-D-glucans or cereal xyloglucans, and other plant material containing cellulosic components. Endoglucanase activity can be determined by measuring the reduction in substrate viscosity or the increase in reducing ends, as determined by a reducing sugar assay (Zhang et al., 2006, Biotechnology Advances 24: 452-481). For the purposes of the present invention, the endoglucanase activity is 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. Glycoside hydrolase family 61: The term glycoside hydrolase family 61 or GH61 family or GH61 means a polypeptide that belongs to the glycoside hydrolase family 61 according to Henrissat, 1991, A classification of glycosyl hydrolases on the basis of amino acid sequence similarities, Biochem. J. 280: 309-316, and Henrissat and Bairoch, 1996, Update of the classification on the basis of sequence 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 family member. The structure and mode of action of these enzymes are not canonical, and they cannot be considered authentic glycosidases.However, they remain in the CAZy classification based on their ability to enhance lignocellulose decomposition when used in conjunction with a cellulase or a mixture of cellulases. GH61 polypeptides have recently been classified as lytic polysaccharide monooxygenases (Quinlan et al., 2011, Proc. Natl. Acad. Sci. USA, 208: 15079-15084; Phillips et al., 2011, ACS Chem. Biol. 6: 1399-1406; Lin et al., 2012, Structure 20: 1051-1061), and are designated Auxiliary Activity 9 or AA9 polypeptides. Hydrolytic enzymes or hydrolase / polypeptide with hydrolase activity: Hydrolytic enzymes refer to any catalytic protein that uses water to break down substrates. Hydrolytic enzymes include cellulases (EC 3.2.1.4), xylanases (EC 3.2.1.8), arabinofuranosidases (EC 3.2.1.55 (non-reducing terminal alpha-L-arabinofuranosidases); EC 3.2.1.185 (non-reducing terminal beta-L-arabinofuranosidases), 237873 1433329 of 42 cellobiohydrolase I (EC 3.2.1.150), cellobiohydrolase II (EC 3.2.1.91), cellobiosidase (EC 3.2.1.176), beta-glucosidase (EC 3.2.1.21), beta-xylosidases (EC 3.2.1.37). Xylanases / polypeptide with xylanase activity: The term xylanase refers to a 1,4β-D-xylan-xylohydrolase (EC 3.2.1.8) that catalyzes the endohydrolysis of 1,4-β-D-xylosidic linkages in xylans. Xylanase activity can be determined using 0.2% AZClarabinoxylan as a substrate in 0.01% TRITON® X-100 and 200 mM sodium phosphate, 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 pH 6. Xylanases can be found, for example, in the GH5, GH30, GH10 and GH11 families. Polypeptide GH5: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 5 family in the Carbohydrate-Active EnZymes (CAZymes) database (http: / / www.cazv.org / ). Polypeptide GH8: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 5 family in the Carbohydrate-Active EnZymes (CAZymes) database (http: / / www.cazv.org / ). Polypeptide GH30: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 30 family in the Carbohydrate-Active EnZymes (CAZymes) database (http: / / www.cazv.org / ). Polypeptide GH10: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 10 family in the Carbohydrate-Active EnZymes (CAZymes) database available at http: / / www.cazv.org / . (Lombard, V.; Golaconda Ramulu, H.; Drula, E.; Coutinho, PM; Henrissat, B. (November 21, 2013). The carbohydrate-active enzymes (CAZy) database in 2013. Nucleic Acids Research. 42 (D1): D490-D495; Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (January 2009). The Carbohydrate-Active Enzymes (CAZy) Database: A Qualified Resource for Nucleic Acids Res. 37 (Database Publication): D233-8). Polypeptide GH11 refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase family 11 in the Carbohydrate-Active EnZymes (CAZymes) database. 237873 1433329 of 42 Polypeptide GH62: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 62 family in the Carbohydrate-Active EnZymes (CAZymes) database. Polypeptide GH43: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 43 family in the Carbohydrate-Active EnZymes (CAZymes) database. Polypeptide GH51: refers to a polypeptide with enzymatic activity, where the polypeptide is classified as a member of the glycoside hydrolase 51 family in the Carbohydrate-Active EnZymes (CAZymes) database. Other definitions: In this context, the terms are commonly used to refer to the expert. Some of these terms are clarified below: Contact time: For one or more enzymes to react with a substrate, they must be in contact with it. Contact time refers to the period of time during which an effective amount of one or more enzymes is in contact with at least a fraction of the substrate's mass. The enzymes may not be in contact with the entire mass of the substrate during the contact time; however, the mixing of the enzymes with a portion of the substrate allows for the potential for enzyme-catalyzed hydrolysis of a fraction of the substrate's mass during the contact time. Corn kernels: There is a diversity of corn kernels, including, for example, dent corn, flint corn, corn on the cob, striped corn, sweet corn, waxy corn, and the like. Some corn kernels have an outer covering called the pericarp, which protects the germ inside the kernel. It is resistant to water and water vapor and is undesirable for insects and microorganisms. The only area of ​​the kernel not covered by the pericarp is the tip cap, which is the point where the kernel attaches to the cob. Corn kernels or a fraction of corn kernels: This term is used to describe corn kernels after the wet milling process. When corn kernels are broken down and processed, all fractionated parts of the corn kernel are considered included when this term is used. The term includes, for example: soaked kernels, ground kernels, corn kernel mass, a first fraction, a second fraction, one or more fractions of the corn kernel mass, etc. 237873 1433329 of 42 Corn kernel mash: This term is preferably used to refer to a mash comprising fiber, gluten, and starch, preferably obtained by steam-milling harvested kernels and separating a mash comprising fiber, gluten, and starch from the germ. As the corn kernel mash moves through the fiber washing process, it separates into several fractions, including a first fraction (s) and a second fraction (f). Therefore, corn kernel mash fractions and one or more corn kernel mash fractions refer, among other things, to these first (s) and second (f) fractions. cDNA: The term cDNA refers to a DNA molecule that can be prepared by reverse transcription from a mature, spliced ​​mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks intronic sequences that may be present in the corresponding genomic DNA. The initial primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as mature, spliced ​​mRNA. Coding sequence: The term coding sequence refers to 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, beginning with a start codon such as ATG, GTG, or TTG, and ending with a stop codon such as TAA, TAG, or TGA. The coding sequence can be genomic DNA, cDNA, synthetic DNA, or a combination thereof. Control sequences: The term control sequences means nucleic acid sequences required for the expression of a polynucleotide encoding a mature polypeptide of the present invention. Each control sequence may be native (i.e., from the same gene) or foreign (i.e., from a different gene) to the polynucleotide encoding the polypeptide, or native or foreign to each other. Such control sequences include, without limitation, a leader sequence, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, control sequences include a promoter and transcription and translation stop signals. Control sequences may be provided with linkers to introduce specific restriction sites that facilitate the binding of the control sequences to the coding region of the polynucleotide encoding a polypeptide. Expression: The term expression includes any step involved in the production of a polypeptide, including, without limitation, transcription, post-transcriptional modification, translation, post-translational modification, and secretion. 237873 1433329 of 42 Expression vector: The term expression vector means a linear or circular DNA molecule comprising a polynucleotide encoding a polypeptide and operatively linked to control sequences that provide for its expression. Fragment: the term fragment means a polypeptide having one or more (e.g., several) amino acids missing from the amino and / or carboxy-terminal end of a mature polypeptide, wherein the fragment has pectin lyase activity. Germ: The germ is the only living part of the corn kernel. It contains the essential genetic information, enzymes, vitamins, and minerals that allow the kernel to develop into a corn plant. In yellow dent corn, about 25 percent of the germ is corn oil. The endosperm, covered or surrounded by the germ, comprises about 82 percent of the kernel's dry weight and is the source of energy (starch) and protein for the germinating seed. There are two types of endosperm: soft and hard. In hard endosperm, the starch is tightly bound. In soft endosperm, the starch is loosely bound. Gluten: Gluten is a protein composed of two smaller proteins, glutenin and gliadin. In this document, gluten refers to most of the proteins found in corn kernels. The main gluten products from wet milling of corn are corn gluten meal (approximately 60% protein) and corn gluten feed (approximately 20% protein). Grinding or milling: The term grinding refers to breaking down corn kernels into smaller components. Host cell: The term host cell means any type of cell that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or with an expression vector comprising a polynucleotide of the present invention. The term host cell encompasses any progeny of a parental cell that is not identical to the parental cell due to mutations occurring during replication. Isolated: The term isolated means a substance in a form or environment not found in nature. Non-limiting examples of isolated substances include (1) any non-natural substance; (2) any substance, including, without limitation, any enzyme, variant, nucleic acid, protein, peptide, or cofactor, that has been 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 intervention in relation to that substance as found in nature; or (4) any substance modified by increasing the amount of the 237873 1433329 of 42 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 promoter stronger than the promoter naturally associated with the gene encoding the substance). Incubation time: time during which one or more fractions of the corn kernel mass are in contact with the hydrolytic enzyme during fiber washing, without being sieved. In many preferred embodiments, a method according to the present invention uses a system comprising a space (V), or incubator, within which the material is left to be affected by the enzymes, and in such situations, the incubation time can be determined by: incubator volume [m3] * influx density to the incubator [kg / m3] * mass influx per unit time to the incubator [kg / s] Alternatively, if the influx to the incubator is expressed in terms of volume per unit of time: incubator volume [m3] inflow volume per unit of time to the incubator [m3 / s] 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. It is known in the art that a host cell can produce a mixture of two different mature polypeptides (i.e., with a different C-terminal and / or N-terminal amino acid) expressed from the same polynucleotide. It is also known in the art that different host cells process polypeptides differently, and therefore, a host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., one with a different C-terminal and / or N-terminal amino acid) compared to another host cell expressing the same polynucleotide. Mature polypeptide coding sequence: The term mature polypeptide coding sequence means a polynucleotide that encodes a mature polypeptide. Grinding equipment: “Grinding equipment” refers to all the equipment used in a mill. The wet grinding process will vary depending on the grinding equipment available. Examples of grinding equipment include soaking tanks, evaporators, 237873 1433329 of 42 screw press, rotary dryer, dewatering screen, centrifuge, hydrocyclone, etc. The size and quantity of each grinding equipment or grinding line may vary in different mills, which will affect the grinding process. For example, the number of fiber washing screening units may vary, as well as the size of a centrifuge. Nucleic acid construct: The term nucleic acid construct means a nucleic acid molecule, either single-stranded or double-stranded, that is isolated from a natural gene or modified to contain nucleic acid segments in a manner that does not exist in nature, or that is synthetic, comprising one or more control sequences. Operationally bound: The term operationally bound means a configuration in which a control sequence is placed in an appropriate position with respect to the coding sequence of a polynucleotide, such that the control sequence directs the expression of the coding sequence. Retention time: The time during which one or more hydrolytic enzymes and corn kernels or a fraction of the corn kernels are allowed to react during the fiber washing procedure. In some embodiments, the retention time is the period of time during which the mass of corn kernels, received at the first screening unit (S1), and one or more fractions thereof are brought into contact with an effective quantity of one or more hydrolytic enzymes before exiting the fiber washing system again. During the retention time, the one or more fractions of corn kernel mass are incubated with one or more hydrolytic enzymes in a space (V) before exiting the fiber washing system, either as part of a first fraction (s1) from the upstream screening unit (S1) or as part of a second fraction (f4) from the downstream screening unit (S4). The retention time can preferably be estimated as the average duration of time that the solid material spends in a fiber washing system as defined in relation to the present invention. This can be estimated using the following relationship: system volume: [m3] * mass inflow density [^^ / m3] mass inflow per unit time to the system [H] Alternatively, if the inflow to the system is expressed in terms of volume per unit of time: 237873 1433329 of 42 system volume [m3] inflow volume per unit of time to the system [m3 / s] The volume of the system is generally set equal to the sum of the volumes of all the voids in the system; however, since the system tube is normally made small, it may be preferable to ignore the volume of the tube. Screening: The term screening refers to the process of separating the mass of corn kernels into a first fraction s and a second fraction f, and the movement of these fractions from one screening unit to another. A non-screening period is a period of non-separation provided for the incubation of the mass of corn kernels, or its fractions, with enzymes. Sequence identity: The relationship between two amino acid sequences or between two nucleotide sequences is described by the sequence identity parameter. For the purposes of the present invention, the degree of 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 EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 3.0.0 or later. Version 6.1.0 was used. The optional parameters used are a space opening penalty of 10, a space extension penalty of 0.5, and the EBLOSUM62 substitution matrix (EMBOSS version of BLOSUM62). The Needle output labeled as the longest identity (obtained using the -not short option) is used as the percent identity, and is calculated as follows: (Identical residues x 100) / (Alignment length - Total number of spaces in the alignment). Starch: The term starch means any material composed of complex plant polysaccharides, made up of glucose units that are widely found in plant tissues in the form of storage granules, consisting of amylose and amylopectin, and are represented as (C6H10O5)n, where n is any number. Soaking or soaking: The term “soaking” means soaking the harvested grain with water and, optionally, SO2. 237873 1433329 of 42 DETAILED DESCRIPTION. It is an object of the present invention to provide a method that improves the yield of starch and gluten from a wet milling process of corn. In particular, it is an object of the present invention to provide a method for improving the starch and / or gluten yields obtainable from corn kernels in a wet milling process by treating the fiber fraction with a hydrolytic enzyme composition, preferably during a fiber washing procedure. The inventors of the present invention have surprisingly discovered that the enzymatic treatment of corn fiber in the presence of at least one xylanase and / or cellulase and an effective amount of SO2 increases the release of bound starch and gluten from the fiber and thus improves the obtainable starch and / or gluten yields. The wet grinding process: The corn kernels are wet-milled to open the kernels and separate them into their four main components: starch, germ, fiber, and gluten. The wet grinding process can vary significantly from mill to mill; however, conventional wet grinding generally comprises the following steps: 1. Soaking 2. Grinding 3. Separation into streams comprising: i) germ; ii) fiber; iii) starch and gluten 4. Washing, pressing and drying of fibers 5. Starch / gluten separation, and 6. Starch washing. Soaking, grinding and germ separation. The corn kernels are softened by soaking them in water for about 30 minutes to about 48 hours, preferably from 30 minutes to about 15 hours. 237873 1433329 of 42, such as around 1 hour to around 6 hours at a temperature of around 50°C, such as between around 45°C and 60°C. During soaking, the kernels absorb water, increasing their moisture content from 15 percent to 45 percent and more than doubling their size. The optional addition of, for example, 0.1 percent sulfur dioxide (SO2) and / or NaHSO3 to the water prevents excessive bacterial growth in the warm environment. As the corn swells and softens, the mild acidity of the soaking water begins to loosen the gluten bonds within the corn and release the starch. After soaking, the corn kernels are opened by milling to release the germ. The germ contains corn oil.The germ is separated from the denser mixture of starch, gluten, and fiber (the mass of corn kernels comprising fiber, starch, and gluten) essentially by floating the germ segment free of the other substances under strictly controlled conditions. This method eliminates any adverse effects of traces of corn oil in subsequent processing steps. The germ can then be dried, and the oil extracted. The mass of corn kernels comprising fiber, starch, and gluten is subsequently separated into fractions of fiber, starch, and gluten, for example, in a fiber washing step. Washing, pressing and drying of fibers. To maximize starch and gluten recovery while minimizing fiber content in the final product, it is necessary to wash the free starch and gluten off the fiber during processing. The free starch and gluten are separated from the fiber during screening (washing) and collected as milled starch. The remaining fiber is then pressed to reduce its moisture content. Starch and gluten separation. The starch and gluten suspension, along with the additional starch gluten released from the fiber washing step, called milling starch, are separated into starch and gluten. Gluten has a lower density compared to starch. When milling starch is passed through a centrifuge, the gluten is easily centrifuged. Starch washing. The starch suspension from the starch separation step contains some insoluble protein and a lot of soluble protein. These must be removed before high-quality starch (high-purity starch) can be made. The starch, with only one or two percent protein remaining, is diluted, washed 8 to 14 times, diluted again, and washed once more. 237873 1433329 of 42 hydroclones to remove the last trace of protein and produce high-quality starch, generally more than 99.5% pure. Products of wet milling: Wet milling can be used to produce, without limitation, corn mash liquor, corn gluten feed, germ, corn oil, corn gluten meal, corn starch, modified corn starch, syrups such as corn syrup and corn ethanol. One aspect of the present description is to provide a method for increasing the total yield of starch and / or gluten that can be obtained from corn kernels in a wet milling process, wherein the method comprises: mixing corn kernels or a fraction of corn kernels with an enzymatic composition comprising an effective amount of one or more hydrolytic enzymes, wherein at least one of said hydrolytic enzymes is selected from the group consisting of a xylanase polypeptide and / or cellulase polypeptide or one of their combinations. Some of the starch and / or gluten in corn kernels or corn kernel fractions may be bound to the fiber fraction and never released during the wet milling process. However, the addition of hydrolytic enzymes, which may include any catalytic protein that can use water to break down the substrates present in the corn kernels, can release some of the bound starch and / or gluten, thus increasing the overall starch and / or gluten yield in the wet milling process. The present inventors have surprisingly discovered that the effect of adding hydrolytic enzymes, such as cellulases and xylanases, to the fiber-rich fraction of the milled grain mass, particularly in a fiber washing step, can be enhanced with high levels of SO2. In one aspect, the present invention relates to a method for increasing the starch and / or gluten yield of corn kernels in a wet milling process, wherein the method comprises contacting milled corn kernels or a fraction thereof, particularly a fiber-rich fraction, with an effective amount of SO2 and an effective amount of one or more hydrolytic enzymes, wherein at least one of said hydrolytic enzymes is selected from xylanase and / or cellulase enzymes. Preferably, the contact is made during a fiber washing step. 237873 1433329 of 42 In one embodiment, the method of the present invention leads to an increase in the amount of starch and / or gluten released from the fiber during the wet milling process compared to a process in which there is no presence / addition of SO2. The specific procedure and equipment used in the wet grinding process may vary, but the main principles of the process remain the same (see description on the wet grinding process). In one particular embodiment, the method of the invention comprises the steps of: a) soaking the corn kernels in water to produce soaked kernels; b) grind the soaked grains to produce ground grains; c) separating the germs from the ground grains to produce a mass of corn kernels comprising fiber, starch and gluten; and d) subjecting the resulting mass of corn kernels comprising fiber to a fiber washing procedure, so as to separate starch, gluten and fiber; wherein at least one xylanase and / or cellulase and an effective amount of SO2 are present or added before or during step d). To achieve maximum starch and gluten recovery while minimizing fiber in the final product, it is necessary to wash free starch and gluten from the fiber fraction during processing. The fiber is collected, suspended, and sieved, typically after soaking, milling, and germ removal from the corn kernels, to recover any residual starch or gluten from the corn kernel mass. This process is referred to herein as the fiber washing procedure. In a preferred embodiment, said corn kernels or a fiber-rich fraction of said corn kernels are mixed with said one or more hydrolytic enzymes during the step of subjecting the corn kernel mass to a fiber washing procedure. According to the invention, to maximize the effect of the hydrolytic enzymes during the fiber washing step, a boosting effect is observed when an effective amount of SO2 is present during fiber washing. SO2 is often added in the grain soaking step; however, in downstream steps, such as the fiber washing step, the SO2 levels will have fallen below the levels claimed according to the present method. 237873 1433329 of 42 In one embodiment, SO2 is present / added during fiber washing in quantities of at least 400 ppm, at least 450 ppm, at least 500 ppm, at least 600 ppm, at least 700 ppm, at least 800 ppm. In another embodiment, SO2 is present or added during fiber washing in quantities in a range of 400-3000 ppm, 500-2000 ppm, 600-1500 ppm, such as 600-1200 ppm. The specific equipment used in the fiber washing process may vary, but the main principle of the process remains the same. The document WO2018 / 053220 describes a fiber washing system that includes a dedicated enzyme incubation space / tank. Based on this description and the general knowledge of the person skilled, it will be possible to design a fiber washing system that achieves a sufficient incubation time for the hydrolytic enzymes to function. In one embodiment, said corn kernels or a fraction of said corn kernels, for example, a fiber-rich fraction, is allowed to react with said one or more hydrolytic enzymes for at least 15 minutes, such as at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 35 minutes, at least 40 minutes, at least 45 minutes, at least 50 minutes, at least 55 minutes, at least 60 minutes, at least 70 minutes, at least 80 minutes, at least 90 minutes, at least 100 minutes, at least 110 minutes, or at least 120 minutes. In one embodiment, said fiber washing process comprises the use of a fiber washing system optimized for the introduction of one or more hydrolytic enzymes, wherein the fiber washing system comprises a space (V) configured to provide a total reaction time in the fiber washing system (retention time) of at least 35 minutes, such as at least 40 minutes, at least 45 minutes, at least 50 minutes, at least 60 minutes, at least 70 minutes, at least 80 minutes, at least 90 minutes, at least 100 minutes, at least 110 minutes, or at least 120 minutes and less than 48 hours, such as less than 40 hours, less than 36 hours, less than 30 hours, less than 24 hours, less than 20 hours, less than 12 hours, less than 10 hours, less than 8 hours, less than 6 hours, less than 5 hours, less than 4 hours. less than 3 hours.In one embodiment, the total retention time in the fiber washing system is between 35 minutes and 48 hours, for example, between 35 minutes and 24 hours, 35 minutes and 12 hours, 35 minutes and 6 hours, 35 minutes and 5 hours, 35 minutes and 4 hours, 35 minutes and 3 hours, 35 minutes and 2 hours, 45 minutes and 48 hours, 45 minutes and 24 hours, 45 minutes and hours, 45 minutes and 6 hours, 45. 237873 1433329 of 42 minutes and 5 hours, 45 minutes and 4 hours, 45 minutes and 3 hours, 45 minutes and 2 hours, 1-48 hours, 1-24 hours, 1-12 hours, 1-6 hours, 1-5 hours, 1-4 hours, 1-3 hours, 1-2 hours. In one embodiment, the fiber washing system comprises: - a plurality of screening units (S1^ S4) fluidly connected in a countercurrent washing configuration; wherein each screening unit is configured to separate a mass stream of corn kernels and liquid into two fractions: a first fraction (s) and a second fraction (f), wherein said second fraction (f) contains a greater amount, measured in % by weight, of fiber than the first fraction (s); - a space (V) arranged in the system and fluidly connected to receive said first fraction(s), said second fraction (f), or a mixed first and second fraction(s, f), preferably only a second fraction (f), and configured to provide an incubation time for one or both fractions received in the space; and the outlet of one or both fractions thus incubated to a downstream screening unit (S4), wherein the system is configured to - input of corn kernel mass and liquid to the upstream screening unit (S1) - outlet of the first fraction (s1) from the upstream screening unit (S1) as a starch-containing product stream, - process water inlet, preferably arranged for the inlet of process water to a downstream screening unit (S4), - output of the second fraction (f4) from the downstream screening unit (S4) as a washed corn kernel mass containing a lower amount of starch and gluten than the original corn kernel mass, - introduction of hydrolytic enzymes into the system. In one embodiment, the incubation time in said space (V) configured in the fiber washing system is at least 5 minutes, such as at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 30 minutes, at least 40 minutes, at least 45 minutes, at least 50 minutes, at least 60 minutes, at least 70 minutes, at least 80 minutes, at least 90 minutes, at least 100 minutes, at least 110 minutes or at least 120 minutes, and less than 48 hours, such as less than 40 hours, less than 36 hours, less than 30 hours, less than 24 hours, 237873 1433329 of 42 less than 20 hours, less than 12 hours, less than 10 hours, less than 8 hours, less than 6 hours, less than 5 hours, less than 4 hours, less than 3 hours. In one embodiment, the incubation time in said space (V) is between 35 minutes and 48 hours, such as between 35 minutes and 24 hours, 35 minutes and hours, 35 minutes and 6 hours, 35 minutes and 5 hours, 35 minutes and 4 hours, 35 minutes and 3 hours, 35 minutes and 2 hours, 45 minutes and 48 hours, 45 minutes and 24 hours, 45 minutes and 12 hours, 45 minutes and 6 hours, 45 minutes and 5 hours, 45 minutes and 4 hours, 45 minutes and 3 hours, 45 minutes and 2 hours, 1-48 hours, 1-24 hours, 1-12 hours, 1-6 hours, 1-5 hours, 1-4 hours, 1-3 hours, 1-2 hours. In one embodiment, the incubation temperature in said space (V) is between 25 and 95°C, such as between 25 and 90°C, 25 and 85°C, 25 and 80°C, 25 and 75°C, 25 and 70°C, 25 and 65°C, 25 and 60°C, 25 and 55°C, 25 and 53°C, 25 and 52°C, 30 and 90°C, 30 and 85°C, 30 and 80°C, 30 and 75°C, and 70°C, 30 and 65°C, 30 and 60°C, 30 and 55°C, 30 and 53°C, 30 and 52°C, 35 and 90°C, 35 and 85°C, and 80°C, 35 and 75°C, 35 and 70°C, 35 and 65°C, 35 and 60°C, 35 and 55°C, 35 and 53°C, 35 and 52°C, and 90°C, 39 and 85°C, 39 and 80°C, 39 and 75°C, 39 and 70°C, 39 and 65°C, 39 and 60°C, 39 and 55°C, and 53°C, 39 and 52°C, such as 46 and 52°C. Furthermore, the dimension of the space (in m3) is preferably configured to provide an incubation time of at least 5 minutes, such as at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 35 minutes, at least 40 minutes, at least 45 minutes, at least 50 minutes, at least 55 minutes, at least 60 minutes, at least 70 minutes, at least 80 minutes, at least 90 minutes, at least 100 minutes, at least 110 minutes, at least 120 minutes. The space (V) designated for incubation preferably has a volume of at least 30 m³, at least 40 m³, at least 50 m³, at least 60 m³, at least 70 m³, at least 80 m³, at least 90 m³, at least 100 m³, at least 110 m³, at least 120 m³, at least 130 m³, at least 140 m³, at least 150 m³, at least 160 m³, at least 170 m³, at least 180 m³, at least 190 m³, at least 200 m³, at least 210 m³, at least 220 m³, at least 230 m³, at least 240 m³, at least 250 m³, at least 260 m³, at least 270 m³, at least 280 m³, at least 290 m³, at least 300 m³, at least 400 m³, or at least 500 m³. The incubation period may also be in more than one space V with a total or combined volume of at least 100 m³, at least 110 m³, at least 120 m³, at least 130 m³, at least 140 m³, at least 150 m³, at least 237873 1433329 of 42 160 m3, at least 170 m3, at least 180 m3, at least 190 m3, at least 200 m3, at least 210 m3, at least 220 m3, at least 230 m3, at least 240 m3, at least 250 m3, at least 260 m3, at least 270 m3, at least 280 m3, at least 290 m3, at least 300 m3, at least 400 m3, at least 500 m3. During the incubation period, it is preferable that the fluid received in space V not be screened. Therefore, the fluid leaving space V has the same composition, e.g., of starch and fiber, as the fluid received in space V, although it preferably contains a higher proportion of starch that has been released from the fibers. To ensure intimate contact between the enzymes and the fiber, it may be preferable to configure space V for agitation of the matter contained in said space V, for example, by comprising a rotor or an impeller. Space V is preferably arranged downstream of the upstreammost screening unit S1, and upstream of the downstreammost screening unit S4; in particular, space V is arranged to feed fluid to the second downstream screening unit S3. Hydrolytic enzymes suitable for the method of invention. In one embodiment, the hydrolytic enzymes suitable for use in the method of the invention comprise one or more enzymes selected from the group consisting of: cellulases (EC 3.2.1.4), xylanases (EC 3.2.1.8), arabinofuranosidases (EC 3.2.1.55 (non-reducing terminal alpha-larabinofuranosidases); EC 3.2.1.185 (non-reducing terminal beta-larabinofuranosidases), cellobiohydrolase I (EC 3.2.1.150), cellobiohydrolase II (EC 3.2.1.91), cellobiosidase (EC 3.2.1.176), beta-glucosidase (EC 3.2.1.21), beta-xylosidases (EC 3.2.1.37), and proteases (EC 3.4). In one embodiment, xylanase is selected from the group consisting of a GH5 polypeptide, a GH30 polypeptide, a GH10 polypeptide, a GH11 polypeptide, a GH8 polypeptide, or a combination thereof. In another embodiment, the hydrolytic enzymes comprise one or more cellulases. The cellulases may be selected from at least the group consisting of an endoglucanase (EG) and a cellobiohydrolase (CBH). More specifically, the cellulases comprise one or more enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase I, a cellobiohydrolase II, or a combination thereof. 237873 1433329 of 42 In one embodiment, the hydrolytic enzymes further comprise an arabinofuranosidase. The arabinofuranosidase can be selected from the group consisting of polypeptide GH43, polypeptide GH62, and polypeptide GH51, particularly polypeptide GH62. In one embodiment, one or more hydrolytic enzymes are expressed in an organism with a cellulase background, such as Trichoderma reesei. According to these embodiments, the xylanase and / or arabinofuranosidase polypeptides defined according to the invention are expressed together with endogenous cellulases from Trichoderma. In one embodiment, the enzyme composition comprising one or more hydrolytic enzymes may comprise cellulases expressed in Trichoderma reesei and other hydrolytic enzymes that are added to the enzyme composition in a purified or semi-purified form. In one embodiment, one or more hydrolytic enzymes are purified. The purified enzymes can be used in an enzyme composition as described in other embodiments of the present invention. In one embodiment, the hydrolytic enzyme(s) are in a liquid composition. The composition can be homogeneous or heterogeneous. In one embodiment, the hydrolytic enzyme(s) are in a solid composition. In one embodiment, the effective amount of one or more hydrolytic enzymes mixed with one or more fractions of said mass of corn kernels is between 0.005-0.5 kg of enzyme protein (EP) / 1000 kg (1 metric ton (MT)) of corn kernels entering the wet milling process, such as between 0.010-0.5 kg EP / 1000 kg (1 MT) of corn kernels, such as between 0.05-0.5 kg / 1000 kg (1 MT) of corn kernels, or 0.075-0.5 kg / 1000 kg (1 MT) or 0.1-0.5 kg / 1000 kg (1 MT) of corn kernels, or 0.005-0.4 kg / 1000 kg (1 MT) of corn kernels, or 0.01-0.4 kg / 1000 kg (1 MT) of corn kernels, or 0.05-0.4 kg / 1000 kg (1 MT) of corn kernels, or 0.075-0.4 kg / 1000 kg (1 MT) of corn kernels, or 0.1-0.4 kg / 1000 kg (1 MT) of corn kernels, or 0.005-0.3 kg / 1000 kg (1 MT) of corn kernels, or 0.01-0.3 kg / 1000 kg (1 MT) of corn kernels, or 0.05-0.3 kg / 1000 kg (1 MT) of corn kernels, or 0.075-0.3 kg / 1000 kg (1 MT) or 0.1-0.3 kg / 1000 kg (1 MT) of corn kernels, or 0.005-0,2 kg / 1000 kg (1 MT) of corn kernels, or 0.01-0.2 kg / 1000 kg (1 MT) of corn kernels, or 0.05-0.2 kg / 1000 kg (1 MT) of corn kernels, or 0.075-0.2 kg / 1000 kg (1 MT) or 0.1-0.2 kg / 1000 kg (1 MT) of corn kernels, or 237873 1433329 of 42 such as 0.075-0.10 kg / 1000 kg (1 MT) of corn kernels, or 0.075-0.11 kg / 1000 kg (1 MT) of corn kernels. In preferred embodiments, the enzyme composition comprises cellulase obtained from a culture of Trichoderma reesei, such as a culture of Trichoderma reesei ATCC 26921. Suitable cellulases are available, for example, from Novozymes A / S under the trade name Celluclast®. Polypeptides that have xylanase activity. Xylanases are suitable for use in the method according to the invention. The xylanase polypeptide can be selected from the GH5, GH10, GH30, GH11, and GH8 families. The more specific embodiments relate to the method according to the invention, wherein the xylanase enzyme GH5 is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, 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: 1; (b) a variant of the mature polypeptide of SEQ ID NO: 1 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. The mature polypeptide, in one embodiment, is amino acids 25 to 551 of SEQ ID NO: 1. Another specific embodiment refers to the method according to the invention, wherein the GH10 xylanase is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, 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: 2; (b) a variant of the mature polypeptide SEQ ID NO: 2 comprising a substitution, deletion and / or insertion at one or more positions; and 237873 1433329 of 42 (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. The mature polypeptide in one embodiment form is amino acids 21 to 405 of SEQ ID NO: 2. Another specific embodiment refers to the method according to the invention, wherein the xylanase GH10 is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, 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; (b) a variant of the mature polypeptide of SEQ ID NO: 4 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. The mature polypeptide in one embodiment form is amino acids 20 to 319 of SEQ ID NO: 4. Polypeptides that have arabinofuranosidase activity. Another specific embodiment relates to the method according to the invention, wherein the arabinofuranosidase GH62 is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, 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: 3; (b) a variant of the mature polypeptide of SEQ ID NO: 3 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. The mature polypeptide in one embodiment is amino acids 17 to 325 of SEQ ID NO: 3. 237873 1433329 of 42 Sources of polypeptides that have xylanase activity. A polypeptide having xylanase activity can be obtained from microorganisms of any genus. For the purposes of the present invention, the term "obtained from," as used herein in relation to a given source, means that the polypeptide encoded by a polynucleotide is produced by the source or by a strain into which the polynucleotide from the source has been inserted. In one aspect, the polypeptide obtained from a given source is secreted extracellularly. El polipeptide puede ser un polipeptide bacterialo. Por ejemplo, the polypeptide can be a Gram-positive bacterial polypeptide, such as a Bacillus, Chryseobacterium, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces que tiene activity de pectin liasa, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaplasma. In one aspect, the polypeptide is a polypeptide 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. In another aspect, the polypeptide is a polypeptide from Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, or Streptococcus equi subsp. Zooepidemicus. In another aspect, the polypeptide is a polypeptide of Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus, or Streptomyces lividans. The polypeptide can be a fungal polypeptide. For example, the polypeptide can be a yeast polypeptide, such as a Candida, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces, or Yarrowia polypeptide; or a filamentous fungal polypeptide such as a polypeptide from Acremonium, Agaricus, Alternaria, Aspergillus, for example, Aspergillus niger, 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, by 237873 1433329 of 42 example, Talaromyces leycettanus, Thermoascus, Thielavia, Tolypocladium, Trichoderma, Trichophaea, Verticillium, Volvariella, or Xylaria. Strains of these species are readily accessible to the public from a number of 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). 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 the probes mentioned above. Techniques for isolating microorganisms and DNA directly from natural habitats are well known in the field. A polynucleotide encoding the polypeptide can then be obtained by similarly screening a genomic DNA or cDNA library from another microorganism or a mixed DNA sample. Once a polynucleotide encoding a polypeptide has been detected with the probes, the polynucleotide can be isolated or cloned using techniques known to those skilled in the art (see, for example, Sambrook et al., 1989, supra). Enzyme compositions. An enzyme composition for use in the method according to the invention may comprise a xylanase polypeptide as the main enzyme component, for example, a single-component composition. Alternatively, the compositions may comprise multiple enzyme activities, such as one or more (for example, several) enzymes selected from the group consisting of cellobiohydrolase, cellulase, endoglucanase, and / or arabinofuranosidase. The compositions can be prepared according to known methods in the art and can be presented in liquid or dry form. The compositions can be stabilized according to known methods in the art. The invention is further described in the following numbered embodiments. Implementation 1. A method for increasing the starch yield and / or gluten yield of maize kernels in a wet milling process, which 237873 1433329 of 42 comprises contacting a fiber-rich fraction of ground grains with an effective amount of SO2 and an effective amount of one or more hydrolytic enzymes, wherein at least one of said hydrolytic enzymes is selected from xylanase and / or cellulase enzymes, during a fiber washing step. Embodiment 2. The method according to embodiment 1, wherein the amount of starch and / or gluten released from the fiber during the wet milling process is increased compared to a process in which SO2 is neither present nor added. Embodiment 3. The method according to any of the above embodiments, comprising the steps of: a) soaking the corn kernels in water to produce soaked kernels; b) grind the soaked grains to produce ground grains; c) separating the germs from the ground grains to produce a mass of corn kernels comprising fiber, starch and gluten; and d) subjecting the resulting mass of corn kernels comprising fiber to a fiber washing procedure, so as to separate starch, gluten and fiber; wherein at least one xylanase and / or cellulase enzyme and an effective amount of SO2 are present or added before or during step d). Embodiment 4. The method of any of embodiments 1-3, wherein SO2 is present or added during the fiber washing step (d) in amounts of at least 400 ppm, at least 450 ppm, at least 500 ppm, at least 600 ppm, at least 700 ppm, at least 800 ppm. Embodiment 5. The method of any of embodiments 1-4, wherein SO2 is present or added during fiber washing in quantities in a range of 400-3000 ppm, 500-2000 ppm, 600-1500 ppm, such as 600-1200 ppm. Embodiment 6. The method of any of the above embodiments, wherein the xylanase is selected from the group consisting of a GH5 polypeptide, GH30 polypeptide, GH10 polypeptide, GH11 polypeptide, GH8 polypeptide, or a combination thereof. 237873 1433329 of 42 Embodiment 7. The method of any of the preceding embodiments, wherein the hydrolytic enzymes comprise one or more cellulases, particularly cellulases obtained from Trichoderma, more particularly from Trichoderma reesei. Embodiment 8. The method of embodiment 7, wherein the cellulases comprise one or more enzymes selected from the group consisting of an endoglucanase (EG) and a cellobiohydrolase (CBH). Embodiment 9. The method of embodiment 8, wherein the cellulases comprise one or more enzymes selected from the group consisting of an endoglucanase, a cellobiohydrolase I, a cellobiohydrolase II, or a combination thereof. Embodiment 10. The method of any of the above embodiments, wherein the hydrolytic enzymes further comprise an arabinofuranosidase. Embodiment 11. The method of embodiment 10, wherein the arabinofurasnosidase is selected from the group consisting of a polypeptide GH43, a polypeptide GH62 and a polypeptide GH51. Embodiment 12. The method according to any of embodiments 3-9, wherein said fiber washing procedure comprises the use of a fiber washing system comprising a space (V) / tank configured to provide a total retention time in the fiber washing system of at least 35 minutes and less than 48 hours. Embodiment 13. The method according to any of the above embodiments, wherein the incubation time in said space (V) / tank configured in the fiber washing system is at least 5 minutes and less than 48 hours, such as between 35 minutes and 24 hours, 35 minutes and hours, 35 minutes and 6 hours, 35 minutes and 5 hours, 35 minutes and 4 hours, 35 minutes and 3 hours, 35 minutes and 2 hours, 45 minutes and 48 hours, 45 minutes and 24 hours, 45 minutes and 12 hours, 45 minutes and 6 hours, 45 minutes and 5 hours, 45 minutes and 4 hours, 45 minutes and 3 hours, 45 minutes and 2 hours. 237873 1433329 of 42 Embodiment 14. The method according to any of the preceding embodiments, wherein the incubation temperature is between 25°C and 95°C, such as between 25 and 90°C, 25 and 85°C, 25 and 80°C, 25 and 75°C, 25 and 70°C, 25 and 65°C, 25 and 60°C, 25 and 55°C, 25 and 53°C, 25 and 52°C, 30 and 90°C, 30 and 85°C, 30 and 80°C, 30 and 75°C, 30 and 70°C, and 65°C, 30 and 60°C, 30 and 55°C, 30 and 53°C, 30 and 52°C, 35 and 90°C, 35 and 85°C, 35 and 80°C, and 75°C, 35 and 70°C, 35 and 65°C, 35 and 60°C, 35 and 55°C, 35 and 53°C, 35 and 52°C, 39 and 90°C, and 85°C, 39 and 80°C, 39 and 75°C, 39 and 70°C, 39 and 65°C, 39 and 60°C, 39 and 55°C, 39 and 53°C, and 52°C, preferably 46 and 52°C. Embodiment 15. The method according to any of the above embodiments, wherein the level of SO2 present or added during fiber washing produces the same starch and gluten extraction yield, while reducing the required contact time between the hydrolytic enzyme and the mass of ground corn kernels compared to a method where SO2 levels are below 400 ppm. Embodiment 16. The method according to any of the above embodiments, wherein one or more hydrolytic enzymes are expressed in an organism with a cellulase background, such as Trichoderma reesei. Implementation method 17. The method in accordance with any of the above embodiments, wherein one or more hydrolytic enzymes are purified. Implementation method 18. The method in accordance with any of the above embodiments, wherein the one or more hydrolytic enzymes are in a liquid composition. Implementation method 19. The method in accordance with any of the above embodiments, wherein the one or more hydrolytic enzymes are in a solid composition. Implementation method 20. The method according to any of the above embodiments, wherein the effective quantity of one or more hydrolytic enzymes mixed or brought into contact with one or more fractions of said mass of grains of 237873 1433329 of 42 ground corn is between 0.005-0.5 kg of enzymatic protein / metric ton of corn kernels entering the wet milling process. Embodiment 21. The method according to any of the above embodiments, wherein the source of SO2 is sodium metabisulfite (Na2S2O5) and / or the addition of SO2 gas. Embodiment 22. The method according to any of the above embodiments wherein the xylanase is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, 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: 1; (b) a variant of the mature polypeptide of SEQ ID NO: 1 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. Implementation form 23. The method of implementation form 22, wherein the mature polypeptide is amino acids 1 to 551 of SEQ ID NO: 1. Embodiment 24. The method according to any of the above embodiments wherein the xylanase is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, 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: 2; (b) a variant of the mature polypeptide of SEQ ID NO: 2 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. Implementation form 25. The method of implementation form 24, wherein the mature polypeptide is amino acids 21 to 405 of SEQ ID NO: 2. 237873 1433329 of 42 Embodiment 26. The method of any of the above embodiments, wherein the arabinofuranosidase is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, 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: 3; (b) a variant of the mature polypeptide of SEQ ID NO: 3 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. Implementation form 27. The method of implementation form 26, wherein the mature polypeptide is amino acids 17 to 325 of SEQ ID NO: 3. Embodiment 28. The method according to any of the above embodiments wherein the xylanase is selected from the group consisting of: (a) a polypeptide having at least 85%, for example, 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; (b) a variant of the mature polypeptide of SEQ ID NO: 4 comprising a substitution, deletion and / or insertion at one or more positions; and (c) a fragment of the polypeptide of (a) or (b) having xylanase activity. Implementation form 29. The method of implementation form 28, wherein the mature polypeptide is amino acids 20 to 319 of SEQ ID NO: 4. Implementation form 30. The method according to any of the above implementation forms, wherein the cellulases are derived from Trichoderma reesei. The invention is further illustrated by the following examples. EXAMPLES. Enzymes: 237873 1433329 of 42 GH5 Xylanase A: GH5 xylanase derived from Chryseobacterium species 10696 and disclosed as SEQ ID NO: 1 Cellulase A: A whole cellulase derived from Trichoderma reesei. This cellulase composition will comprise all cellulase activities expressed in T. reesei; for example, endoglucanases and cellobiohydrolases. Example 1: The 10 g fiber assay is performed using a 5% dry fiber sample incubated at pH 4.0 and 50°C for 150 minutes with a dose of 200 pg or 300 pg of enzyme protein per gram of dry fiber. The enzyme used is a combination of cellulase A and xylanase GH5 A, along with 400 ppm or 800 ppm of hydrogen sulfite (HSO3-). The combination consists of 8% GH5 Xylanase A and 92% cellulase A based on the enzyme protein. Hydrogen sulfite is generated by adding sodium metabisulfite (Na2S2O5) to the buffer solution via the reaction Na2S2O5 + H2O → 2Na+ + 2HSO3-. For comparison, a combination containing 92% Cellulase A and 8% GH5 Xylanase A only (without SO2) was included at both low (200 pg EP / g-ds of fiber) and high (300 pg EP / g-ds of fiber) doses. Maize fiber with 17.77% residual starch and 9.88% residual protein was used as the substrate in the fiber assay.The release of starch + gluten (dry matter) as well as the individual protein of the corn fiber was measured in the treatment specified below. Table 1. Starch and gluten yield with and without enzymatic treatment. Treatments Dose (pg of enzyme protein / g-ds fiber) Starch + Gluten recovered Individual protein recovered Without enzyme 0 10.05% 0.65% Cellulase A + GH5 Xylanase A 200 12.20% 1.02% Cellulase A + GH5 Xylanase A + HSO3- (400 ppm) 200 14.45% 1.60% Cellulase A + GH5 Xylanase A + HSO3- (800 ppm) 200 15.00% 1.74% Cellulase A + GH5 Xylanase A 300 14.65% 1.48% Cellulase A + GH5 Xylanase A + HSO3- (400 ppm) 300 15.35% 1.82% 237873 1433329 of 42 Therefore, the addition of hydrogen sulfite on top of Cellulase A + GH5 Xylanase A can significantly increase the yield of starch + gluten, as well as protein in the wet milling process of corn. Example 2. A 10 g fiber assay typically involves incubating wet fiber samples obtained from a wet milling plant in the presence of enzymes, under process-appropriate conditions (pH 4, temperature around 50°C), for a period of 1 to 4 hours. After incubation, the fiber is transferred and pressed onto a 75-micron sieve, where the filtrates, consisting mainly of separated starch and gluten, are collected. Several washes are performed on the sieve, and these washes are collected along with the initial filtrate. The collected filtrates are allowed to stand overnight to allow the insolubles to settle to the bottom of the flask. Most of the supernatant is aspirated under vacuum, and the remaining insolubles are then centrifuged into 50 mL conical tubes. The supernatant is decanted to leave a wet, insoluble pellet. The wet, insoluble pellet is then lyophilized overnight until completely dry.This insoluble dry mass is weighed to determine the % insoluble yield, and then analyzed to determine the total nitrogen (protein) content using Leco analysis. This 10 g fiber assay was performed using a 6.4% dry fiber sample incubated at pH 4.0 and 48°C for 240 minutes with a dose of 5000 μg of enzyme protein per gram of dry fiber. The enzyme combination included cellulase A and GH5 xylanase A. The combination consisted of 10% GH5 xylanase A and 90% cellulase A on an enzyme protein basis. This combination was evaluated both in the substrate as is and in a sheared (homogenized) substrate (mixed for 3 minutes). The homogenized substrate was treated with the enzyme combination with and without 1000 ppm of SO2 (added from a 20x dilution of 1.48 g of sodium metabisulfate dissolved in 50 mL of water) and without enzymes. The substrate itself was treated with the combination of enzymes with and without 1000 ppm of SO2, while two treatments were carried out without enzyme, with and without 1000 ppm of SO2.The weights of insoluble mass (starch and gluten) and insoluble protein (gluten) released by the specified treatments are given below. Table 2. Results. 237873 1433329 of 42 Treatment % Initial fiber insolubles % Initial fiber insoluble protein % Increase in CGM over the respective control without enzymes Homogenate without enzyme Xylanase A 37.1% 38.3% 1.9% 3.3% 0.23% Xylanase A + SO2 39.7% 4.0% 0.35% as such without enzyme 29.6% 1.2% without enzyme + SO2 29.5% 1.5% 0.04% Xylanase A 36.5% 3.4% 0.36% Xylanase A + SO2 36.9% 3.7% 0.42% 237873 1433329 of 42 LIST OF SEQUENCES < 110> NOVOZYMES A / S < 120> IMPROVED FIBER WASHING IN WET MILLING OF CORN < 130> 15222-AR-NP < 160>4 < 170> PATENT VERSION 3.5 < 210>1 < 211>551 < 212> PRT < 213> ARTIFICIAL <220> < 223> SYNTHETIC CONSTRUCTION < 400> 1 MET 1 ASP GLU LYS ASN 5 LEU LEU GLU ASP PRO ASP 10 SER ASN LEU SER 15 ALA GLY ALA SER ALA 20 ARG ALA LEU ALA ALA 25 THR PRO MET LEU HIS 30 VAL GLY GLY ARG TYR 35 LEU LYS ASP PRO CYS 40 ASP ASN ASN VAL LEU 45 LEU HIS GLY VAL ALA 50 ILE THR PRO SER PRO 55 TRP PHE ASN GLY CYS 60 GLN TYR GLY ALA ASN 65 SER GLY TYR CYS THR 70 TRP ASP ASN TYR ASN 75 VAL GLN GLY CYS LEU 80 ASN TYR ASN LYS ALA 85 VAL MET ASN LYS LEU 90 THR SER ALA ALA ASP 95 GLY TRP TYR LEU ASN 100 TYR ILE ARG LEU HIS 105 ILE ASP PRO TYR TRP 110 THR ASN ASP PRO GLY 115 PRO SER ILE PRO GLU 120 ASN ASP ILE SER ARG 125 PHE ASN TYR ASN ARG 130 LEU VAL THR TYR THR 135 ASP GLN VAL ILE ILE 140 PRO LEU ILE ASN HIS 145 ALA ARG SER ARG GLY 150 MET TYR VAL ILE LEU 155 ARG PRO PRO GLY VAL 160 CYS PRO ASN ARG ILE 165 ALA VAL ASN ASP ALA 170 TYR HIS SER TYR LEU 175 LYS THR VAL TRP THR PHE LEU SER GLN HIS PRO GLY LEU LYS ASN ALA ASP 237873 1433329 de 42 180 185 190 5 ASN VAL MET 195 PHE GLU LEU ALA ASN 200 GLU PRO VAL GLU ILE 205 LEU GLY THR 10 ASN GLY 210 THR TRP GLY GLN THR 215 GLY ASN GLU HIS PHE 220 ALA ALA LEU LYS ASN 225 PHE PHE GLN PRO LEU 230 VAL ASN ILE ILE ARG 235 ASN ASN GLY ALA ASN 240 15 ASN VAL CYS TRP ILE 245 PRO GLY THR GLY TRP 250 GLN SER HIS TYR GLN 255 GLY 20 TYR PRO ASN ASN 260 GLN ILE THR GLY GLY 265 ASN ILE GLY TYR ALA 270 VAL HIS 25 ILE TYR PRO 275 SER TYR TRP GLY GLY 280 LEU SER ASN TYR GLN 285 ALA PHE GLN 30 ASN ALA 290 TRP ASN ILE ASN VAL 295 LYS PRO ILE ALA ASP 300 ILE ALA PRO ILE ALA 305 ILE THR GLU THR ASP 310 TRP ALA PRO GLN GLY 315 TYR GLY THR PHE GLY 320 35 ILE GLY THR THR GLY 325 THR ALA GLY GLY SER 330 GLY PHE GLY ALA ASN 335 LEU 40 LYS TYR ILE VAL 340 ASP GLN SER GLY ASN 345 VAL SER TRP ASN VAL 350 LEU ALA 45 PRO ASP ASN 355 LEU LEU HIS LYS GLY 360 ASP PRO ASN GLY GLY 365 THR ALA TYR 50 ASN ASN 370 ASP TRP GLU ALA CYS 375 ALA ALA PRO VAL LYS 380 GLN TRP PHE GLN GLN 385 TYR ALA LYS SER ASN 390 TYR PROVAL GLY ASN 395 CYS ASN THR THR SER 400 55 SER LEU VAL ASN ASN 405 GLY ILE TYR GLU ILE 410 GLU PHE GLN THR ASP 415 ALA 60 ASN LYS VAL VAL 420 ASP LEU LYS SER GLY 425 GLU ASP ALA ASN GLY 430 ALA VAL 65 LEU ARG PRO 435 TRP THR ARG ASN GLY 440 ALA ALA ALA GLN ARG 445 TRP VAL ALA 237873 1433329 de 42 ILE ASP ALA GLY ASN GLY TYR TRP ARG PHE VAL SER LYS ALA SER ALA 450 455 460 THR ASN ARG CYS ILE THR LEU ALA SER ASN SER 465 470 475 SER ILE VAL LEU TRP GLN ASN TYR GLY ASN ASP 485 490 VAL VAL ALA VAL SER ASN GLY TYR TYR LYS ILE 500 505 PRO THR ARG GLY TRP ASP ILE PRO ASN CYS THR 515 520 ASN LEU HIS LEU TRP ASP TYR TYR GLY THR SER 530 535 PHE LYS TYR ILE GLY MET ASN 545 550 <210>2 <211>405 < 212>PRT < 213> TALAROMYCES LEYCETTANUS < 400>2 MET VAL HIS LEU SER SER LEU ALA 15 ASN THR LEU GLY THR 480 ALA GLN ALA TRP GLN 495 LEU SER LYS VAL ASP 510 MET ASP GLY ASN SER 525 CYS GLN LEU PHE LYS 540 LEU ALA LEU ALA ALA GLY SER GLN 15 LEU ALA GLN ALA ALA GLY LEU ASN THR ALA ALA LYS ALA ILE GLY LYS 25 30 LEU TYR PHE GLY THR ALA THR ASP 40 ASN PRO GLU LEU SER ASP SER THR 45 TYR MET GLN GLU THR ASP ASN THR 55 ASP ASP PHE GLY GLN LEU THR PRO 60 ALA ASN SER MET LYS TRP ASP ALA 65 70 THR GLU PRO SER GLN ASN THR PHE 80 THR PHE THR ASN GLY ASP GLN ILE 85 ALA ASN LEU ALA LYS SER ASN GLY 95 GLN MET LEU ARG CYS HIS ASN LEU 100 VAL TRP TYR ASN GLN LEU PRO SER 105 110 TRP VAL THR SER GLY SER TRP THR 115 120 ASN ALA THR LEU LEU ALA ALA MET 125 237873 1433329 de 42 LYS ASN HIS ILE THR ASN VAL VAL THR HIS TYR LYS GLY GLN CYS TYR 130 135 140 ALA 145 SER PHE ASP ILE LEU 225 GLN THR ALA THR SER 305 ASP LEU THR GLY PRO 385 TRP ASP VAL VAL ASN 150 GLU ALA LEU ASN ASP ASP GLY THR TYR ARG 155 160 ASN VAL PHE TYR 165 GLN TYR ILE GLY GLU ALA TYR ILE PRO ILE ALA 170 175 ALA THR ALA 180 ALA ALA ALA ASP PRO ASN ALA LYS LEU TYR TYR ASN 185 190 TYR VAL 210 GLN SER GLU GLN PRO 290 TRP SER GLY ARG VAL 370 THR ASN 195 ILE GLU TYR PRO GLY 200 ALA LYS ALA THR ALA ALA GLN ASN 205 LYS SER ASN LEU GLN 275 LYS VAL ASN GLY THR 355 ALA THR MET VAL LYS ALA 215 TYR GLY ALA LYS ILE ASP GLY VAL GLY 220 HIS PHE ILE 230 VAL GLY SER THR PRO SER GLN SER SER GLN 235 240 MET ASP 260 SER CYS PRO TYR SER 340 SER GLN CYS ALA 245 ALA PHE THR ALA LEU GLY VAL GLU VAL ALA ILE 250 255 ILE ARG MET THR LEU PRO SER THR SER ALA LEU LEU 265 270 THR ASP TYR GLN 280 SER THR VAL SER ALA CYS VAL ASN 285 ILE ASN GLN 325 ALA THR HIS ALA GLY THR 310 LYS SER THR TRP SER 390 ILE 295 THR LEU TRP ASP TRP THR ASP LYS TYR 300 PHE LYS THR THR GLY 375 PRO SER PRO SER SER 360 GLN TYR GLY GLN GLY ASP ALA CYS PRO TRP 315 320 ALA TYR TYR GLY ILE LEU THR ALA 330 335 THR THR THR THR LEU VAL THR SER 345 350 THR SER ALA THR SER THR SER THR 365 CYS GLY GLY ILE GLY TRP THR GLY 380 THR CYS GLN GLU LEU ASN PRO TYR 395 400 237873 1433329 de 42 TYR TYR GLN CYS LEU 405 <210> <211> <212> <213> <400> MET HIS 1 3 325 PRT TALAROMYCES PINOPHILUS 3 ALA 5 PHE LEU ALA LEU LEU ALA VAL 10 SER PRO VAL PRO GLU LYS ARG SER GLY CYS LEU ALA PRO LEU LEU PRO VAL SER 30 SER 15 THR GLY TYR LYS TRP THR 35 SER THR GLY PRO LEU 40 ALA SER PRO LYS SER 45 GLY LEU VAL ALA LEU 50 ARG ASP TYR SER HIS 55 VAL ILE TYR ASN GLY 60 GLN HIS LEU VAL TYR 65 GLY SER THR ALA ASN 70 THR ALA GLY SER TYR 75 GLY SER MET ASN PHE 80 GLY LEU PHE SER ASP 85 TRP SEE GLU MET SEE 90 SEE ALA SEE GLN ASN 95 THR MET SEE THR GLOW 100 ALA CHOICE ALA PRO THR 105 ILE PHE BULL PHE ALA 110 PRO LIGHT SEE CHOICE TRP 115 ILE LEU ALA BULL GLN 120 TRP GLOW PRO BULL ALA 125 PHE SEE BULL ARG THR 130 SEE THR ASP PRO SEE 135 ASN ALA ASN GLOW TRP 140 SER SER PRO GLN PRO 145 LEU PHE THR GLY THR 150 ILE SER GLY SER SER 155 THR GLY VAL ILE ASP 160 GLN THR VAL ILE GLY 165 ASP SER GLU ASN MET 170 TYR LEU PHE PHE ALA 175 GLY ASP ASN GLY HIS 180 ILE TYR ARG ALA SER 185 MET PRO ILE GLY ASP 190 PHE PRO GLY SER PHE 195 GLY SER ALA SER THR 200 ILE VAL LEU SER ASP 205 SER THR ASN ASN LEU 210 PHE GLU ALA VAL GLU 215 VAL TYR THR VAL GLU 220 GLY GLN ASN GLN 237873 1433329 de 42 TYR LEU MET ILE VAL GLU ALA ILE GLY ALA ASN 225 230 235 GLY ARG TYR PHE ARG 240 SER PHE THR ALA SER SER LEU GLY GLY THR TRP 245 250 THR GLU SER ASN PRO PHE ALA GLY LYS ALA ASN 260 265 THR ASN ASP ILE SER SER GLY ASP LEU VAL ARG 275 280 THR GLN THR ILE ASP ALA CYS ASN LEU GLN PHE 290 295 SER THR SER SER GLY GLY ASP TYR ASN LEU LEU 305 310 315 LEU LEU THR LEU ALA 325 <210>4 <211>319 < 212>PRT < 213> ASPERGILLUS NIGER < 400>4 MET VAL GLN ILE LYS VAL ALA 15 VAL LEU SER GLU PRO ILE GLU 20 THR LYS PHE LYS ALA HIS GLY GLN TYR THR LEU THR LYS ASN 55 ASP PHE GLY ALA LEU THR PRO 70 GLU PRO SER ARG GLY GLN PHE ASN PHE ALA GLN SER ASN ASN 100 TRP HIS SER GLN LEU PRO SER 115 THR ALA GLN ALA SER 255 SER GLY ALA THR TRP 270 THR ASN PRO ASP GLN 285 LEU TYR GLN GLY ARG 300 PRO TYR GLN PRO GLY 320 ALA LEU ALA MET LEU PHE ALA SER GLN 15 PRO ARG GLN ALA SER VAL SER ILE ASP 30 LYS LYS TYR LEU GLY ASN ILE GLY ASP 40 45 SER LYS THR PRO ALA ILE ILE LYS ALA 60 GLU ASN SER MET LYS TRP ASP ALA THR 75 80 SER PHE SER GLY SER ASP TYR LEU VAL 90 95 LYS LEU ILE ARG GLY HIS THR LEU VAL 105 110 TRP VAL GLN SER ILE THR ASP LYS ASN 120 125 237873 1433329 de 42 THR LEU 130 ILE GLU VAL MET GLU ASN HIS ILE THR THR VAL MET GLN HIS 135 140 TYR LYS 145 GLU ASP ASP TYR ALA LYS LYS LEU 210 ILE PRO 225 ASN ALA ASP ILE CYS LEU ASP PRO 290 ASN TYR 305 GLY LYS ILE TYR ALA TRP ASP VAL VAL ASN GLU ILE PHE ASN 150 155 160 GLY SER LEU ARG ASP SER VAL PHE TYR LYS VAL ILE GLY GLU 165 170 175 VAL ARG ILE ALA PHE GLU THR ALA ARG ALA ALA ASP PRO ASN 180 185 190 LEU TYR ILE ASN ASP TYR ASN LEU ASP SER ALA SER TYR PRO 195 200 205 THR GLY MET VAL SER HIS VAL LYS LYS TRP ILE ALA ALA GLY 215 220 ILE ASP GLY ILE GLY SER GLN THR HIS LEU SER ALA ALA LEU 230 235 240 LEU ALA GLY ALA GLY THR LYS GLU ILE ALA VAL THR GLU LEU 245 250 255 ALA GLY ALA SER SER THR ASP TYR VAL GLU VAL VAL GLU ALA 260 265 270 ASN GLN PRO LYS CYS ILE GLY ILE THR VAL TRP GLY VAL ALA 275 280 285 ASP SER TRP ARG SER SER SER THR PRO LEU LEU PHE ASP SER 295 300 ASN PRO LYS PRO ALA TYR THR ALA ILE ALA ASN ALA LEU 310 315 237873 1433329 de 42 20225952036 CRISTIAN DANIEL BITTEL - 20225952036 Digitally signed by PORTALTRAM ITES - INPI Date: 2021.07.07 15:04:28 -03:00 Reason: Digitally Signed by the INPI Location: Buenos Aires, Argentina 1433329

Claims

1. A method for increasing the starch and / or gluten yield of corn kernels in a wet milling process, characterized in that it comprises the steps of: a) soaking the corn kernels in water to produce soaked kernels; b) milling the soaked kernels to produce ground kernels; c) separating the germs from the ground kernels to produce a mass of corn kernels comprising fiber, starch, and gluten; d) subjecting the resulting mass of corn kernels comprising fiber to a fiber washing procedure, so as to separate starch, gluten, and fiber;wherein the xylanase, the cellulase enzyme(s), and SO2 are present or added during step d), wherein SO2 is added during the fiber washing step (d) in amounts of 400 ppm - 1200 ppm, and wherein the xylanase is selected from a GH5 xylanase consisting of a polypeptide of SEQ ID NO: 1, and cellulases consisting of cellulases naturally produced from Trichoderma reesei, wherein said fiber washing process comprises the use of a fiber washing system comprising a space (V) / tank, and the incubation time in said space (V) / tank configured in the fiber washing system is between 45 minutes and 5 hours, and the incubation temperature is between 35 and 55°C. Five claims follow;