WO2026008449A2 - Procédé de production d'un produit de fermentation et d'un co-produit protéique concentré - Google Patents

Procédé de production d'un produit de fermentation et d'un co-produit protéique concentré

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Publication number
WO2026008449A2
WO2026008449A2 PCT/EP2025/068082 EP2025068082W WO2026008449A2 WO 2026008449 A2 WO2026008449 A2 WO 2026008449A2 EP 2025068082 W EP2025068082 W EP 2025068082W WO 2026008449 A2 WO2026008449 A2 WO 2026008449A2
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WIPO (PCT)
Prior art keywords
starch
alpha
amylase
produce
process according
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WO2026008449A3 (fr
Inventor
Mohan Bilekalahalli HUCHEGOWDA
Pandurang Shinde
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Novozymes AS
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Novozymes AS
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Publication of WO2026008449A3 publication Critical patent/WO2026008449A3/fr
Pending legal-status Critical Current
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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
    • C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic
    • C12P7/06—Ethanol, i.e. non-beverage
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
    • C12C7/00—Preparation of wort
    • C12C7/04—Preparation or treatment of the mash
    • C12C7/047—Preparation or treatment of the mash part of the mash being unmalted cereal mash
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
    • C12C7/00—Preparation of wort
    • C12C7/14—Lautering, i.e. clarifying wort
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/02—Monosaccharides
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01001—Alpha-amylase (3.2.1.1)

Definitions

  • the present invention relates to a process for producing a fermentation product and a concentrated protein co-product from a starch/fiber-containing material.
  • Ethanol has widespread application, including for use as a gasoline additive or as a straight liquid fuel.
  • Processes for producing fermentation products, such as ethanol, from a starch or lignocellulose containing material are well known in the art.
  • the preparation of the starch containing material such as corn or rice for utilization in such fermentation processes typically begins with grinding the corn in a dry-grind or wet-milling process.
  • Wet-milling processes involve fractionating the grain/kernels into different components where only the starch fraction enters the fermentation process.
  • Dry-grind processes involve grinding the grain/kernels into meal and mixing the meal with water and enzymes. Generally, two different kinds of dry-grind processes are used.
  • the most commonly used process includes grinding the starch-containing grain and then liquefying gelatinized starch at a high temperature using typically a bacterial alpha-amylase, followed by simultaneous saccharification and fermentation (SSF) carried out in the presence of a glucoamylase and a fermentation organism.
  • SSF simultaneous saccharification and fermentation
  • Another well-known process often referred to as a “raw starch hydrolysis” process (RSH process) includes grinding the starch-containing grain and then simultaneously saccharifying and fermenting granular starch below the initial gelatinization temperature typically in the presence of an acid fungal alphaamylase and a glucoamylase.
  • the liquid fermentation products are recovered from the fermented mash (often referred to as “beer mash”), e.g., by distillation, which separates the desired fermentation product, e.g. ethanol, from other liquids and/or solids.
  • the remaining fraction is referred to as “whole stillage”.
  • Whole stillage typically contains about 10 to 20% solids.
  • the whole stillage is separated into a solid and a liquid fraction, e.g., by centrifugation.
  • the separated solid fraction is referred to as “wet cake” (or “wet grains”) and the separated liquid fraction is referred to as “thin stillage”.
  • Wet cake and thin stillage contain about 30%-35% and 6-10% solids, respectively.
  • Wet cake, with optional additional dewatering is used as a component in animal feed or is dried to provide “Distillers Dried Grains” (DDG) used as a component in animal feed.
  • DDG Disillers Dried Grains
  • Thin stillage is typically evaporated to provide evaporator condensate and syrup or may alternatively be recycled to the slurry tank as “backset”. Evaporator condensate may either be forwarded to a methanator before being discharged and/or may be recycled to the slurry tank as “cook water”.
  • the syrup may be blended into DDG or added to the wet cake before or during the drying process, which can comprise one or more dryers in sequence, to produce DDGS (Distillers Dried Grain with Solubles).
  • Syrup typically contains about 25% to 35% solids. Oil can also be extracted from the thin stillage and/or syrup as a by-product for use in biodiesel production, as a feed or food additive or product, or other bio-renewable products.
  • WO 2010/138110 A1 is directed to a method for producing a high protein corn meal from a whole stillage byproduct produced in a corn dry-milling process for making ethanol and a system therefore.
  • the method therein includes separating the whole stillage byproduct into an insoluble solids portion and a thin stillage portion.
  • the thin stillage portion is separated into a protein portion and a water soluble solids portion.
  • the present invention relates to a process for producing a fermentation product and a concentrated protein co-product from a starch-containing material, comprising the steps of:
  • the present invention relates to a process for producing a fermentation product and a concentrated protein co-product from a starch-containing material, comprising the steps of:
  • FIG 1 shows the process of concentrated protein co-product.
  • Alpha-amylases (EC 3.2.1.1) are a group of enzymes which catalyze the hydrolysis of starch and other linear and branched 1 ,4 glucosidic oligo- and polysaccharides. The skilled person will know how to determine alpha-amylase activity. It may be determined, e.g., by measuring residual activity after stressing the sample at pH 4.0 using a commercial alpha-amylase activity assay kit, such as kits containing G7-pNP substrate and alpha-Glucosidase, e.g., manufactured by Roche/Hitachi (cat. No.11876473) or Sigma-Aldrich (Catalog number MAK009).
  • a commercial alpha-amylase activity assay kit such as kits containing G7-pNP substrate and alpha-Glucosidase, e.g., manufactured by Roche/Hitachi (cat. No.11876473) or Sigma-Aldrich (Catalog number MAK009).
  • Alpha-Amylase having raw starch activity means an alpha-amylase (EC 3.2.1.1) having activity against raw starch (non-gelatinized starch), and preferably comprising of Carbohydrate-Binding Module Family 20 or 26 (CBM20 or CBM26) (URL: http://www.cazy.org/Carbohydrate-Binding-Modules.html).
  • CBM20 or CBM26 Carbohydrate-Binding Module Family 20 or 26
  • Cellobiohydrolase/polypeptide with cellobiohydrolase activity 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-glucosidic linkages in cellulose, cellooligosaccharides, or any beta-1 ,4-linked glucose containing polymer, releasing cellobiose from the reducing end (cellobiohydrolase I) or non-reducing end (cellobiohydrolase II) of the chain (Teeri, 1997, Trends in Biotechnology 15: 160-167; Teeri et al., 1998, Biochem.
  • 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 etal., 1988, Eur. J. Biochem. 170: 575-581.
  • Cellulolytic enzyme or cellulase/polypeptide with cellulase activity or cellulolytic activity means one or more (e.g., several) enzymes that hydrolyze a cellulosic material, which comprise any material comprising cellulose, such as fiber.
  • Cellulytic 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 for measuring cellulolytic enzyme activity include: (1) measuring the total cellulolytic enzyme activity, and (2) measuring the 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 N°1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc.
  • the most common total cellulolytic activity assay is the filter paper assay using Whatman N°1 filter paper as the substrate. The 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 production/release of sugars during 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, e.g., 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, e.g., 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 addition of cellulolytic enzyme protein.
  • PCS pretreated corn stover
  • Typical conditions are 1 ml reactions, washed or unwashed PCS, 5% insoluble solids (dry weight), 50 mM sodium acetate pH 5, 1 mM MnSO4, 50°C, 55°C, or60°C, 72 hours, sugar analysis by AMINEX® HPX-87H column chromatography (Bio-Rad Laboratories, Inc., Hercules, CA, USA).
  • expression includes any step involved in the production of a polypeptide including, but not limited to, transcription, post- transcriptional modification, translation, post-translational modification, and secretion.
  • Expression vector means a linear or circular DNA molecule that comprises a polynucleotide encoding a polypeptide and is operably linked to control sequences that provide for its expression.
  • Endoglucanase means an endo-1 ,4-(1 ,3;1 ,4)- beta-D-glucan 4-glucanohydrolase (E.C. 3.2.1.4) that catalyzes endohydrolysis of 1 ,4- beta-D-glycosidic linkages in cellulose, cellulose derivatives (such as carboxymethyl cellulose and hydroxyethyl cellulose), lichenin, beta-1 ,4 bonds in mixed beta-1 ,3 glucans such as cereal beta-D-glucans or xyloglucans, and other plant material containing cellulosic components.
  • endoglucanase means an endo-1 ,4-(1 ,3;1 ,4)- beta-D-glucan 4-glucanohydrolase (E.C. 3.2.1.4) that catalyzes endohydrolysis of 1 ,4- beta-D-glycosidic linkages in cellulose, cellulose derivatives (such as carboxymethyl cellulose
  • Endoglucanase activity can be determined by measuring reduction in substrate viscosity or increase in reducing ends determined by a reducing sugar assay (Zhang et al., 2006, Biotechnology Advances 24: 452-481). For purposes of the present invention, endoglucanase activity is determined using carboxymethyl cellulose (CMC) as substrate according to the procedure of Ghose, 1987, Pure and Appl. Chem. 59: 257-268, at pH 5, 40°C.
  • Fragment means a polypeptide having one or more (e.g., several) amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide, wherein the fragment has pectin lyase activity.
  • Family 61 glycoside hydrolase The term “Family 61 glycoside hydrolase” or “Family GH61” or “GH61” means a polypeptide falling into the glycoside hydrolase Family 61 according to Henrissat, 1991 , A classification of glycosyl hydrolases based on amino-acid sequence similarities, Biochem. J. 280: 309-316, and Henrissat and Bairoch, 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 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 non-canonical and they cannot be considered as bona fide glycosidases. However, they are kept in the CAZy classification on the basis of their capacity to enhance the breakdown of lignocellulose when used in conjunction with a cellulase or a mixture of cellulases.
  • the 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. Q: 1399-1406; Lin et al., 2012, Structure 20: 1051-1061) and are designated “Auxiliary Activity 9” or “AA9” polypeptides.
  • Fermentation product means a product produced by a process including fermenting using a fermenting organism. Fermentation products include alcohols (e.g., ethanol, methanol, butanol); organic acids (e.g., citric acid, acetic acid, itaconic acid, lactic acid, succinic acid, gluconic acid); ketones (e.g., acetone); amino acids (e.g., glutamic acid); gases (e.g., H2 and CO2); antibiotics (e.g., penicillin and tetracycline); enzymes; vitamins (e.g., riboflavin, B12, beta-carotene); and hormones.
  • alcohols e.g., ethanol, methanol, butanol
  • organic acids e.g., citric acid, acetic acid, itaconic acid, lactic acid, succinic acid, gluconic acid
  • ketones e.g., acetone
  • amino acids e.g.
  • the fermentation product is ethanol, e.g., fuel ethanol; drinking ethanol, i.e., potable neutral spirits; or industrial ethanol or products used in the consumable alcohol industry (e.g., beer and wine), dairy industry (e.g., fermented dairy products), leather industry and tobacco industry.
  • Preferred beer types comprise ales, stouts, porters, lagers, bitters, malt liquors, happoushu, high-alcohol beer, low-alcohol beer, low-calorie beer or light beer.
  • the fermentation product is ethanol.
  • Fermenting organism refers to any organism, including bacterial and fungal organisms, especially yeast, suitable for use in a fermentation process and capable of producing the desired fermentation product.
  • Glucoamylase The term glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) is defined as an enzyme, which catalyzes the release of D-glucose from the non-reducing ends of starch or related oligo- and polysaccharide molecules.
  • GH5 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 5 in the database of Carbohydrate-Active EnZymes (CAZymes) (http://www.cazy.org/).
  • GH5_21 xylanase is an abbreviation for Glycoside Hydrolase Family 5 subfamily 21 endo-beta-1, 4-xylanases that possess a three- dimensional structure characterized by a (P / a) 8 barrel and use a glutamine residue as a catalytic nucleophile/base.
  • GH5_35 xylanase is an abbreviation for Glycoside Hydrolase Family 5 subfamily 35 endo-beta-1, 4-xylanases that possess a three- dimensional structure characterized by a ( / a) 8 barrel and use a glutamine residue as a catalytic nucleophile/base.
  • GH8 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 5 in the database of Carbohydrate-Active EnZymes (CAZymes) (http://www.cazy.org/).
  • GH30 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 30 in the database of Carbohydrate-Active EnZymes (CAZymes) (http://www.cazy.org/).
  • GH10 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 10 in the database of Carbohydrate-Active EnZymes (CAZymes) available at http://www.cazy.org/. (Lombard, V.; Golaconda Ramulu, H.; Drula, E.; Coutinho, P. M.; Henrissat, B. (21 November 2013). "The carbohydrate-active enzymes database (CAZy) 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 database (CAZy): an expert resource for Glycogenomics”. Nucleic Acids Res. 37 (Database issue): D233-8).
  • GH11 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 11 in the database of Carbohydrate-Active EnZymes (CAZymes).
  • GH62 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 62 in the database of Carbohydrate-Active EnZymes (CAZymes).
  • GH43 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 43 in the database of Carbohydrate-Active EnZymes (CAZymes).
  • GH51 polypeptide refers to a polypeptide with enzyme activity, the polypeptide being classified as member of the Glycoside hydrolase family 51 in the database of Carbohydrate-Active EnZymes (CAZymes).
  • Hydrolytic enzymes refers to any catalytic protein that use water to break down substrates. Hydrolytic enzymes include alpha-amylase (EC 3.2.1.1), glucoamylase (EC 3.2.1.3), cellulases (EC 3.2.1.4), xylanases (EC 3.2.1.8) arabinofuranosidases (EC 3.2.1.55 (Non-reducing end alpha-L-arabinofuranosidases); EC 3.2.1.185 (Nonreducing end beta-L-arabinofuranosidases) 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).
  • alpha-amylase EC 3.2.1.1
  • glucoamylase EC 3.2.1.3
  • cellulases EC 3.2.1.4
  • Raw Starch Material means primary starch- based grains, which has not been subjected to temperatures above the initial gelatination temperature for starch, e.g., non-gelatinized starch.
  • Starch means any material comprised of complex polysaccharides of plants, composed of glucose units that occurs widely in plant tissues in the form of storage granules, consisting of amylose and amylopectin, and represented as (CeH Osjn, where n is any number.
  • S8A protease means an S8 protease belonging to subfamily A. Subtilisins, EC 3.4.21.62, are a subgroup in subfamily S8A. The S8A protease hydrolyses the substrate Suc-Ala-Ala-Pro-Phe-pNA. The release of p- nitroaniline (pNA) results in an increase of absorbance at 405 nm and is proportional to the enzyme activity.
  • pNA p- nitroaniline
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
  • 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 EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:
  • 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 later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NLIC4.4) substitution matrix.
  • the output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:
  • Xylanases/polypeptide with xylanase activity means a 1 ,4-beta-D-xylan-xylohydrolase (E.C. 3.2.1.8) that catalyzes the endohydrolysis of 1 ,4-beta-D-xylosidic linkages in xylans.
  • Xylanase activity can be determined with 0.2% AZCL-arabinoxylan as substrate in 0.01% TRITON® X-100 and 200 mM sodium phosphate pH 6 at 37°C.
  • xylanases One unit of xylanase activity is defined as 1.0 pmole of azurine 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 in, e.g., the GH5, GH30, GH10, and GH11 families.
  • Thin Stillage refers to centrate separated from whole stillage that is pumped toward the evaporators to be concentrated into syrup.
  • Whole Stillage includes the material that remains at the end of the distillation process after recovery of the fermentation product, e.g., ethanol.
  • the process of the invention is particularly suitable for the conventional starch to ethanol industry, which is well-known in the art and relies on producing fermentation products, such as ethanol from gelatinized starch-containing material.
  • the starch containing material is typically dry-milled before the liquefaction step.
  • This type of process includes a liquefaction step and sequentially or simultaneously performed saccharification and fermentation steps.
  • the conventional process for producing fermentation products from starch-containing material therefore comprises the steps of:
  • step (b) saccharifying the liquefied material obtained in step (a) using a glucoamylase
  • the present invention combines the above process in the conventional space with a protein purification process, extraction protein from an insoluble fraction isolated after the liquefaction step and at the same time increases the overall ethanol yield.
  • the process of the present invention comprises at least one separation step performed after the liquefaction step, resulting in a liquid portion comprising soluble starch/oligosacchrides and an insoluble portion comprising solids from the liquefied mash, said insoluble portion undergoing a protein concentration process, and the liquid portion comprising soluble starch/oligosacchrides undergoing saccharification and fermentation to produce ethanol.
  • Dry milling processes are well-known in the art, and generally involve the step of grinding/milling whole cereal grains in a dry or substantially dry state.
  • the production of ethanol in accordance with a dry milling process generally includes the main process steps of grinding/milling whole cereal grains to produce a meal, and subjecting the meal to liquefaction, saccharification, fermentation, and optionally distillation to produce ethanol.
  • Whole corn grains are the preferred starting raw material for ethanol production; however, other cereal grains may also be used, including, for example, milo, wheat and barley.
  • Liquefaction is a process in which the long-chained starch is degraded into oligosaccharides. Liquefaction processes are well-known in the art and are usually performed by enzymatic or acid hydrolysis.
  • liquefaction is performed by treating the meal with an effective amount of an alpha-amylase.
  • Liquefaction is often carried out at a temperature of about 105 to 120°C. for about 5 to 15 minutes followed by a lower temperature holding period of about 1 to 3 hours at >85°C.
  • Saccharification is a process in which the oligosaccharides resulting from liquefaction are converted by hydrolysis to fermentable sugars.
  • the hydrolysis is preferably preformed enzymatically by addition of a glucoamylase, alone or in combination with other enzymes, such as alpha-glucosidase, acid alpha-amylase and/or pullulanase.
  • Saccharification processes are also well-known in the art.
  • a full saccharification process may be about 40-92 hours, and is often carried out at temperatures from about 30 to 60°C.
  • presaccharification step lasting for about 40 to 720 minutes, and then to do a complete saccharification process during fermentation in simultaneous saccharification and fermentation (SSF) or simultaneous liquefaction, saccharification, and fermentation (LSF).
  • SSF simultaneous saccharification and fermentation
  • LSF simultaneous liquefaction, saccharification, and fermentation
  • the invention relates to a process for producing fermentation products and a concentrated protein co-product from a starch-containing material, comprising the steps of:
  • step (d) fermenting the sugar with a fermenting organism to produce the fermentation product, wherein at least one separation step is performed after the liquefaction in step (a) resulting in a liquid portion comprising soluble starch/ oligosaccharides and an insoluble portion comprising solids from the liquefied mash, said insoluble portion undergoing said protein concentration process.
  • the protein extraction and concentration process preferably comprise several additional process steps, such as at least a liquefaction step, a saccharification step, and one or more separation steps as shown in Figure 1 . Therefore, in a second aspect the present invention relates to a process for producing a fermentation product and a concentrated protein co-product from a starch- containing material, comprising the steps of:
  • the process of the invention further comprises, prior to the step a), a steps of: reducing the particle size of the starch-containing material, and forming a slurry comprising the starch-containing material and water.
  • starch-containing material Any suitable starch-containing material may be used.
  • the material is selected based on the desired fermentation product.
  • starch-containing materials include without limitation, barley, cassava, millet, sorghum, oats, potatoes, rice, wheat, and maize, or any mixture thereof.
  • starch-containing material is rice.
  • the separation is done using centrifugation, filtration, decantation and/or cloth filtration.
  • the particle size is reduced to between 0.05 to 3.0 mm, preferably 0.1 -0.5 mm, or so that at least 30 percent, preferably at least 50 percent, more preferably at least 70 percent, even more preferably at least 90 percent of the starch-containing material fit through a sieve with a 0.05 to 3.0 mm screen, preferably 0.1 -0.5 mm screen.
  • the aqueous slurry may contain from 10-55 w/w- percent dry solids (DS), preferably 25- 45 w/w- percent dry solids (DS), more preferably 30-40 w/w- percent dry solids (DS) of starch-containing material.
  • the slurry is heated to above the gelatinization temperature and an alphaamylase may be added to initiate liquefaction (thinning).
  • the slurry may be heated to above the initial gelatinization temperature.
  • the slurry may optionally be jet-cooked to further gelatinize the starch in the slurry before adding alpha-amylase during liquefying step (a). Jet cooking can be performed at temperatures ranging from 100 °C to 120 °C for up to at least 15 minutes.
  • Liquefaction may in an embodiment be carried out as a three-step hot slurry process.
  • the slurry may be heated to between 60-105 degrees centigrade, at a pH of 4-6, and alpha-amylase, optionally together with a protease, a carbohydrate-source generating enzyme, such as a glucoamylase, a phospholipase, a phytase, and/or pullulanase, are added to initiate liquefaction (thinning).
  • the pH used during liquefying step (a) may range from 4 to 6, from 4.5 to 5.5, or from 4.8 to 5.2.
  • the pH is at least 4.5, at least 4.6, at least 4.7, at least 4.8, at least 4.9, at least 5.0, or at least 5.1.
  • the liquefaction for performing liquefying step (a) may range from 30 minutes to 5 hours, from 1 hour to 3 hours, or 90 minutes to 150 minutes.
  • the time is at least 30 minutes, at least about 45 minutes, at least about 60 minutes, at least about 90 minutes, or at least about 2 hours.
  • the temperature used during liquefying step (a) may range from 70°C to 110°C, such as from 75°C to 105°C, from 80°C to 100°C, from 85°C to 95°C, or from 88°C to 92°C.
  • the temperature is at least 70°C, at least 80°C, at least 85°C, at least 88°C, or at least 90°C.
  • Saccharification step (b) may be carried out using conditions well known in the art. For instance, a full saccharification process may last up to from about 40 to about 92 hours, however, it is common only to do a pre-saccharification of typically 40-720 minutes at a temperature between 30-65 degrees centigrade, typically about 60 degrees centigrade, followed by complete saccharification during fermentation in a simultaneous saccharification and fermentation process (SSF process). Saccharification is typically carried out at a temperature from 20-75 degrees centigrade, in particular 40-70 degrees centigrade, typically around 60 degrees centigrade, and at a pH between 4 and 5, normally at about pH 4.5.
  • SSF process simultaneous saccharification and fermentation process
  • SSF simultaneous saccharification and fermentation
  • a fermenting organism such as yeast
  • enzyme(s) may be added together.
  • SSF may typically be carried out at a temperature from 25 degrees centigrade to 40 degrees centigrade, such as from 28 degrees centigrade to 35 degrees centigrade, such as from 30 degrees centigrade to 34 degrees centigrade, preferably around about 32 degrees centigrade
  • fermentation is ongoing for 6 to 120 hours, in particular 24 to 96 hours.
  • Distillation is a process of separating ethanol from the fermented mash, preferably, by evaporation.
  • the vapours are preferably driven off by applying direct heat to the fermented mash.
  • the vapours are collected, condensed and recovered as a liquid and may be redistilled to increase the ethanol concentration. Because ethanol has a higher vapor pressure than water, the vaporization of water and ethanol results in a liquid higher in ethanol. Through condensation, a highly concentrate distillate is obtained. Normal distillation results in a liquid with a purity of about 95 volume-% ethanol (190 proof). For fuel ethanol, the final proof must approach 200. To accomplish this result, the ethanol may be subjected to further dehydration steps.
  • Stillage is a product which remains after mash has been converted to sugar, fermented and distilled into ethanol. Stillage can be separated into two fractions, such as, by centrifugation or screening: (1) wet grain (solid phase) and (2) the thin stillage (supernatant).
  • the solid fraction or distillers' wet grains (DWG) can be pressed to remove excess moisture and then dried to produce distillers' dried grains (DDG). After ethanol has been removed from the liquid fraction, the remaining liquid can be evaporated to concentrate the soluble material into condensed distillers' solubles (DS) or dried and ground to create distillers' dried solubles (DDS). DDS is often mixed with DDG to form distillers' dried grains with solubles (DDGS). DDG, DDGS, and DWG are collectively referred to as distillers' grains.
  • the concentrated protein coproduct recovery is above 50% w/w, such as 60% w/w, such as 70% w/w, such as 80% w/w.
  • the concentrate protein co-product purity is at least 65% w/w, at least 70% w/w, at least 75% w/w, at least 80% w/w, at least 85% w/w, such as at least 90% w/w.
  • thermostable enzymes during liquefying step (a). It is well known in the art to use various thermostable enzymes during liquefying step (a), including, for example, thermostable alpha-amylases, thermostable glucoamylases, thermostable endoglucanases, thermostable lipases, thermostable phytase, thermostable proteases, thermostable pullulanases, and/or thermostable xylanases.
  • the present invention contemplates the use of any thermostable enzyme in liquefying step (a).
  • the published patent applications listed below describe activity assays for determining whether a candidate thermostable enzyme contemplated for use in liquefying step (a) will be deactivated at a temperature contemplated for liquefying step (a).
  • thermostable alpha-amylases examples include, without limitation, the alpha-amylases described in WO94/18314, WO94/02597, WO 96/23873, WO 96/23874, WO 96/39528, WO 97/41213, WO 97/43424, WO 99/19467, WO 00/60059, WO 2002/010355, WO 2002/092797, WO 2009/149130, WO 2009/61378, WO 2009/061379, WO
  • Suitable commercially available alpha-amylases includes Liquozyme® LpH, Liquozyme® SC, Liquozyme® Supra, Fortiva® Edge Alpha, Spezyme® HT, Spezyme® Ethyl, Spezyme® Fred.
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 1 ;
  • the alpha-amylase added during liquefaction is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 2; c) a fragment of the polypeptide of (a) or (b); wherein the polypeptide has alphaamylase activity.
  • the alpha-amylase added during liquefaction is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 1 and SEQ ID NO: 2; c) a fragment of the polypeptide of (a) or (b); wherein the polypeptide has alphaamylase activity.
  • thermostable glucoamylases include, without limitation, the glucoamylases described in WO 2011/127802, WO 2013/036526, WO 2013/053801 , WO 2018/164737, WO 2020/010101 , and WO 2022/090564 (each of which is incorporated herein by reference).
  • thermostable endoglucanases examples include, without limitation, the endoglucanases described in WO 2015/035914 (which is incorporated herein by reference)
  • thermostable lipases examples include, without limitation, the lipases described in WO 2017/112542 and WO 2020/014407 (which are both incorporated herein by reference).
  • thermostable phytases include, without limitation, the phytases described in WO 1996/28567, WO 1997/33976, WO 1997/38096, WO 1997/48812, WO 1998/05785, WO 1998/06856, WO 1998/13480, WO 1998/20139, WO 1998/028408, WO 1999/48330, WO 1999/49022, WO 2003/066847, WO 2004/085638, WO 2006/037327, WO 2006/037328, WO 2006/038062, WO
  • phytase containing products include BIO-FEED PHYTASETM, PHYTASE NOVOTM CT or L, LIQMAX or RONOZYMETM NP, RONOZYME® HIPHOS, RONOZYME® P5000 (CT), NATUPHOSTM NG 5000.
  • thermostable proteases include, without limitation, the proteases described in WO 1992/02614, WO 98/56926, WO 2001/151620, WO 2003/048353, WO 2006/086792, WO 2010/008841 , WO 2011/076123, WO 2011/087836, WO 2012/088303, WO 2013/082486, WO 2014/209789, WO 2014/209800, WO 2018/098124, WO2018/118815 A1 , and WO2018/169780A1 (each of which is incorporated herein by reference).
  • Suitable commercially available protease containing products include AVANTEC AMP®, FORTIVA REVO®, FORTIVA HEM I®.
  • thermostable pullulanases include, without limitation, the pullulanases described in WO 2015/007639, WO 2015/110473, WO 2016/087327, WO 2017/014974, and WO 2020/187883 (each of which is incorporated herein by reference in its entirety).
  • Suitable commercially available pullulanase products include PROMOZYME 400L, PROMOZYMETM D2 (Novozymes A/S, Denmark), OPTIMAX L- 300 (Genencor Int. , USA), and AMANO 8 (Amano, Japan).
  • thermostable xylanases examples include, without limitation, the xylanases described in WO 2017/112540 and WO 2021/126966 (each of which is incorporated herein by reference).
  • Suitable commercially available thermostable xylanase containing products include FORTIVA HEMI®.
  • the enzyme(s) described above are to be used in effective amounts in the processes of the present invention.
  • Guidance for determining effective amounts of enzymes to be used in liquefying step (a) can be found in the published patent applications cited for each of the different thermostable liquefaction enzymes, along with guidance for performing activity assays for determining the activity of those enzymes.
  • saccharification may be performed at temperatures ranging from 20 °C to 75 °C, from 30 °C to 70 °C, or from 40 °C to 65 °C.
  • the saccharification temperature is at least about 50 °C, at least about 55 °C, or at least about 60 °C.
  • saccharification may occur at a pH ranging from 4 to 5.
  • the pH is about 4.5.
  • saccharification may last from about 24 hours to about 72 hours.
  • fermentation may last from 6 to 120 hours, from 24 hours to 96 hours, or from 35 hours to 60 hours.
  • Simultaneous Saccharification and Fermentation may be performed at a temperature from 25 °C to 40 °C, from 28 °C to 35 °C, or from 30 °C to °C, at a pH from 3.5 to 5 or from 3.8 to 4.3., for 24 to 96 hours, 36 to 72 hours, or from 48 to 60 hours.
  • SSF is performed at about 32 °C, at a pH from 3.8 to 4.5 for from 48 to 60 hours.
  • the present invention contemplates the use of enzymes during saccharifying step and/or fermenting step.
  • alpha-amylases alpha-glucosidases, beta-amylases, beta-glucanases, beta-glucosidases, cellobiohydrolases, endoglucanases, glucoamylases, lipases, lytic polysaccharide monooxygenases (LPMOs), maltogenic alpha-amylases, pectinases, peroxidases, phytases, proteases, and trehalases.
  • LPMOs lytic polysaccharide monooxygenases
  • the enzymes used in saccharifying step and/or fermenting step may be added exogenously as mono-components or formulated as compositions comprising the enzymes.
  • the enzymes used in saccharifying step and/or fermenting step may also be added via in situ expression from the fermenting organism (e.g., yeast).
  • alpha-amylases include, without limitation, the alphaamylases described in WO 2004/055178, WO 2006/069290, WO 2013/006756, WO 2013/034106, WO 2013/044867, WO 2021/163011 , and WO 2021/163030 (each of which is incorporated herein by reference).
  • glucoamylases include, without limitation, the glucoamylases described in WO 1984/02921 , WO 1992/00381 , WO 1999/28448, WO 2000/04136, WO 2001/04273, WO 2006/069289, WO 2011/066560, WO 2011/066576, WO 2011/068803, WO 2011/127802, WO 2012/064351 , WO
  • compositions comprising alpha-amylases and glucoamylases include, without limitation, the compositions described in WO 2006/069290, WO 2009/052101 , WO 2011/068803, and WO 2013/006756 (each of which is incorporated by reference herein).
  • compositions comprising glucoamylase include AMG 200L; AMG 300 L; SANTM SUPER, SANTM EXTRA L, SPIRIZYMETM PLUS, SPIRIZYMETM FUEL, SPIRIZYMETM B4U, SPIRIZYMETM ULTRA, SPIRIZYMETM EXCEL, SPIRIZYME ACHIEVE and AMGTM E (from Novozymes A/S); OPTIDEXTM 300, GC480, GC417 (from DuPont-Genencor); AMIGASETM and AMIGASETM PLUS (from DSM); G-ZYMETM G900, G-ZYMETM and G990 ZR (from DuPont-Genencor).
  • beta-glucanases examples include, without limitation, the beta- glucanases described in WO 2021/055395 (which is incorporated herein by reference).
  • beta-glucosidases include, without limitation, the betaglucosidases described in WO 2005/047499, WO 2013/148993, WO 2014/085439 and WO 2012/044915 (each of which is incorporated herein by reference).
  • suitable cellobiohydrolases include, without limitation, the cellobiohydrolases described in WO 2013/148993, WO 2014/085439, WO 2014/138672, and WO 2016/040265 (each of which is incorporated herein by reference).
  • endoglucanases include, without limitation, the endoglucanases described in WO 2013/148993 and WO 2014/085439 (both of which are incorporated herein by reference).
  • lipases examples include, without limitation, the lipases described in WO 2017/112533, WO 2017/112539, and WO 2020/076697 (each of which is incorporated herein by reference).
  • Suitable LPMOs include, without limitation, the LPMOs described in WO 2013/148993, WO 2014/085439, and WO 2019/083831 (each of which is incorporated herein by reference).
  • Suitable phytases include, without limitation, the phytases described in WO 2001/62947 (which is incorporated herein by reference).
  • pectinases examples include, without limitation, the pectinases described in WO 2022/173694 (which is incorporated herein by reference).
  • Suitable peroxidases include, without limitation, the peroxidases described in WO 2019/231944 (which is incorporated herein by reference).
  • proteases examples include, without limitation, the proteases described in WO 2017/050291 , WO 2017/148389, WO 2018/015303, and WO 2018/015304 (each of which is incorporated herein by reference).
  • trehalases examples include, without limitation, the trehalases described in WO 2016/205127, WO 2019/005755, WO 2019/030165, and WO 2020/023411 (each of which is incorporated herein by reference).
  • the alpha-amylase is of fungal or bacterial origin.
  • the alpha-amylase is a fungal acid stable alphaamylase.
  • a fungal acid stable alpha-amylase is an alpha-amylase that has activity in the pH range of 3.0 to 7.0 and preferably in the pH range from 3.5 to 6.5, including activity at a pH of about 4.0, 4.5, 5.0, 5.5, and 6.0.
  • the alpha-amylase is present and/or added in saccharification and/or fermentation is derived from a strain of the genus Rhizomucor, preferably a strain the Rhizomucor pusillus, such as one shown in SEQ ID NO: 3 in WO 2013/006756, such as a Rhizomucor pusillus alpha-amylase hybrid having an Aspergillus niger linker and starch-binding domain, such as the one shown in SEQ ID NO: 3 herein, or a variant thereof.
  • a strain of the genus Rhizomucor preferably a strain the Rhizomucor pusillus, such as one shown in SEQ ID NO: 3 in WO 2013/006756, such as a Rhizomucor pusillus alpha-amylase hybrid having an Aspergillus niger linker and starch-binding domain, such as the one shown in SEQ ID NO: 3 herein, or a variant thereof.
  • the alpha-amylase is an acid stable amylase of fungal origin, preferably from a stain of Aspergillus, preferably A. niger, A. awamori, or A. oryzae or a strain of Rhizomucor, preferably Rhizomucor pusilus.
  • the alpha-amylase is of bacterial origin. E.g., derived from a strain of Bacillus sp.
  • the alpha-amylase comprises a CBM20 or CBM26.
  • the alpha-amylase catalytic domain is derived from Rhizomucor, such as a strain of Rhizomucor pusillus, such as the one comprised in in SEQ ID NO: 3 herein, and optionally comprising the substitutions G128D + D143N using SEQ ID NO: 3 for numbering.
  • the glucoamylase used in saccharification or simultaneous saccharification and fermentation is of fungal origin, preferably from a stain of Aspergillus, preferably A. niger, A. awamori, or A. oryzae or a strain of Trichoderma, preferably T. reeser, or a strain of Talaromyces, preferably T. emersonii or a strain of Trametes, preferably T. cingulata, or a strain of Pycnoporus, preferable P. sanguineus, or a strain of Gloeophyllum, such as G. sepiarium or G. trabeum, or a strain of the Nigrofomes.
  • SSF simultaneous saccharification and fermentation
  • the glucoamylase is derived from Gloeophyllum, such as a strain of Gloeophyllum sepiarium, such as the one shown in SEQ ID NO: 4.
  • a glucoamylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 4;
  • a glucoamylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 4; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has glucoamylase activity.
  • Glucoamylases may in an embodiment be added to the saccharification and/or fermentation in an amount of 0.0001-20 AGU/g DS, preferably 0.001-10 AGU/g DS, especially between 0.01-5 AGU/g DS, such as 0.1-2 AGU/g DS.
  • compositions comprising glucoamylase include AMG 200L; AMG 300 L; SANTM SUPER, SANTM EXTRA L, SPIRIZYMETM PLUS, SPIRIZYMETM FUEL, SPIRIZYMETM B4U, SPIRIZYMETM ULTRA, SPIRIZYMETM EXCEL and AMGTM E (from Novozymes A/S); OPTIDEXTM 300, GC480, GC417 (from DuPont.); AMIGASETM and AMIGASETM PLUS (from DSM); G-ZYMETM G900, G- ZYMETM and G990 ZR (from DuPont).
  • thermostable protease may be optionally present and/or added during liquefaction together with an alpha-amylase, such as a thermostable alpha-amylase, and optionally a carbohydrate-source generating enzyme, in particular a thermostable glucoamylase, and/or optionally a pullulanase.
  • an alpha-amylase such as a thermostable alpha-amylase
  • a carbohydrate-source generating enzyme in particular a thermostable glucoamylase, and/or optionally a pullulanase.
  • Proteases are classified on the basis of their catalytic mechanism into the following groups: Serine proteases (S), Cysteine proteases (C), Aspartic proteases (A), Metallo proteases (M), and Unknown, or as yet unclassified, proteases (U), see Handbook of Proteolytic Enzymes, A. J. Barrett, N.D. Rawlings, J. F. Woessner (eds), Academic Press (1998), in particular the general introduction part.
  • S Serine proteases
  • C Cysteine proteases
  • A Aspartic proteases
  • M Metallo proteases
  • U Unknown, or as yet unclassified, proteases
  • thermostable protease used according to the invention is a “metallo protease” defined as a protease belonging to EC 3.4.24 (metalloendopeptidases); preferably EC 3.4.24.39 (acid metallo proteinases).
  • protease is a metallo protease or not
  • determination can be carried out for all types of proteases, be it naturally occurring or wild-type proteases; or genetically engineered or synthetic proteases.
  • Protease activity can be measured using any suitable assay, in which a substrate is employed, that includes peptide bonds relevant for the specificity of the protease in question.
  • Assay-pH and assay-temperature are likewise to be adapted to the protease in question. Examples of assay-pH-values are pH 6, 7, 8, 9, 10, or 11. Examples of assay-temperatures are 30, 35, 37, 40, 45, 50, 55, 60, 65, 70 or 80°C.
  • thermostable protease has at least 20%, such as at least 30%, such as at least 40%, such as at least 50%, such as at least 60%, such as at least 70%, such as at least 80%, such as at least 90%, such as at least 95%, such as at least 100% of the protease activity of the Protease 196 variant or Protease Pfu determined by the AZCL-casein assay.
  • the protease is of fungal origin.
  • the protease may be a variant of, e.g., a wild-type protease as long as the protease has the thermostability properties defined herein.
  • the thermostable protease is a variant of a metallo protease as defined above.
  • thermostable protease used in a process of the invention is of fungal origin, such as a fungal metallo protease, such as a fungal metallo protease derived from a strain of the genus Thermoascus, preferably a strain of Thermoascus aurantiacus, especially Thermoascus aurantiacus CGMCC No. 0670 (classified as EC 3.4.24.39).
  • thermostable protease may also be derived from any bacterium as long as the protease has the thermostability properties defined according to the invention.
  • thermostable protease is derived from a strain of the bacterium Pyrococcus, such as a strain of Pyrococcus furiosus (pfu protease). Fermenting Organisms
  • Suitable fermenting organisms able to ferment i.e., convert, sugars, such as arabinose, glucose, maltose, and/or xylose, directly or indirectly into the desired fermentation product, such as ethanol.
  • fermenting organisms include fungal organisms, such as yeast.
  • Preferred yeast includes strains of Saccharomyces spp., in particular, Saccharomyces cerevisiae.
  • yeast examples include, e.g., RED STARTM and ETHANOL REDTM yeast (available from Fermentis/Lesaffre, USA), FALI (available from Fleischmann’s Yeast, USA), SUPERSTART and THERMOSACCTM fresh yeast (available from Ethanol Technology, Wl, USA), BIOFERM AFT and XR (available from NABC - North American Bioproducts Corporation, GA, USA), GERT STRAND (available from Gert Strand AB, Sweden), FERMIOL (available from DSM Specialties) and Innova® Achieve® D; Innova® Apex; Innova® Excel T; Innova® PT; Innova® Force; Innova® Ultra-L (available from Novozymes, Denmark).
  • RED STARTM and ETHANOL REDTM yeast available from Fermentis/Lesaffre, USA
  • FALI available from Fleischmann’s Yeast, USA
  • SUPERSTART and THERMOSACCTM fresh yeast available from Ethanol Technology, Wl, USA
  • yeast strains are available from biological depositories such as the American Type Culture Collection (ATCC) or the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ), such as, e.g., BY4741 (e.g., ATCC 201388); Y108-1 (ATCC PTA.10567) and NRRL YB-1952 (ARS Culture Collection). Still other S.
  • ATCC American Type Culture Collection
  • DSMZ Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH
  • BY4741 e.g., ATCC 201388
  • Y108-1 ATCC PTA.10567
  • NRRL YB-1952 NRRL YB-1952
  • a “derivative” of strain is derived from a referenced strain, such as through mutagenesis, recombinant DNA technology, mating, cell fusion, or cytoduction between yeast strains.
  • a referenced strain such as through mutagenesis, recombinant DNA technology, mating, cell fusion, or cytoduction between yeast strains.
  • the genetic alterations including metabolic modifications exemplified herein, may be described with reference to a suitable host organism and their corresponding metabolic reactions or a suitable source organism for desired genetic material such as genes for a desired metabolic pathway.
  • those skilled in the art can apply the teachings and guidance provided herein to other organisms.
  • the metabolic alterations exemplified herein can readily be applied to other species by incorporating the same or analogous encoding nucleic acid from species other than the referenced species.
  • the fermenting organism may be Saccharomyces strain, e.g., Saccharomyces cerevisiae strain produced using the method described and concerned in US patent no. 8,257,959-BB.
  • the recombinant cell is a derivative of a strain Saccharomyces cerevisiae CIBTS1260 (deposited under Accession No. NRRL Y- 50973 at the Agricultural Research Service Culture Collection (NRRL), Illinois 61604 U.S.A.).
  • the fermenting organism may also be a derivative of Saccharomyces cerevisiae strain NMI V14/004037 (See, WO2015/143324 and WO2015/143317 each incorporated herein by reference), strain nos. V15/004035, V15/004036, and V15/004037 (See, WO 2016/153924 incorporated herein by reference), strain nos. V15/001459, V15/001460, V15/001461 (See, WO2016/138437 incorporated herein by reference), strain no. NRRL Y67342 (See, WO2018/098381 incorporated herein by reference), strain nos. NRRL Y67549 and NRRL Y67700 (See, WO 2019/161227 incorporated herein by reference), or any strain described in WO2017/087330 (incorporated herein by reference).
  • the fermenting organisms may comprise one or more heterologous polynucleotides encoding an alpha-amylase, glucoamylase, protease and/or cellulase.
  • alpha-amylase, glucoamylase, protease and cellulases suitable for expression in the fermenting organism are known in the art (See, WO2021/231623 incorporated herein by reference).
  • the fermenting organism may be in the form of a composition comprising a fermenting organism and a naturally occurring and/or a non-naturally occurring component.
  • the fermenting organism may be in any viable form, including crumbled, dry, including active dry and instant, compressed, cream (liquid) form etc.
  • the fermenting organism e.g., a Saccharomyces cerevisiae yeast strain
  • the fermenting organism is dry yeast, such as active dry yeast or instant yeast.
  • the fermenting organism is crumbled yeast.
  • the fermenting organism is a compressed yeast.
  • the fermenting organism is cream yeast.
  • a process comprising a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain), and one or more of the components selected from the group consisting of: surfactants, emulsifiers, gums, swelling agent, and antioxidants and other processing aids.
  • a fermenting organism described herein e.g., a Saccharomyces cerevisiae yeast strain
  • the process described herein may comprise a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain) and any suitable surfactants.
  • the surfactant(s) is/are an anionic surfactant, cationic surfactant, and/or nonionic surfactant.
  • the process described herein may comprise a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain) and any suitable emulsifier.
  • the emulsifier is a fatty-acid ester of sorbitan.
  • the emulsifier is selected from the group of sorbitan monostearate (SMS), citric acid esters of monodiglycerides, polyglycerolester, fatty acid esters of propylene glycol.
  • the process comprises a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain), and Olindronal SMS, Olindronal SK, or Olindronal SPL including composition concerned in European Patent No. 1 ,724,336 (hereby incorporated by reference). These products are commercially available from Bussetti, Austria, for active dry yeast.
  • a fermenting organism described herein e.g., a Saccharomyces cerevisiae yeast strain
  • Olindronal SMS, Olindronal SK, or Olindronal SPL including composition concerned in European Patent No. 1 ,724,336 (hereby incorporated by reference).
  • the process described herein may comprise a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain) and any suitable gum.
  • the gum is selected from the group of carob, guar, tragacanth, arabic, xanthan and acacia gum, in particular for cream, compressed and dry yeast.
  • the process described herein may comprise a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain) and any suitable swelling agent.
  • the swelling agent is methyl cellulose or carboxymethyl cellulose.
  • the process described herein may comprise a fermenting organism described herein (e.g., a Saccharomyces cerevisiae yeast strain) and any suitable anti-oxidant.
  • the antioxidant is butylated hydroxyanisol (BHA) and/or butylated hydroxytoluene (BHT), or ascorbic acid (vitamin C), particular for active dry yeast.
  • Suitable concentrations of the viable fermenting organism during fermentation are well known in the art or can easily be determined by the skilled person in the art.
  • the fermenting organism such as ethanol fermenting yeast, (e.g., Saccharomyces cerevisiae) is added to the fermentation medium so that the viable fermenting organism, such as yeast, count per mL of fermentation medium is in the range from 105 to 1012, preferably from 107 to 1010, especially about 5x107. Fermentation Products
  • Fermentation product means a product produced by a process including a fermentation step using a fermenting organism.
  • Fermentation products contemplated according to the invention include alcohols (e.g., ethanol, methanol, butanol; polyols such as glycerol, sorbitol and inositol); organic acids (e.g., citric acid, acetic acid, itaconic acid, lactic acid, succinic acid, gluconic acid); ketones (e.g., acetone); amino acids (e.g., glutamic acid); gases (e.g., H2 and CO2); antibiotics (e.g., penicillin and tetracycline); enzymes; vitamins (e.g., riboflavin, B12, beta-carotene); and hormones.
  • alcohols e.g., ethanol, methanol, butanol
  • polyols such as glycerol, sorbitol and inosito
  • the fermentation product is ethanol, e.g., fuel ethanol; drinking ethanol, i.e., potable neutral spirits; or industrial ethanol or products used in the consumable alcohol industry (e.g., beer and wine), dairy industry (e.g., fermented dairy products), leather industry and tobacco industry.
  • Preferred beer types comprise ales, stouts, porters, lagers, bitters, malt liquors, happoushu, high-alcohol beer, low-alcohol beer, low-calorie beer or light beer.
  • processes of the invention are used for producing an alcohol, such as ethanol.
  • the fermentation product, such as ethanol, obtained according to the invention may be used as fuel, which is typically blended with gasoline. However, in the case of ethanol it may also be used as potable ethanol.
  • the fermentation product may be separated from the fermentation medium.
  • the slurry may be distilled to extract the desired fermentation product (e.g., ethanol).
  • the desired fermentation product may be extracted from the fermentation medium by micro or membrane filtration techniques.
  • the fermentation product may also be recovered by stripping or other method well known in the art.
  • the wet cake containing about 25-45 wt-%, preferably 30-38 wt-% dry solids, can be dried using methods such as a drum dryer, spray dryer, ring drier, fluid bed drier.
  • the drying process produces “Protein Concentrate” (PC) a valuable feed ingredient for human consumption, and animals, such as livestock, poultry and fish.
  • PC Protein Concentrate
  • Paragraph 1 A process for producing a fermentation product and a concentrated protein co-product from a starch-containing material, comprising the steps of:
  • step (d) fermenting the sugar with a fermenting organism to produce the fermentation product, wherein at least one separation step is performed after the liquefaction in step
  • Paragraph 2 A process for producing a fermentation product and a concentrated protein co-product from a starch-containing material, comprising the steps of:
  • Paragraph 3 The process according to any one of the preceding paragraph, wherein the starch containing material is selected from group consisting of rice, wheat, maize, millet, sorghum, oats, barely, potatoes and casava.
  • Paragraph 4 The process according to paragraph 3, wherein the starch- containing material comprises rice.
  • Paragraph 5 The process according to any of the preceding paragraphs, wherein the starch containing material is obtained from a dry-milling process.
  • Paragraph 6 The process according to any of the preceding paragraphs, wherein the concentrated protein coproduct recovery is above 50% w/w, such as 60% w/w, such as 70% w/w, such as 80% w/w.
  • Paragraph 7 The process according to any of the preceding paragraphs, wherein the concentrate protein co-product purity is at least 65% w/w, at least 70% w/w, at least 75% w/w, at least 80% w/w, at least 85% w/w, such as at least 90% w/w.
  • Paragraph 8 The process according to paragraph 1 , wherein saccharification in step (c) and fermentation in step (d) is carried out sequentially or simultaneously.
  • Paragraph 9 The process according to paragraph 2, wherein saccharification in step (h) and fermentation in step (i) is carried out sequentially or simultaneously.
  • Paragraph 10 The process according to any of the preceding paragraphs, wherein the pH during liquefaction is between above 5.0-6.5, such as above 5.0-6.0, such as above 5.0-5.5, such as between 5.2-6.2, such as around 5.2, such as around 5.4, such as around 5.6, such as around 5.8.
  • Paragraph 11 The process according to any of the preceding paragraphs, wherein the temperature during liquefaction is in the range from 70-100°C, such as between 75-95°C, such as between 75-90°C, preferably between 80-90°C, such as around 85°C.
  • Paragraph 12 The process according to any of the preceding paragraphs, wherein the saccharification step is carried out at pH values between 4.0 and 6.0.
  • Paragraph 13 The process according to any of the preceding paragraphs, wherein saccharification is carried out at a temperature from 20-75°C, preferably from 40-70°C, such as around 60°C.
  • Paragraph 14 The process according to any of the preceding paragraphs, wherein the fermentation product is recovered after fermentation, such as by distillation.
  • Paragraph 15 The process according to any of the preceding paragraphs, wherein the fermentation product is an alcohol, preferably ethanol, especially fuel ethanol, potable ethanol and/or industrial ethanol.
  • the fermentation product is an alcohol, preferably ethanol, especially fuel ethanol, potable ethanol and/or industrial ethanol.
  • Paragraph 16 The process according to any of the preceding paragraphs, wherein the fermenting organism is yeast, preferably a strain of Saccharomyces, especially a strain of Saccharomyces cerevisae.
  • Paragraph 17 The process according to any of the preceding paragraphs, further wherein a pullulanase is present or added during saccharification.
  • Paragraph 18 The process according to any of the preceding paragraphs, further wherein a glucoamylase is present or added during saccharification.
  • Paragraph 19 The process according to any of the preceding paragraphs, further wherein a protease is present or added during liquefaction.
  • Paragraph 20 The process according to any of the preceding paragraphs, wherein the alpha amylase is of bacterial or fungal origin.
  • Paragraph 21 The process according to any of preceding paragraphs, wherein the alpha amylase in step (a) is derived from Bacillus amyloliquefaciens or Bacillus stearothermophilus.
  • Paragraph 22 The process according any of preceding paragraphs, wherein the alpha amylase added during saccharification is derived from a group consisting of Aspergillus niger, Aspergillus terreus, Meripilus giganteus, Rhizomucor pusillus and combination thereof.
  • Paragraph 23 The process according to any of preceding paragraphs, wherein the alpha amylase applied in saccharification is derived from a group consisting of Aspergillus niger, Aspergillus terreus, Meripilus giganteus, Rhizomucor pusillus and combination thereof.
  • glucoamylase is of fungal origin, preferably from a strain of Aspergillus, preferably A. niger, Aspergillus fumigatus, A. awamori, or A. oryzae or a strain of Trichoderma, preferably T. reeser, or a strain of Talaromyces, preferably T. emersonii or a strain of Trametes, preferably T. cingulata, or a strain of Pycnoporus, or a strain of Gloeophyllum, such as G. serpiarium or G. trabeum, or a strain of the Nigrofomes, Penicillium oxalicum or Humicloa insolens.
  • a strain of Aspergillus preferably A. niger, Aspergillus fumigatus, A. awamori, or A. oryzae or a strain of Trichoderma, preferably T. reeser, or
  • Paragraph 25 The process according to paragraph 17, wherein the pullulanase is derived from Bacillus deramificans or Bacillus acidopullulyticus.
  • Paragraph 26 The process according to paragraph 19, wherein the protease is a variant of a metallo protease derived from a strain of the genus Thermoascus, preferably a strain of Thermoascus aurantiacus, especially Thermoascus aurantiacus CGMCC No. 0670.
  • Paragraph 27 The process according to claim 19, wherein the protease is derived from a strain of Pyrococcus, preferably a strain of Pyrococcus furiosus.
  • Paragraph 28 The process of any one of preceding paragraphs, wherein the fermentation product is ethanol.
  • Paragraph 29 The process of any one of preceding paragraphs, wherein the fermenting organism is yeast.
  • Paragraph 30 The process of any one of preceding paragraphs, wherein separation is done using centrifugation, filtration, decantation and/or cloth filtration.
  • Paragraph 31 The process of any one of preceding paragraphs, wherein the alpha-amylase added during liquefaction is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 1 ; c) a fragment of the polypeptide of (a) or (b); wherein the polypeptide has alphaamylase activity.
  • Paragraph 32 The process of any one of preceding paragraphs, wherein the alpha-amylase added during liquefaction is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 2;
  • Paragraph 33 The process of any one of preceding paragraphs, wherein the alpha-amylase added during liquefaction is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 1 and SEQ ID NO: 2; c) a fragment of the polypeptide of (a) or (b); wherein the polypeptide has alphaamylase activity.
  • Paragraph 34 The process of any one of preceding paragraphs, wherein the alpha-amylase added during saccharification is selected from the group consisting of:
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 3;
  • an alpha-amylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 3; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has alpha-amylase activity.
  • Paragraph 35 The process of any one of preceding paragraphs, wherein the glucoamylase added during saccharification is selected from the group consisting of:
  • a glucoamylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 4;
  • a glucoamylase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 4; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has glucoamylase activity.
  • Paragraph 36 The process of any one of preceding paragraphs, wherein the pullulanase added in saccharification step (d) is selected from the group consisting of:
  • a pullulanase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 5;
  • a pullulanase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 5; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has pullulanas
  • Paragraph 37 The process of any one of preceding paragraphs, wherein the lysophospholipase added in saccharification step (d) is selected from the group consisting of:
  • a xylanase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 7;
  • a xylanase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 7; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has xylanase activity.
  • Paragraph 38 The process of any one of preceding paragraphs, wherein the lysophospholipase added in saccharification step (d) is selected from the group consisting of:
  • a lysophospholipase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to the polypeptide of SEQ ID NO: 6;
  • a lysophospholipase comprising an amino acid sequence having at least 60%, at least 70%, e.g., at least 75%, at least 80%, at least 85%, 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%, or at least 99% identity to amino acids 1-556 of SEQ ID NO: 6; d) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has lysophospholipase activity.
  • Paragraph 39 The process of any one of preceding paragraphs, wherein the cellulase composition produced from Trichoderma reesei is added during saccharification.
  • Paragraph 40 The process according to paragraph 2, further comprises of addition of protease before step (g).
  • Paragraph 41 A fermentation product and a concentrated protein co-product produced by a process as claimed in paragraphs 1-40.
  • Paragraph 42 The process according to paragraph 41 , wherein the fermentation product is an alcohol, an organic acid, a ketone, an amino acid, or a gas.
  • Paragraph 43 The process according to paragraph 42, wherein the alcohol is ethanol.
  • Paragraph 44 The process according to paragraph 43, wherein the protein coproduct us used in feed, food and/or beverage industry.
  • Alpha-Amylase composition added during liquefaction comprising of an alphaamylase shown in as SEQ ID NO: 1 and an alpha-amylase shown in as SEQ ID NO: 2 herein.
  • Experimental saccharification composition added during saccharification step (d) comprising of alpha-amylase as shown in SEQ ID NO: 3 herein, glucoamylase as shown in as SEQ ID NO: 4 herein, pullulanase as shown in as SEQ ID NO: 5 herein, lysophospholipase as shown in as SEQ ID NO: 6 herein and xylanase as shown in as SEQ ID NO: 7 herein.
  • Example 1 Rice protein concentrate
  • First Liquefaction has two steps: first is Jet cooking A and then Liquefaction A. Once the rice slurry was prepared, the initial 30% of alpha amylase (0.3 Kg/ TDS) was added before jet cooking A at 110 °C for 10 minutes. Then, the remaining 70% of alpha-amylase (alpha-amylase composition was added at 0.7 Kg/ TDS) was added before liquefaction A, which was incubated at 95 °C for 3.5 hours with constant mixing.
  • Wet Cake Slurry Preparation Wet cake was transferred to the slurry preparation tank, and a 16% dry solids (DS) slurry was prepared by adjusting the slurry pH to 5.8 and conductivity to be greater than 400 microsiemens.
  • Second Liquefaction Second Liquefaction has two steps: first was Jet cooking B and then Liquefaction B. Once the 16% DS slurry was prepared, alpha-amylase (alpha-amylase composition was added at 1.5 Kg/ T DS) was added before jet cooking B at 110 °C for 10 minutes. Then, another dosage of alpha-amylase (alpha-amylase composition was added at 1 .5 Kg/ T DS) was added before liquefaction B, which was incubated at 95 °C for 2 hours with constant mixing.
  • Saccharification After second Liquefaction, the liquefied slurry is cooled to 55 °C. Then, glucoamylase, alpha-amylase, pullulanase, lysophospholipase, cellulase, xylanase, arabinofuranisidase, and/or hemicellualse (Experimental saccharification composition added during saccharification comprising of alpha-amylase as shown in SEQ ID NO: 3 herein, glucoamylase as shown in as SEQ ID NO: 4 herein, pullulanase as shown in as SEQ ID NO: 5 herein, lysophospholipase as shown in as SEQ ID NO: 6 herein and xylanase as shown in as SEQ ID NO: 7 herein and supplemented with cellulases from T. reeser, each at a dosage of 1 .5 Kg/ TDS), are added and incubated for 18 hours at 55
  • washing After cloth filtration, the wet cake was further washed with hot water at 70 °C using a ratio of 1 :1.4, meaning that for every portion of wet cake, 1.4 portion of water are added. This process involves constant mixing for 30 minutes to remove sugars bound to protein molecules and further concentrate the protein content.
  • Protein-rich rice wet cake was then transferred to a dryer and dried at 50°C, achieving a protein purity of 85%.
  • PROTEIN MASS BALANCE Protein extraction efficiency was calculated based on the initial protein quantity in the starting raw material rice and compared with the final protein quantity. Protein extraction efficiency was found to be in the range of 86 to 87% in all three different variety of Rice. 2. FERMENTATION Across three different varieties of Rice (Calrose Rice, Grod Ris and Parboiled Ris) more than 83% protein purity has been achieved using our enzyme application, with >86% recovery. Calrose Rice showed highest protein purity of 90.47% on dry basis as compared with Grod Ris (88.29%) and Parboiled Ris (83.22%). Overall ethanol yield >15.14 %v/v with 72 hours of fermentation. Different variety of Rice showed the efficiency of fermentation varied from 90 to 92% which are identical to conventional distilling process.
  • Residual Sugar (RS) in the final fermented wash was in the range of 0.2 to 0.5%.
  • Resistant Starch (RST) in the final fermented wash was in the range of 0.62 to 1.63%.

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Abstract

L'invention concerne un procédé de production d'un produit de fermentation et d'un co-produit protéique concentré à partir d'un matériau contenant de l'amidon.
PCT/EP2025/068082 2024-07-04 2025-06-26 Procédé de production d'un produit de fermentation et d'un co-produit protéique concentré Pending WO2026008449A2 (fr)

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