Classifications

• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L7/00—Cereal-derived products; Malt products; Preparation or treatment thereof
  • A23L7/10—Cereal-derived products
  • A23L7/104—Fermentation of farinaceous cereal or cereal material; Addition of enzymes or microorganisms
  • A23L7/107—Addition or treatment with enzymes not combined with fermentation with microorganisms
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; PREPARATION THEREOF
  • A23C11/00—Milk substitutes, e.g. coffee whitener compositions
  • A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
  • A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; PREPARATION THEREOF
  • A23C9/00—Milk preparations; Milk powder or milk powder preparations
  • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
  • A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
  • A23C9/1216—Other enzymes
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/14—Vegetable proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
  • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
  • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
  • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
  • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
  • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
  • A23L2/38—Other non-alcoholic beverages
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
  • A23L2/52—Adding ingredients
  • A23L2/66—Proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
  • A23L29/015—Inorganic compounds
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
  • A23L29/06—Enzymes
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L9/00—Puddings; Cream substitutes; Preparation or treatment thereof
  • A23L9/20—Cream substitutes
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/10—Transferases (2.)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
  • C12N9/18—Carboxylic ester hydrolases (3.1.1)
  • C12N9/20—Triglyceride splitting, e.g. by means of lipase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
  • C12N9/2405—Glucanases
  • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; PREPARATION THEREOF
  • A23C2220/00—Biochemical treatment
  • A23C2220/10—Enzymatic treatment
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
  • C12Y101/03—Oxidoreductases acting on the CH-OH group of donors (1.1) with a oxygen as acceptor (1.1.3)
  • C12Y101/03004—Glucose oxidase (1.1.3.4)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y203/00—Acyltransferases (2.3)
  • C12Y203/02—Aminoacyltransferases (2.3.2)
  • C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y301/00—Hydrolases acting on ester bonds (3.1)
  • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
  • C12Y301/01003—Triacylglycerol lipase (3.1.1.3)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y301/00—Hydrolases acting on ester bonds (3.1)
  • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
  • C12Y301/01004—Phospholipase A2 (3.1.1.4)
• • 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)
  • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
• • 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)
  • C12Y302/01015—Polygalacturonase (3.2.1.15)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)

Definitions

• the present invention relates to a method for producing plant-based milk; a method for improving the dispersion stability during the production of plant-based milk; and an enzyme preparation for modifying plant-based milk or for improving the dispersion stability during the production of plant-based milk.
• Foamed milk coffee also known as caffe latte, cappuccino, latte macchiato, etc.
• Foamed milk coffee served at restaurants and the like is prepared by combining milk that has been frothed to create bubbles (foamed milk) with coffee (or a mixture of coffee and liquid milk) to form a layer of foamed milk and a layer of coffee (or a mixture of coffee and liquid milk).
• non-dairy plant-based milks e.g., oat milk
• plant-based milks that can be used to prepare milk foam.
• plant-based milks such as oat milk have poor foaming properties, making it difficult to produce foamed milk with a sufficient amount of bubbles.
• the oil phase and the water phase are likely to separate, or oat-derived precipitation is likely to occur, making the production difficult.
• Patent Document 1 discloses a method for producing a processed vegetable protein food or beverage material and/or a vegetable protein food or beverage product, which comprises a step of treating a vegetable protein food or beverage material and/or a vegetable protein food or beverage with a protein deamidating enzyme and at least one enzyme selected from the group consisting of lipase and cyclodextrin glucanotransferase.
• US Patent No. 5,399,633 discloses a method for producing oat milk using alkaline protease and an emulsifier.
• 5,399, 667 discloses a method for producing a liquid oat base or drink with an improved soluble oat protein content from an oat material, comprising starch and oat protein, characterized in that the oat protein is solubilized in an aqueous solvent, in particular water, by means of a protein-deamidase; and optionally decanting the product.
• a specific enzyme described below in the present invention can produce a plant-based milk capable of preparing foamed milk having a sufficient amount of bubbles.
• the object of the present invention is to provide a method for producing plant-based milk that can produce foamed milk with a sufficient amount of bubbles. It is also an object of the present invention to provide a method for improving the dispersion stability during the production of plant-based milk.
• the present inventors have conducted intensive research to solve the above problems, and have found that when a vegetable milk (e.g., oat milk) is produced, a vegetable milk (e.g., oat milk) capable of producing foamed milk having a sufficient amount of bubbles can be produced by allowing a specific enzyme of the present invention, which will be described later, to act on a raw material (e.g., raw oats) containing vegetable protein.
• a specific enzyme of the present invention which will be described later
• the present inventors have also found that when a vegetable milk (e.g., oat milk) is produced, separation of the oil phase and the aqueous phase can be suppressed, or precipitation derived from oats can be suppressed, thereby improving dispersion stability. Based on these findings, the present inventors conducted further studies and completed the present invention.
• a method for producing plant-based milk comprising treating a raw material containing plant protein with two or more enzymes selected from the group consisting of (1) to (6) below.
• a method for producing plant-based milk comprising treating a raw material containing plant protein with one or more enzymes selected from the group consisting of (1) to (6) below, and an alkali metal salt.
• one or more enzymes selected from the group consisting of (1) to (6) below, and an alkali metal salt.
• a method for improving dispersion stability during the production of plant-based milk comprising treating a raw material containing plant protein with two or more enzymes selected from the group consisting of (1) to (6) below.
• a method for improving dispersion stability during the production of plant-based milk comprising treating a raw material containing a plant protein with one or more enzymes selected from the group consisting of (1) to (6) below, and an alkali metal salt.
• one or more enzymes selected from the group consisting of (1) to (6) below, and an alkali metal salt.
• An enzyme preparation for modifying plant-based milk or for improving the dispersion stability during the production of plant-based milk comprising two or more enzymes selected from the group consisting of (1) to (6) below: (1) lipase, (2) glucose oxidase, (3) cell wall decomposition enzyme, (4) protease, (5) transglutaminase, and (6) phospholipase.
• An enzyme preparation for modifying vegetable milk or for improving the dispersion stability during the production of vegetable milk comprising one or more enzymes selected from the group consisting of the following (1) to (6) and an alkali metal salt: (1) lipase, (2) glucose oxidase, (3) cell wall decomposition enzyme, (4) protease, (5) transglutaminase, and (6) phospholipase.
• a plant-based milk e.g., oat milk
• a plant-based milk capable of preparing foamed milk having a sufficient amount of bubbles.
• the plant-based milk (e.g., oat milk) produced by the production method of the present invention can prepare foamed milk having a sufficient amount of bubbles.
• FIG. 1 is a schematic diagram for explaining the method for evaluating the foaming properties of oat milk in Test Examples 1 to 4.
• the method for producing plant-based milk of the present invention includes the following aspects (A) and (B).
• a method for producing plant-based milk comprising treating a raw material containing a plant protein with two or more enzymes selected from the group consisting of (1) to (6) below (hereinafter also referred to as the production method (A) of the present invention).
• B) A method for producing vegetable milk comprising treating a raw material containing vegetable protein with one or more enzymes selected from the group consisting of the following (1) to (6) and an alkali metal salt (hereinafter also referred to as the production method (B) of the present invention).
• the "production method of the present invention” includes the production methods (A) and (B) of the present invention.
• the method (A) for producing plant-based milk of the present invention comprises treating a raw material containing plant protein with two or more enzymes selected from the group consisting of (1) to (6) below.
• the method (B) for producing plant-based milk of the present invention comprises treating a raw material containing plant protein with one or more enzymes selected from the group consisting of (1) to (6) below, and an alkali metal salt.
• Combinations of two or more enzymes used in the production method of the present invention include, for example, the following (7) to (12).
• a combination of two or more types of proteases e.g., a combination of two or more types selected from the group consisting of chymotrypsin, trypsin, chymotrypsin-like proteases, trypsin-like proteases, metal proteases, and serine proteases (e.g., a combination of a metal protease and a serine protease (particularly a chymotrypsin-like protease))
• Protease and lipase 9
• Protease and phospholipase 10
• Protease and transglutaminase (11)
• Protease and cell wall decomposition enzyme (12) Lipase and phospholipase
• examples of combinations of two or more enzymes used in the production method (A) of the present invention include the following (i) to (xx).
• examples of the one or more enzymes (one type of enzyme, or a combination of two or more types of enzymes) used in the production method (B) of the present invention include the following (I) to (VI) and (i) to (xx).
• enzymes (1) to (12), (I) to (VI), (i) to (xx), etc. will be collectively referred to as "enzymes of the present invention.”
• the protease used in the present invention is an enzyme that catalyzes the hydrolysis of peptide bonds in proteins, and the present invention can use any protease with any substrate specificity and any reaction characteristics as long as it has the activity and can degrade proteins.
• any protease of any origin such as plant-derived, mammal-derived, fish-derived, or microbial-derived, can be used, and recombinant enzymes may also be used.
• the activity unit of an endoprotease is defined as one unit (1 U) of the amount of enzyme that causes an increase in a Folin's test solution color substance equivalent to 1 ⁇ g of tyrosine per minute using casein as a substrate.
• the activity unit of an exoprotease is defined as the activity to produce 1 ⁇ mol of p-nitroaniline per minute using L-leucyl-p-nitroanilide as a substrate (1 U).
• the protease is preferably an endo-type protease.
• the endoprotease used in the present invention is an enzyme that hydrolyzes peptide bonds within a protein to produce several peptides.
• Examples of the endoprotease used in the present invention include chymotrypsin, trypsin, chymotrypsin-like proteases, trypsin-like proteases, metalloproteases, serine proteases, endoneutral proteases, and endoalkaline proteases.
• the protease used in the present invention may be a commercially available product, and examples thereof include Protin SD-NY10 (manufactured by Amano Enzyme Inc., endo-type neutral protease), Protin SD-AY10 (manufactured by Amano Enzyme Inc., endo-type alkaline protease), and Formea CTL 300 BG (manufactured by Novozymes Japan Ltd., chymotrypsin-like protease).
• the amount of protease added is preferably 0.0001 to 1,000,000 U, more preferably 0.001 to 100,000 U, even more preferably 0.01 to 10,000 U, and particularly preferably 0.1 to 1,000 U in terms of enzyme activity per gram of protein contained in the raw material containing vegetable protein (e.g., raw oats).
• Lipase used in the present invention is an enzyme that catalyzes the reaction of hydrolyzing fatty acid esters into fatty acids and glycerin.
• the lipase is a lipase that can be added to foods.
• lipases examples include, but are not limited to, “Lipase A-10D” (manufactured by Nagase & Co., Ltd.), “Lipase DF “Amano”, “Lipase R” (manufactured by Amano Enzyme Inc.), “Lipase OF”, “Lipase PL” (manufactured by Meito Sangyo Co., Ltd.), and Lipozyme TL 100 L (manufactured by Novozymes Japan Ltd.).
• the enzyme activity of lipase is defined as follows.
• the lipase is preferably a lipase acting on mono- or di-coordinated triglycerides.
• the lipase used in the present invention may be a commercially available product, for example, Lipase AY “Amano” 30SD (manufactured by Amano Enzyme Inc.) or Lipase MHA “Amano” 10SD (manufactured by Amano Enzyme Inc.).
• the amount of lipase added is preferably 0.0001 to 10,000,000 U, more preferably 0.001 to 1,000,000 U, even more preferably 0.01 to 100,000 U, and particularly preferably 0.1 to 10,000 U in terms of enzyme activity per gram of protein contained in the raw material containing vegetable protein (e.g., raw oats).
• Phospholipase used in the present invention is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances.
• Phospholipase A2 is an enzyme that cleaves the SN-2 acyl group of phospholipids.
• the enzyme activity of phospholipase is defined as follows. When the enzyme is added to a 1% L- ⁇ -phosphotidylcholine solution (pH 8.0, 0.1 M Tris-HCl buffer, 5 mM CaCl 2 ) and reacted at 37° C., the amount of enzyme that produces 1 ⁇ mol of free fatty acid per minute is defined as 1 U (1 unit).
• the phospholipase is preferably phospholipase A2.
• the phospholipase used in the present invention may be a commercially available product, for example, PLA2 Nagase 10P/R (manufactured by Nagase ChemteX Corporation).
• the amount of phospholipase added is preferably 0.0001 to 1,000,000 U, more preferably 0.001 to 100,000 U, even more preferably 0.01 to 10,000 U, and particularly preferably 0.1 to 1,000 U in terms of enzyme activity per gram of protein contained in the raw material containing vegetable protein (e.g., raw oats).
• the transglutaminase used in the present invention is an enzyme having an activity of catalyzing an acyl transfer reaction in which a glutamine residue in a protein or peptide is used as a donor and a lysine residue is used as an acceptor, and transglutaminase of various origins, such as those derived from mammals, fish, and microorganisms, is known.
• the transglutaminase used in the present invention is not particularly limited in origin as long as it has the above-mentioned activity, and transglutaminase of any origin can be used, and recombinant enzymes can also be used.
• transglutaminase used in the present invention may be a commercially available product, and as a specific example, transglutaminase derived from a microorganism commercially available from Ajinomoto Co., Inc. under the product name "Activa" TG can be used alone or in combination.
• the enzymatic activity of transglutaminase is defined as 1 unit (1 U) of the enzyme amount that produces 1 ⁇ mole of hydroxamic acid per minute, as determined by reacting transglutaminase in a reaction system containing benzyloxycarbonyl-L-glutamylglycine and hydroxylamine as substrates in a Tris buffer solution at 37° C.
• the amount of transglutaminase added is preferably 0.00001 to 100,000 U, more preferably 0.0001 to 10,000 U, even more preferably 0.001 to 1,000 U, and particularly preferably 0.01 to 100 U in terms of enzyme activity per gram of protein contained in the raw material containing vegetable protein (e.g., raw oats).
• the cell wall decomposing enzymes used in the present invention refer to enzymes such as cellulase, hemicellulase, and pectinase that can act on cell wall components.
• Cellulase is a cellulolytic enzyme that randomly hydrolyzes the ⁇ -1,4 glycosidic bonds between ⁇ -glucose units that constitute cellulose. It may be produced by any method as long as it has this property. It may be extracted from plants, produced by microorganisms, or may be a genetically modified enzyme.
• the enzyme may be in any form, such as powder, liquid, or granules.
• cellulase T "Amano"4" commercially available from Amano Enzyme Co., Ltd.
• Cellulose is the main component that constitutes cell walls, and the action of cellulase can decompose the cell walls.
• Hemicellulase is a general term for enzymes that hydrolyze hemicellulose.
• the hemicellulase is a hemicellulase that can be added to food.
• hemicellulase examples include, but are not limited to, "Hemicellulase "Amano”90” (manufactured by Amano Enzyme Inc.) and “Sumiteam X” (manufactured by Shin Nippon Chemical Industry Co., Ltd.).
• the enzyme activity of cellulase is defined as 1 U (unit) when sodium carmellose is used as a substrate and the amount of enzyme that increases the reducing power equivalent to 1 ⁇ mol of glucose per minute is defined as 1 U.
• pectinase is an enzyme that has the activity of catalyzing the reaction of hydrolyzing pectin (EC 3.2.1.15, etc.). This activity is also called "pectinase activity.” Specifically, pectinase activity may be activity that catalyzes the reaction of hydrolyzing the ⁇ -1,4 glycosidic bonds of the polygalacturonic acid chain that constitutes pectin.
• pectinase activity also includes pectin lyase activity that degrades polygalacturonic acid chains by ⁇ -elimination, pectin methylesterase activity that demethylates the methyl ester group of pectin, and protopectinase activity that acts on water-insoluble protopectin to liberate water-soluble pectin.
• the enzyme activity of pectinase can be measured by the following procedure. That is, the activity of pectinase can be measured by incubating the enzyme with a substrate and measuring the enzyme-dependent decomposition of the substrate.
• the decomposition of the substrate can be measured, for example, using the generation of reducing ends (i.e., an increase in reducing power) as an index.
• the increase in reducing power can be measured, for example, by the dinitrosalicylic acid (DNS) method or the Somogyi-Nelson method.
• DAS dinitrosalicylic acid
• Somogyi-Nelson method the amount of enzyme that causes an increase in reducing power equivalent to 1 ⁇ mol of galacturonic acid per minute at 45° C. and pH 4.5 when an enzyme reaction is carried out using polygalacturonic acid as a substrate is defined as 1 U (unit).
• the increase in reducing power equivalent to a certain amount of galacturonic acid may be read as the production of that amount of galacturonic acid.
• the production amount of galacturonic acid can be measured by a known method used for quantifying compounds, such as HPLC, LC/MS, GC/MS, and NMR.
• the cell wall decomposing enzyme is preferably pectinase, cellulase, or hemicellulase, and more preferably pectinase.
• the cell wall decomposing enzymes used in the present invention may be commercially available products, such as Cellulase A "Amano" 3 (manufactured by Amano Enzyme Inc.), Hemicellulase “Amano” 90 (manufactured by Amano Enzyme Inc.), Pectinase XP-534 NEO (manufactured by Nagase ChemteX Corporation), and Sumiteam AP2 (manufactured by Shin Nippon Kagaku Kogyo Co., Ltd.).
• Cellulase A "Amano" 3 manufactured by Amano Enzyme Inc.
• Hemicellulase "Amano” 90 manufactured by Amano Enzyme Inc.
• Pectinase XP-534 NEO manufactured by Nagase ChemteX Corporation
• Sumiteam AP2 manufactured by Shin Nippon Kagaku Kogyo Co., Ltd.
• the amount of the cell wall-degrading enzyme to be added is preferably 0.00001 to 1,000,000 U, more preferably 0.00001 to 100,000 U, even more preferably 0.0001 to 10,000 U, and particularly preferably 0.001 to 1,000 U, in terms of enzyme activity per gram of protein contained in a raw material containing vegetable protein (e.g., raw oats).
• the amount of cellulase added is preferably 0.00001 to 100,000 U, more preferably 0.0001 to 10,000 U, even more preferably 0.001 to 1,000 U, and particularly preferably 0.01 to 100 U in terms of enzyme activity per gram of protein contained in a raw material containing vegetable protein (e.g., raw oats).
• the amount of hemicellulase added is preferably 0.00001 to 100,000 U, more preferably 0.0001 to 10,000 U, even more preferably 0.001 to 1,000 U, and particularly preferably 0.01 to 100 U in terms of enzyme activity per gram of protein contained in a raw material containing vegetable protein (e.g., raw oats).
• the amount of pectinase added is preferably 0.00001 to 100,000 U, more preferably 0.0001 to 10,000 U, even more preferably 0.001 to 1,000 U, and particularly preferably 0.01 to 100 U in terms of enzyme activity per gram of protein contained in a raw material containing vegetable protein (e.g., raw oats).
• Glucose oxidase used in the present invention is an enzyme that catalyzes the reaction of producing gluconolactone (gluconolactone is non-enzymatically hydrolyzed to gluconic acid) and hydrogen peroxide using glucose and oxygen as substrates.
• the hydrogen peroxide produced by this reaction oxidizes the SH group in the protein, promoting the production of SS bonds (disulfide bonds) and forming a cross-linked structure in the protein.
• Glucose oxidases of various origins, such as those derived from microorganisms such as koji mold and those derived from plants, are known, and any of these glucose oxidases may be used, and the origin is not limited.
• glucose oxidase is the glucose oxidase derived from a microorganism that is commercially available from Shin-Nihon Kagaku Kogyo Co., Ltd. under the trade name "Sumiteam PGO".
• the activity unit of glucose oxidase is defined as 1 U (unit) as the amount of enzyme that oxidizes 1 ⁇ mol of glucose per minute at 37° C. and pH 7.0.
• the activity of glucose oxidase can be exemplified by the following method. Glucose is used as a substrate, and hydrogen peroxide is generated by acting glucose oxidase in the presence of oxygen.
• a quinoneimine dye is generated by acting peroxidase on the generated hydrogen peroxide in the presence of aminoantipyrine and phenol.
• the generated quinoneimine dye is measured at a wavelength of 500 nm.
• the method is as follows. Glucose oxidase is stirred and dissolved in 0.1 mol/L phosphate buffer (adjusted to pH 7.0 with potassium dihydrogen phosphate and sodium hydroxide aqueous solution), and then diluted 50 times with 0.1 mol/L phosphate buffer to obtain a GO solution.
• a phenol-containing buffer solution (Milli-Q, 1.36 g of potassium dihydrogen phosphate, 3 mL of 5% phenol test solution, and 3 mL of 5% Triton X-100 solution are mixed and adjusted to pH 7.0 with sodium hydroxide aqueous solution, 100 mL), 500 ⁇ L of a 10% glucose solution, 500 ⁇ L of a 0.01% peroxidase solution (PO "amano" 3 (1250 U ⁇ 250 U) is used), and 100 ⁇ L of a 0.4% 4-aminoantipyrine solution are added in order, mixed by inversion, and kept at 37 ⁇ 0.1 ° C. for 10 minutes.
• a phenol-containing buffer solution (Milli-Q, 1.36 g of potassium dihydrogen phosphate, 3 mL of 5% phenol test solution, and 3 mL of 5% Triton X-100 solution are mixed and adjusted to pH 7.0 with sodium hydroxide aqueous solution, 100 mL)
• GO activity value is measured from the increment (slope) between 120 seconds and 300 seconds.
• the value measured by adding 0.1 mol/L phosphate buffer instead of the GO solution was used and subtracted from the value measured for the GO test group.
• the amount of enzyme required to oxidize or reduce 1 ⁇ mol of substrate per minute is defined as 1 U (unit).
• the amount of glucose oxidase added is, for example, 0.00001 to 100,000 U, preferably 0.0001 to 10,000 U, more preferably 0.001 to 1000 U, and even more preferably 0.01 to 100 U in terms of enzyme activity per gram of starch contained in the raw material containing vegetable protein (e.g., raw oats).
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• lipase and Cell Wall Decomposing Enzyme In the production method of the present invention, when lipase and cell wall decomposing enzyme (e.g., cellulase, hemicellulase, pectinase) are used in combination, the weight ratio of the amounts added (lipase:cell wall decomposing enzyme) is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• lipase and cell wall decomposing enzyme e.g., cellulase, hemicellulase, pectinase
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001-100,000, preferably 1:0.0001-10,000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• the weight ratio of the amounts added is, for example, 1:0.00001-100,000, preferably 1:0.0001-10,000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• glucose oxidase and cell wall decomposing enzyme e.g., cellulase, hemicellulase, pectinase
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.00001 to 100,000, preferably 1:0.0001 to 10,000, more preferably 1:0.001 to 1,000, and even more preferably 1:0.01 to 100.
• the weight ratio of the amounts added is, for example, 1:0.0001-10,000, preferably 1:0.001-1,000, more preferably 1:0.01-100, and even more preferably 1:0.1-10.
• cell Wall Decomposing Enzyme and Phospholipase In the production method of the present invention, when a cell wall decomposing enzyme (e.g., cellulase, hemicellulase, pectinase) and a phospholipase are used in combination, the weight ratio of the amounts added (cell wall decomposing enzyme:phospholipase) is, for example, 1:0.0001-10,000, preferably 1:0.001-1,000, more preferably 1:0.01-100, and even more preferably 1:0.1-10.
• a cell wall decomposing enzyme e.g., cellulase, hemicellulase, pectinase
• phospholipase phospholipase
• the weight ratio of the amounts added is, for example, 1:0.00001-100000, preferably 1:0.0001-10000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• the weight ratio of the amounts added is, for example, 1:0.00001-100,000, preferably 1:0.0001-10,000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• the weight ratio of the amounts added is, for example, 1:0.00001-100,000, preferably 1:0.0001-10,000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• the weight ratio of the amounts added is, for example, 1:0.00001-100,000, preferably 1:0.0001-10,000, more preferably 1:0.001-1000, and even more preferably 1:0.01-100.
• lipase, cell wall decomposing enzyme, and protease In the production method of the present invention, when lipase, cell wall decomposing enzyme (e.g., cellulase, hemicellulase, pectinase), and protease are used in combination, the weight ratio of the amounts added (lipase:cell wall decomposing enzyme:protease) is, for example, 1:0.00001-100000:0.00001-100000, preferably 1:0.0001-10000:0.0001-10000, more preferably 1:0.001-1000:0.001-1000, and even more preferably :0.01-100:0.01-100.
• lipase, cell wall decomposing enzyme e.g., cellulase, hemicellulase, pectinase
• protease the weight ratio of the amounts added (lipase:cell wall decomposing enzyme:protease) is, for example, 1:0.00001-100000:0.00001-100000, preferably 1:0.0001-10
• the weight ratio of the amounts added is, for example, 1:0.00001-100000:0.00001-100000, preferably 1:0.0001-10000:0.0001-10000, more preferably 1:0.001-1000:0.001-1000, and even more preferably :0.01-100:0.01-100.
• cell Wall Decomposing Enzymes, Proteases, and Transglutaminase In the production method of the present invention, when a cell wall decomposing enzyme (e.g., cellulase, hemicellulase, pectinase), a protease, and a transglutaminase are used in combination, the weight ratio of the amounts added (cell wall decomposing enzyme:protease:transglutaminase) is, for example, 1:0.00001-100000:0.00001-100000, preferably 1:0.0001-10000:0.0001-10000, more preferably 1:0.001-1000:0.001-1000, and even more preferably :0.01-100:0.01-100.
• a cell wall decomposing enzyme e.g., cellulase, hemicellulase, pectinase
• the weight ratio of the amounts added is, for example, 1:0.00001-100000:0.00001-100000, preferably 1:0.0001-10000:0.0001-10000
• the raw material containing vegetable protein to be treated with the enzyme can be a plant or a processed product thereof that is conventionally used as a raw material for vegetable milk, such as grains such as oats and rice, nuts and seeds such as almonds, cashew nuts, and coconuts, beans such as soybeans and peas, and processed products thereof.
• the grains, nuts and seeds, and beans may be whole grains or may have the skin and germ removed, or may be ground, but ground products are preferred.
• Examples of processed grains, nuts and seeds, and beans include vegetable milk (e.g., oat milk powder) produced by a conventional production method.
• the raw material containing vegetable protein may be a commercially available product, and examples thereof include whole oat flour under the product name "Oat Flour” (produced in Denmark/Sansho Co., Ltd.) and oat milk powder produced by a conventional production method under the product name "Oat Milk Powder GD-F” (Godo Co., Ltd.).
• oat milk can be produced by using a raw material derived from oats (e.g., whole oats, oats with the skin and germ removed, crushed oats, processed oats) (referred to as "raw oats" in this specification) as the raw material containing vegetable protein to be treated with the enzyme.
• a raw material derived from oats e.g., whole oats, oats with the skin and germ removed, crushed oats, processed oats
• raw oats e.g., whole oats, oats with the skin and germ removed, crushed oats, processed oats
• the manufacturing method of the present invention can be produced in the same manner and using the same raw materials as regular plant-based milk, except that it is treated with the enzyme of the present invention.
• the manufacturing method of the present invention can produce the plant-based milk (e.g., oat milk) of the present invention by comprising the steps of: (i) A raw material containing vegetable protein (for example, raw oats) is mixed with water (if necessary, the raw material is pulverized in a mill or the like and then mixed with water, or the raw material is pulverized together with water in a mill or the like) to obtain a 1 to 30 w/w % suspension.
• a raw material containing vegetable protein for example, raw oats
• water if necessary, the raw material is pulverized in a mill or the like and then mixed with water, or the raw material is pulverized together with water in a mill or the like
• the mixture is subjected to solid-liquid separation by centrifugation or the like, the liquid is recovered, and the pH is adjusted to 6 to 10 using a pH adjuster (e.g., tripotassium phosphate) as necessary, to obtain the plant-based milk of the present invention (e.g., oat milk).
• a pH adjuster e.g., tripotassium phosphate
• an alkali metal salt e.g., tripotassium phosphate
• the production method (B) of the present invention includes treating the above-mentioned raw material with one or more of the above-mentioned enzymes and an alkali metal salt (e.g., tripotassium phosphate).
• the addition of the alkali metal salt is expected to improve the foaming properties of vegetable milk (e.g., oat milk).
• the alkali metal salt may be added at any time without limitation when a raw material containing a vegetable protein (e.g., raw oats) is dispersed, when amylase is added, when an enzyme is added, or when the enzyme reaction is completed.
• the amount of the alkali metal salt added is preferably 0.00001 w/w% to 10.0 w/w%, more preferably 0.0001 w/w% to 5.0 w/w%, even more preferably 0.001 w/w% to 1.0 w/w%, and particularly preferably 0.01 w/w% to 0.1 w/w%, based on the total weight (raw materials containing vegetable protein + dissolution water).
• an alkali metal salt eg, tripotassium phosphate
• it is sufficient that the alkali metal salt is added within the above range, and there is no need to add any further alkali metal salt.
• the manufacturing method of the present invention allows for the production of an improved vegetable milk (e.g., oat milk).
• modified includes improvement of foaming properties.
• the presence or absence of modification (improvement in foaming property) can be evaluated in accordance with the evaluation of foaming property in the test examples described below.
• the improved plant-based milk (e.g., oat milk) produced by the manufacturing method of the present invention has excellent foaming properties and is therefore useful as plant-based milk for preparing foamed milk (also referred to in this specification as "plant-based milk for foamed milk”).
• the improved plant-based milk (e.g., oat milk) produced by the manufacturing method of the present invention can also be used as plant-based milk for mixing with coffee to prepare a coffee beverage (also referred to in this specification as "plant-based milk for coffee beverages”).
• a "coffee beverage” may be any beverage that contains a combination of coffee and vegetable milk, and includes, for example, foamed milk coffee (also known as caffe latte, cappuccino, latte macchiato, etc.), which is prepared to have a layer of foamed vegetable milk and a layer of coffee (or a mixture of coffee and liquid vegetable milk), and coffee with vegetable milk, which is prepared by mixing liquid vegetable milk with coffee.
• the present invention also relates to a method for improving dispersion stability during production of plant-based milk, which comprises treating a raw material containing a plant protein with the enzyme of the present invention described above (hereinafter, also simply referred to as the method for improving dispersion stability of the present invention).
• the method for improving dispersion stability of the present invention includes the following aspects (A) and (B).
• (B) A method for improving dispersion stability during the production of vegetable milk, comprising treating a raw material containing vegetable protein with one or more enzymes selected from the group consisting of (1) to (6) above and an alkali metal salt (hereinafter also referred to as the improvement method (B) of the present invention).
• the “improvement method of the present invention” includes the improvement methods (A) and (B) of the present invention.
• improved dispersion stability means that phase separation (separation of oil and water phases, or precipitation due to oats, etc.) is suppressed during the production of plant-based milk.
• the improvement in dispersion stability can be evaluated according to the evaluation of dispersion stability in the test examples described below.
• the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzymatic reaction), examples of raw materials containing vegetable proteins to be treated with the enzyme, examples of alkali metal salts, and amounts to be added of each enzyme in the present invention are the same as the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzymatic reaction), examples of raw materials containing vegetable proteins to be treated with the enzyme, examples of alkali metal salts, and amounts to be added of each enzyme in the production method of the present invention.
• Enzyme preparation for modifying vegetable milk or for improving dispersion stability during production of vegetable milk The present invention also relates to an enzyme preparation for modifying vegetable milk or for improving dispersion stability during production of vegetable milk, which contains the enzyme of the present invention described above (hereinafter, also simply referred to as the enzyme preparation of the present invention).
• the method for improving dispersion stability of the present invention includes the following aspects (A) and (B).
• an enzyme preparation for modifying vegetable milk or for improving the dispersion stability during the production of vegetable milk comprising one or more enzymes selected from the group consisting of (1) to (6) above and an alkali metal salt (hereinafter also referred to as the enzyme preparation (B) of the present invention).
• the "enzyme preparation of the present invention” includes the enzyme preparations (A) and (B) of the present invention.
• the definition, amount to be added, method of addition (action time, action temperature, method of terminating the enzyme reaction), examples of raw materials containing vegetable proteins to be treated with the enzyme, examples of alkali metal salts, and amounts to be added of each enzyme in the present invention are the same as the definition, amount to be added, method of addition (action time, action temperature, method of terminating the enzyme reaction), examples of raw materials containing vegetable proteins to be treated with the enzyme, examples of alkali metal salts, and amounts to be added of each enzyme in the production method or method of improving dispersion stability of the present invention.
• the enzyme preparation of the present invention can be added to a raw material containing vegetable protein (e.g., raw oats) in accordance with the method and amount of addition of the enzyme (or oxygen and alkali metal salt) of the present invention explained in the above-mentioned production method of the present invention, and reacted to produce a modified vegetable milk (e.g., oat milk).
• the enzyme preparation of the present invention can also be used in the method of improving dispersion stability of the present invention.
• ⁇ -amylase (trade name Spitase CP-40FG, Nagase Chemtex Corporation) was added to the obtained suspension at 170 U/g of starch, and ⁇ -amylase (trade name ⁇ -amylase-F "Amano", Amano Enzyme Co., Ltd.) was added at 0.09 U/g of starch, and the mixture was reacted at 60°C for 1 hour. After the reaction, the pH of the reaction solution was adjusted to 8 using tripotassium phosphate. Then, each enzyme shown in Tables 6 and 7 was added to the mixture at the respective concentrations shown in Tables 6 and 7, and the mixture was reacted at 60°C for 1 hour.
• the mixture was heated at 95°C for 10 minutes, and cooled after completion.
• the cooled suspension was centrifuged at 1000 G/1 minute to separate the solid and liquid, and only the liquid was recovered.
• the pH was adjusted to 7.5 using tripotassium phosphate to obtain the oat milks of Examples 17 to 28.
• ⁇ -amylase (trade name Spitase CP-40FG, Nagase ChemteX Corporation) was added at 170 U/g of starch, and ⁇ -amylase (trade name ⁇ -amylase-F "Amano", Amano Enzyme Co., Ltd.) was added at 0.09 U/g of starch, and the mixture was reacted at 60°C for 1 hour.
• the pH of the reaction solution was adjusted to 8 using tripotassium phosphate.
• each enzyme shown in Table 9 was added to the mixture at the concentration shown in Table 9, and the mixture was reacted at 60°C for 1 hour. After the reaction, the mixture was heated at 95°C for 10 minutes, and cooled after completion.
• the cooled suspension was centrifuged at 1000 G/1 min to separate the solid and liquid, and only the liquid was collected and adjusted to pH 7.5 using tripotassium phosphate to obtain the oat milks of Examples 29 to 31.
• the total amount of tripotassium phosphate used for the pH adjustment is shown in Table 9.
• ⁇ -amylase (trade name Spitase CP-40FG, Nagase ChemteX Corporation) was added at 170 U/g of starch, and ⁇ -amylase (trade name ⁇ -amylase-F "Amano", Amano Enzyme Co., Ltd.) was added at 0.09 U/g of starch, and the mixture was reacted at 60°C for 1 hour.
• the pH of the reaction solution was adjusted to 8 using tripotassium phosphate.
• each of the enzymes shown in Tables 11 to 13 was added to the mixture at the concentrations shown in Tables 11 to 13, and the mixture was reacted at 60°C for 1 hour.
• oat milk that can be used to prepare foamed milk with a sufficient amount of bubbles.

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