Classifications

• • 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)
  • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
  • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
• • 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
  • A23C20/00—Cheese substitutes
  • A23C20/02—Cheese substitutes containing neither milk components, nor caseinate, nor lactose, as sources of fats, proteins or carbohydrates
• • 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
  • A23C20/00—Cheese substitutes
  • A23C20/02—Cheese substitutes containing neither milk components, nor caseinate, nor lactose, as sources of fats, proteins or carbohydrates
  • A23C20/025—Cheese substitutes containing neither milk components, nor caseinate, nor lactose, as sources of fats, proteins or carbohydrates mainly containing proteins from pulses or oilseeds
• • 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.)
  • C12N9/1048—Glycosyltransferases (2.4)
  • C12N9/1051—Hexosyltransferases (2.4.1)
• • 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
  • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
  • C12N9/2411—Amylases
  • C12N9/2425—Beta-amylase (3.2.1.2)
• • 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)
  • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
  • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
  • C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
• • 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)
  • C12Y302/01002—Beta-amylase (3.2.1.2)
• • 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)
  • C12Y302/01116—Glucan 1,4-alpha-maltotriohydrolase (3.2.1.116)

Definitions

• the present invention relates to a method for producing plant-based cheese. More specifically, the present invention relates to a method for producing plant-based cheese that is both hard when not heated and melts easily when heated.
• thermo melting One of the characteristics of cheese made from animal milk is that it melts when heated (hereinafter, this characteristic will be referred to as "thermal melting”). This characteristic is related to the milk fat and casein contained in animal milk, and is one of the reasons why cheese is so appetizing. On the other hand, plant-based cheese, which has a completely different protein composition, does not inherently have thermal melting properties.
• Patent Document 1 discloses that treating the ingredients of plant-based cheese with protease improves the heat-melt properties of the resulting plant-based cheese.
• the plant-based cheese obtained by the manufacturing method disclosed in the above Patent Document 1 exhibits excellent heat melting properties, but the acquired heat melting properties come at the expense of reduced hardness.
• the present invention aims to provide a technology for producing plant-based cheese that is both hard when not heated and melts easily when heated.
• the inventors discovered that by subjecting a material containing vegetable protein to hydrolysis and enzymatic treatment with a specific carbohydrate-processing enzyme, it is possible to achieve both hardness when not heated and thermal meltability.
• the present invention was completed through further investigation based on this finding.
• Item 1 A method for producing a plant-based cheese, comprising: (A) subjecting a material containing a plant protein to a hydrolysis treatment and an enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase; and (B) mixing the material with starch.
• Item 2. The method according to Item 1, wherein the glycosyltransferase is a cyclodextrin-forming enzyme.
• Item 3 The method according to Item 1 or 2, wherein the hydrolysis treatment is an enzymatic treatment with a protease.
• Item 5 The production method according to any one of Items 1 to 4, further comprising, after the step (A) and before the step (B), a step of inactivating the enzyme used in the step (A).
• Item 6. The method according to any one of Items 3 to 5, wherein the amount of the protease used per 1 g of the vegetable protein in the step (A) is 5 to 300,000 U.
• Item 11 A method for imparting hardness and heat melting properties to a plant-based cheese, comprising the steps of (A) subjecting a material containing a plant protein to a hydrolysis treatment and an enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase, and (B) mixing starch in the production of a plant-based cheese.
• a plant-based cheese obtained by the production method according to any one of Items 1 to 10.
• Item 13 A plant-based cheese obtained by the production method according to any one of Items 1 to 10.
• a method for producing a plant-based cheese comprising the steps of subjecting a material containing hydrolyzed vegetable protein to an enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase, and mixing with starch.
• the present invention provides a technology for producing plant-based cheese that is both hard when unheated and melts easily when heated.
• the method for producing plant-based cheese of the present invention is characterized by including a step (A) of subjecting a material containing a plant protein to hydrolysis treatment and enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase (hereinafter also referred to as “step (A)"), and a step (B) of mixing starch (hereinafter also referred to as “step (B)”).
• step (A) a material containing a plant protein to hydrolysis treatment and enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase
• step (B) a step of mixing starch
• Step (A) a material containing vegetable protein is subjected to hydrolysis and enzyme treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase (hereinafter, the treatment with an enzyme using these carbohydrates as a substrate is also referred to as "predetermined enzyme treatment"). More specifically, in step (A), a material containing vegetable protein is subjected to hydrolysis and a predetermined enzyme treatment to obtain an enzyme-treated product. The hydrolysis and the predetermined enzyme treatment may be performed simultaneously or sequentially. When these treatments are performed sequentially, either treatment may be performed first.
• the hydrolysis treatment is performed first or simultaneously, and it is more preferable that the hydrolysis is performed first.
• Plant protein-containing material The plant protein-containing material is a mixture that is subjected to hydrolysis and enzyme treatment and contains plant protein and starch.
• the plants from which the vegetable proteins are derived are not particularly limited, but examples include beans such as peas, soybeans, broad beans, chickpeas, and lentils; grains such as barley, wheat, oats, rice, buckwheat, barnyard millet, and foxtail millet; and nuts such as almonds, cashew nuts, hazelnuts, pecan nuts, macadamia nuts, pistachios, walnuts, Brazil nuts, peanuts, and coconuts.
• beans such as peas, soybeans, broad beans, chickpeas, and lentils
• grains such as barley, wheat, oats, rice, buckwheat, barnyard millet, and foxtail millet
• nuts such as almonds, cashew nuts, hazelnuts, pecan nuts, macadamia nuts, pistachios, walnuts, Brazil nuts, peanuts, and coconuts.
• One type of vegetable protein derived from these plants may be used alone, or two or more
• legume proteins from the viewpoint of obtaining an excellent balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or the effect of reducing the flavor of the raw materials in addition to the above viewpoints, preferred are legume proteins, more preferred are pea, broad bean, chickpea and lentil proteins, and even more preferred is pea protein.
• the content of vegetable protein in the vegetable protein-containing material is not particularly limited, but may be, for example, 0.1% by weight or more, 0.5% by weight or more, or 1% by weight or more. From the viewpoint of obtaining excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reducing effect in addition to the above viewpoint, it is preferably 3% by weight or more, more preferably 5% by weight or more, even more preferably 10% by weight or more, even more preferably 15% by weight or more, even more preferably 18% by weight or more, and particularly preferably 20% by weight or more.
• the content of vegetable protein in the vegetable protein-containing material is not particularly limited in its upper limit, but may be, for example, 50% by weight or less, or 40% by weight or less. From the viewpoint of obtaining excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reducing effect in addition to the above viewpoint, it is preferably 30% by weight or less, more preferably 25% by weight or less, and even more preferably 23% by weight or less.
• the plant from which the starch is derived may be the same as or different from the plant from which the vegetable protein is derived. From the viewpoint of obtaining an excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining, in addition to the above, excellent cohesiveness and/or the effect of reducing the flavor of the raw material, the plant from which the starch is derived is preferably the same as the plant from which the vegetable protein is derived.
• the starch content in the vegetable protein-containing material is not particularly limited, but may be, for example, 0.01% by weight or more. From the viewpoint of obtaining excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint, it is preferably 0.05% by weight or more or 0.1% by weight or more, more preferably 0.3% by weight or more, even more preferably 0.5% by weight or more, even more preferably 0.7% by weight or more, and particularly preferably 0.9% by weight or more.
• the starch content in the vegetable protein-containing material is not particularly limited in its upper limit, but may be, for example, 10.0% by weight or less.
• the manufacturing method of the present invention is excellent in improving hardness and stretchability, it can effectively improve hardness even when the starch content is relatively low.
• the upper limit of the range of the starch content in the material to be subjected to the enzyme reaction is preferably 5.0% by weight or less, more preferably 3.0% by weight or less, even more preferably 2.0% by weight or less, even more preferably 1.5% by weight or less, and particularly preferably 1.3% by weight or less.
• the ratio of vegetable protein to starch is determined by the content of each component, but from the viewpoint of obtaining excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reducing effect in addition to the above viewpoint, it is preferably 0.01 or more, more preferably 0.02 or more, even more preferably 0.03 or more, and even more preferably 0.04 or more.
• the upper limit of this ratio is preferably 0.09 or less, even more preferably 0.07 or less, and even more preferably 0.06 or less.
• the vegetable protein-containing material may contain any ingredient used in vegetable cheese (hereinafter also referred to as "other ingredient") as ingredients other than vegetable protein and starch.
• other ingredient include water, organic acids, vegetable oils and fats, thickening polysaccharides, salt, calcium salts, etc., and one or more of these ingredients may be contained in the vegetable protein-containing material.
• the vegetable protein-containing material typically contains water as another ingredient.
• the vegetable protein-containing material contains an organic acid and water among the other ingredient components described above.
• the organic acid may be mixed with the enzyme-treated product together with the starch in step (B) instead of being included in the vegetable protein-containing material in this step (A).
• the organic acid is included in the vegetable protein-containing material in this step (A) when this step (A) and the step (B) described later are performed in this order.
• the organic acid is not particularly limited, but examples thereof include lactic acid, citric acid, acetic acid, succinic acid, etc. These organic acids may be used alone or in combination of two or more kinds. Among these organic acids, lactic acid is preferred.
• the content of the organic acid in the material is not particularly limited, but from the viewpoint of obtaining an excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or the effect of reducing the flavor of the raw material in addition to the above, it is, for example, 0.1 to 1% by weight, more preferably 0.3 to 0.5% by weight.
• the water content in the material is not particularly limited, but from the viewpoint of obtaining a good balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining good cohesiveness and/or raw material flavor reduction effect in addition to the above, for example, 50 to 90% by weight or 60 to 85% by weight, preferably 65 to 80% by weight, more preferably 70 to 75% by weight.
• components other than organic acids and water are not included in the vegetable protein-containing material when this step (A) and the step (B) described below are carried out in this order.
• the present invention does not exclude cases where the components other than the organic acids and water are included in the vegetable protein-containing material.
• the components other than the organic acids and water can be included in the vegetable protein-containing material. More specific examples of vegetable oils and fats, thickening polysaccharides (other than starch), starch, salt, and calcium salts are described in detail in "1-2. Step (B)".
• Preferred specific forms of materials containing vegetable protein include mixtures prepared by mixing vegetable raw materials (organs or parts of the plant from which the vegetable protein is derived), dried powders thereof, or processed raw materials from which the vegetable protein content has been increased by removing at least a portion of the components other than vegetable protein, with other material components (preferably water and organic acid).
• the means of hydrolysis treatment is not particularly limited as long as it is a means capable of hydrolyzing proteins, and may be either an enzyme treatment or a chemical treatment.
• an enzyme treatment is preferably used as the means of hydrolysis treatment.
• any enzyme having a protein hydrolysis action may be used without any particular limitation.
• a protease is preferably used.
• the protease refers to an endopeptidase.
• the protease may be derived from any organism, and examples thereof include proteases derived from filamentous fungi such as those of the genera Aspergillus, Mucor, Neurospora, Penicillium, Rhizomucor, Rhizopus, and Sclerotinia; proteases derived from yeasts of the genus Saccharomyces; proteases derived from bacteria such as those of the genus Bacillus and Geobacillus; and proteases derived from actinomycetes of the genus Streptomyces. These proteases may be used alone or in combination of two or more kinds.
• proteases from the viewpoint of obtaining an excellent balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or the effect of reducing the flavor of raw materials in addition to the above viewpoint, it is preferable to use a protease derived from a filamentous fungus and/or a protease derived from a bacteria, and it is more preferable to use a combination of a protease derived from a filamentous fungus and a protease derived from a bacteria.
• protease derived from a filamentous fungus from the viewpoint of obtaining an excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or an effect of reducing the flavor of raw materials in addition to the above viewpoint, preferably a protease derived from the genus Aspergillus is used, more preferably a protease derived from Aspergillus oryzae or Aspergillus niga, and even more preferably a protease derived from Aspergillus oryzae.
• proteases derived from Bacillus stearothermophilus, Bacillus licheniformis, Bacillus amyloliquefaciens, and these Geobacillus genus are preferably used, and proteases derived from Geobacillus stearothermophilus are more preferably used.
• the amount of protease used is not particularly limited, but may be, for example, 5 to 300,000 U, 50 to 25,000 U, 100 to 20,000 U, or 240 to 10,000 U per gram of vegetable protein. From the viewpoint of obtaining excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint, the amount of protease used may be preferably 400 to 8,000 U, more preferably 700 to 6,000 U, and even more preferably 1,100 to 3,600 U, 1,100 to 2,900 U, 1,100 to 2,300 U, 1,150 to 1,800 U, or 1,200 to 1,500 U per gram of vegetable protein.
• the amount of filamentous fungus-derived protease used is not particularly limited, but can be used so that the protease activity (pH 3.0) per gram of vegetable protein is, for example, 10 to 200,000 U, 100 to 100,000 U, or 190 to 20,000 U.
• the protease activity is preferably 300 to 10,000 U, 400 to 7,500 U, more preferably 500 to 5,000 U, even more preferably 900 to 3,000 U, 900 to 2,500 U, 900 to 2,000 U, 900 to 1,500 U, or 900 to 1,000 U.
• the amount of bacterial protease used is not particularly limited, but it can be used so that the protease activity (pH 8.0) per gram of vegetable protein is, for example, 5 to 60,000 U, 30 to 10,000 U, or 50 to 6,000 U. From the viewpoint of obtaining an excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above, it can be used so that the amount is preferably 100 to 3,000 U, more preferably 200 to 1,000 U, and even more preferably 250 to 600 U, or 250 to 300 U.
• the ratio of the amounts of the fungal protease and the bacterial protease used is determined according to the amount of each of the above proteases used.
• the amount of bacterial protease used per 1 U of fungal protease is preferably 0.05 to 5 U, 0.1 to 3 U, more preferably 0.15 to 2 U, even more preferably 0.2 to 1 U, and even more preferably 0.25 to 0.4 U.
• Protease activity is measured by the Folin method using casein as a substrate.
• protease activity is measured by carrying out an enzyme reaction using casein as a substrate in a standard manner, with the amount of enzyme that causes an increase in the amount of Folin's test solution color substance equivalent to 1 ⁇ g of tyrosine per minute being defined as 1 unit (1 U).
• the conditions for hydrolysis such as processing conditions can be appropriately set by those skilled in the art depending on the hydrolysis means.
• those skilled in the art can appropriately set the conditions under which the protease effectively acts on the material containing vegetable protein.
• the temperature for the enzyme treatment with protease is not particularly limited and can be appropriately determined by a person skilled in the art depending on the optimum temperature of the enzyme used (or, in the case of simultaneous treatment with a specified enzyme, also taking into consideration the optimum temperature of the enzyme used in the specified enzyme treatment), and examples include 35 to 65°C, preferably 40 to 60°C, and more preferably 45 to 55°C.
• the pH (25°C) of the enzyme treatment with protease is not particularly limited and can be appropriately determined by a person skilled in the art depending on the optimum pH of the enzyme used (or, in the case of simultaneous treatment with a specified enzyme, also taking into consideration the optimum pH of the enzyme used in the specified enzyme treatment), and examples include 3.8 to 7.2, preferably 4 to 7, more preferably 4 to 6, and even more preferably 4.2 to 5.
• the time for enzyme treatment with the protease is not particularly limited and may be appropriately determined depending on the preparation scale of the vegetable protein-containing material, but may be, for example, 30 seconds to 24 hours, preferably 1 minute to 12 hours, more preferably 3 minutes to 6 hours, 5 minutes to 3 hours, 10 minutes to 2 hours, or 15 minutes to 1 hour.
• the enzyme treatment is carried out with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase. These enzymes may be used alone or in combination. Among these enzymes, from the viewpoint of obtaining excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint, glycosyltransferase and/or maltotriohydrolase are preferable, and glycosyltransferase is more preferable.
• glycosyltransferase refers to hexosyltransferase (E.C.2.4.1).
• examples of glycosyltransferase include cyclodextrin synthase (E.C.2.4.1.19), 1,4- ⁇ -glucan branching enzyme (E.C.2.4.1.18), 4- ⁇ -glucanotransferase (E.C.2.4.1.25), and the like. These glycosyltransferases may be used alone or in combination of two or more kinds.
• cyclodextrin synthase is preferred from the viewpoint of obtaining excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint.
• Cyclodextrin-forming enzymes derived from any organism can be used, including, for example, the genus Anoxybacillus, the genus Bacillus, the genus Geobacillus, the genus Paenibacillus, the genus Klebsiella, the genus Thermoanaerobacter, the genus Thremoa, and the genus Gluconobacter.
• Examples of cyclodextrin-forming enzymes include those derived from the genera Anoxybacillus caldiproteolyticus (including those previously classified as Geobacillus stearothermophilus) and Brevibacterium.
• Bacillus stearothermophilus Bacillus megaterium, Bacillus circulans, Bacillus macerans, Bacillus ohbensis, Bacillus
• Examples of cyclodextrin-forming enzymes include those derived from Bacillus clarkii, Geobacillus stearothermophilus, Paenibacillus macerans, and Klebsiella pneumoniae. These cyclodextrin-forming enzymes may be used alone or in combination.
• cyclodextrin-forming enzymes from the viewpoint of obtaining an excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint, cyclodextrin-forming enzymes derived from the genera Anoxybacillus, Bacillus, Paenibacillus, and Geobacillus are preferred, cyclodextrin-forming enzymes derived from Anoxybacillus caldiproteolyticus, Paenibacillus macerans, and Geobacillus stearothermophilus are more preferred, and cyclodextrin-forming enzymes derived from Anoxybacillus caldiproteolyticus are even more preferred.
• the amount of glycosyltransferase used is not particularly limited, but can be, for example, 0.5 to 15,000 U, or 5 to 10,000 U per gram of starch.
• the cyclodextrin-forming enzyme can be used in an amount of preferably 10 to 1000 U or 20 to 300 U, more preferably 30 to 150 U, even more preferably 35 to 90 U, 35 to 85 U, 35 to 80 U, 35 to 75 U, 35 to 70 U, 36 to 65 U, 37 to 60 U, 38 to 55 U, or 39 to 50 U per 1 g of starch, and further, from the viewpoint of obtaining an even more excellent raw material flavor reduction effect, the amount of the cyclodextrin-forming enzyme can be preferably 62 to 150 U, even more preferably 65 to 100 U, 70 to 95 U, 75 to 90 U, or 78 to 85 U per 1
• Cyclodextrin-forming enzyme activity is determined by carrying out an enzyme reaction using starch as a substrate in a standard manner, with 1 unit (U) being the amount of enzyme that reduces the blue iodine color of starch by 1% per minute.
• Maltotriohydrolase (maltotriose-producing amylase) (EC3.2.1.11) can be derived from any organism, and examples thereof include maltotriohydrolases derived from the genus Microbacterium and the genus Cellulosimicrobium. Examples of maltotriohydrolases from the genus Microbacterium include Microbacterium imperiale. These maltotriohydrolases may be used alone or in combination.
• maltotriohydrolases from the viewpoint of obtaining an excellent balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or an effect of reducing the flavor of raw materials in addition to the above viewpoint, it is preferable to use maltotriohydrolase derived from the genus Microbacterium, and it is more preferable to use maltotriohydrolase derived from Microbacterium impeliale.
• the amount of maltotriohydrolase used is not particularly limited, but may be, for example, 0.01 to 30 U or 0.05 to 10 U per gram of starch. From the viewpoint of obtaining an excellent balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effect in addition to the above viewpoint, maltotriohydrolase may be used at preferably 0.1 to 5 U, more preferably 0.3 to 3 U, even more preferably 0.5 to 2 U, even more preferably 0.8 to 1.8 U, and particularly preferably 1 to 1.5 U per gram of starch.
• Maltotriohydrolase activity is the enzyme activity where one unit is the amount of enzyme that produces reducing sugar equivalent to 1 ⁇ mol of glucose per minute using starch as a substrate in a standard enzyme reaction.
• ⁇ -amylase ⁇ -amylase derived from any organism can be used, and examples thereof include ⁇ -amylase derived from plants such as wheat, barley, and soybean, and ⁇ -amylase derived from microorganisms such as the genus Bacillus, Streptomyces, and Pseudomonas.
• ⁇ -amylase derived from the genus Bacillus includes Bacillus flexus, Bacillus megaterium, Bacillus polymyxa, and Bacillus circulans. These ⁇ -amylases may be used alone or in combination.
• ⁇ -amylase derived from Bacillus is preferred, more preferably ⁇ -amylase derived from Bacillus flexus, Bacillus megaterium, Bacillus polymyxa, or Bacillus circulans, and even more preferably ⁇ -amylase derived from Bacillus flexus.
• the amount of ⁇ -amylase used is not particularly limited, but may be, for example, 0.005 to 15 U or 0.025 to 5 U per gram of starch. From the viewpoint of obtaining a good balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining good cohesiveness and/or raw material flavor reduction effects in addition to the above, ⁇ -amylase may be used at preferably 0.05 to 2.5 U, more preferably 0.15 to 1.5 U, even more preferably 0.25 to 1 U, even more preferably 0.4 to 0.9 U, and particularly preferably 0.5 to 0.75 U per gram of starch.
• Beta amylase activity is measured by taking potato starch as a substrate and defining the amount of enzyme that increases the reducing power equivalent to 1 mg of glucose per minute as 1 unit (1 U).
• the temperature for the enzyme treatment using the enzyme that uses the above-mentioned carbohydrate as a substrate is not particularly limited and can be appropriately determined by a person skilled in the art depending on the optimum temperature of the enzyme used (or, in the case of simultaneous treatment with hydrolysis using a protease, also taking into consideration the optimum temperature of the protease), and examples of the temperature include 35 to 65°C, preferably 40 to 60°C, and more preferably 45 to 55°C.
• the pH (25°C) of the enzyme treatment using the enzyme that uses the above-mentioned carbohydrate as a substrate is not particularly limited and can be appropriately determined by a person skilled in the art depending on the optimum pH of the enzyme used (or, in the case of simultaneous treatment with hydrolysis using a protease, also taking into consideration the optimum pH of the protease), and examples of this include 3.8 to 7.2, preferably 4 to 7, more preferably 4 to 6, and even more preferably 4.2 to 5.
• the enzyme treatment time using the enzyme that uses the above-mentioned carbohydrate as a substrate is not particularly limited and may be appropriately determined depending on the preparation scale of the vegetable protein-containing material, and may be, for example, 30 seconds to 24 hours, preferably 1 minute to 12 hours, more preferably 3 minutes to 6 hours, 5 minutes to 3 hours, 10 minutes to 2 hours, or 15 minutes to 1 hour.
• the method for producing plant-based cheese of the present invention may also include a step of subjecting a material containing hydrolyzed plant protein to an enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase, and a step of mixing with starch.
• the material containing hydrolyzed plant protein is prepared by subjecting the material described in "1-1-1. Material containing plant protein" above to the treatment described in "1-1-2. Hydrolysis treatment” above. The material containing hydrolyzed plant protein is subjected to the predetermined enzymatic treatment described in "1-1-3. Enzyme treatment” above to obtain the enzyme-treated product.
• step (B) starch is mixed.
• Step (B) may be performed after step (A), simultaneously with step (A), or before step (A).
• step (B) starch is mixed with the enzyme-treated product obtained in step (A).
• an enzyme inactivation step described below starch is mixed with the inactivated enzyme-treated product.
• step (B) is performed simultaneously with step (A)
• starch is mixed with the vegetable protein-containing material to be treated in step (A).
• step (B) is performed before step (A)
• starch is mixed during the preparation of the vegetable protein-containing material.
• step (B) After the step (A) or simultaneously with the step (A); if the hydrolysis treatment and the predetermined enzyme treatment are carried out in this order in the step (A), it is preferable to carry out the step (B) after the step (A); if the hydrolysis treatment and the predetermined enzyme treatment are carried out simultaneously in the step (A), it is preferable to carry out the step (B) simultaneously with the step (A).
• a plant-based cheese dough is obtained by completing the steps (A) and (B).
• the starch is derived from any plant, but examples include cassava, potato, sweet potato, and kudzu. Starches derived from these plants may be used alone or in combination of two or more types of different origins.
• cassava starch (tapioca starch) and potato starch are preferable, and cassava starch (tapioca starch) is more preferable.
• the amount of starch to be mixed is not particularly limited as long as the effects of the present invention can be obtained, but the content in the plant-based cheese dough after mixing can be, for example, 4% by weight or more, and from the viewpoint of obtaining an excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or the effect of reducing the flavor of the raw materials in addition to the above viewpoint, the content can be preferably 5% by weight or more, more preferably 6% by weight or more, and even more preferably 7% by weight or more.
• the amount of starch to be mixed is not particularly limited, even in terms of its upper limit, but the content in the plant-based cheese dough after mixing can be, for example, 20% by weight or less. Furthermore, since the manufacturing method of the present invention is excellent in compatibility between hardness and thermal melting properties, even when the starch content is relatively low, it is possible to effectively achieve both hardness and thermal melting properties. From this perspective, the amount of starch to be mixed is preferably 17% by weight or less, more preferably 15% by weight or less, even more preferably 13% by weight or less, and even more preferably 12% by weight or less.
• the ratio of the vegetable protein used to prepare the enzyme-treated product in step (A) to the starch in this step is determined by the content of each of the above components, but the content of starch per part by weight of the vegetable protein used to prepare the enzyme-treated product is preferably 0.2 to 1 part by weight, more preferably 0.4 to 0.9 parts by weight, and even more preferably 0.6 to 0.7 parts by weight.
• step (B) in addition to the starch, any other ingredients used in the production of vegetable cheese can be blended.
• Such other ingredients include vegetable oils and fats, thickening polysaccharides, salt, calcium salts, and organic acids.
• Vegetable oils and fats are not particularly limited, but examples thereof include canola oil (rapeseed oil), coconut oil, corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, sunflower seed oil, safflower oil, flaxseed oil, palm oil, palm kernel oil, palm fruit oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, etc. These vegetable oils and fats may be used alone or in combination of two or more.
• canola oil canola oil (rapeseed oil), coconut oil, corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, sunflower seed oil, safflower oil, flaxseed oil, palm oil, palm kernel oil, palm fruit oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, etc.
• canola oil rapeseed oil
• coconut oil and sunflower oil
• canola oil rapeseed oil
• coconut oil and sunflower oil are preferable
• canola oil (rapeseed oil) and coconut oil are more preferable.
• the content in the vegetable cheese dough after mixing is, for example, 4 to 30% by weight, preferably 8 to 25% by weight, and more preferably 12 to 20% by weight.
• Thickening polysaccharides are not particularly limited, but examples thereof include locust bean gum, guar gum, carrageenan, xanthan gum, tragacanth gum, tamarind seed gum, pectin, gum arabic, curdlan, tara gum, gellan gum, ghatti gum, CMC (carboxymethylcellulose), sodium alginate, pullulan, etc., and preferably carrageenan.
• These thickening polysaccharides may be used alone or in combination of two or more.
• carrageenan is preferred from the viewpoint of achieving excellent compatibility between hardness and thermal melting properties, and/or from the viewpoint of achieving excellent cohesiveness and/or raw material flavor reduction effects in addition to the above.
• the content in the plant-based cheese dough after mixing is, for example, 0.1 to 2% by weight, more preferably 0.4 to 1.5% by weight, and even more preferably 0.6 to 1% by weight.
• the content in the plant-based cheese dough after mixing is, for example, 0.1 to 2% by weight, more preferably 0.5 to 0.7% by weight.
• the calcium salt is not particularly limited, but examples thereof include calcium gluconate, calcium lactate, calcium phosphate, etc. These calcium salts may be used alone or in combination of two or more. Among these calcium salts, calcium phosphate is preferred from the viewpoint of obtaining an excellent compatibility between hardness and thermal melting property, and/or from the viewpoint of obtaining excellent cohesiveness and/or an effect of reducing the flavor of raw materials in addition to the above viewpoint.
• the amount to be mixed is not particularly limited, but from the viewpoint of obtaining an excellent balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining excellent cohesiveness and/or raw material flavor reduction effects in addition to the above viewpoint, the content in the plant-based cheese dough after mixing is, for example, 0.5 to 4% by weight, more preferably 0.9 to 2.5% by weight, and more preferably 1.2 to 1.8% by weight.
• the organic acid is not particularly limited, but specific examples include lactic acid, citric acid, acetic acid, succinic acid, etc., as described above in “1-1-1. Materials containing vegetable protein.” These organic acids may be used alone or in combination. Of these organic acids, lactic acid is preferred.
• the amount of the organic acid to be mixed is not particularly limited, but from the viewpoint of obtaining a good balance between hardness and thermal melting properties, and/or from the viewpoint of obtaining good cohesiveness and/or an effect of reducing the flavor of raw materials in addition to the above viewpoint, the content in the plant-based cheese dough after mixing is, for example, 0.1 to 1% by weight, more preferably 0.3 to 0.5% by weight.
• Enzyme deactivation step In the present invention, when steps (A) and (B) are carried out in this order, it is preferable to include a step of deactivating the enzyme used in step (A) (hereinafter also referred to as "enzyme deactivation step") after step (A) and before step (B).
• the enzyme-treated product obtained in step (A) may be subjected to enzyme inactivation conditions.
• the enzyme inactivation conditions may be appropriately selected from conditions that denature the enzyme used in step (A) (specifically, an enzyme that uses carbohydrate as a substrate, or an enzyme and protease that uses carbohydrate as a substrate), and typically involve heat inactivation.
• Specific temperature conditions for heat inactivation may be set according to the thermal properties of the enzyme actually used in step (A), and may be, for example, 70°C or higher, preferably 80°C or higher, and more preferably 85°C or higher.
• the time for heat inactivation is not particularly limited, and may be, for example, 10 to 20 minutes.
• the production method of the present invention can further include any other steps for obtaining plant-based cheese, in addition to the above steps (A) and (B) and an enzyme inactivation step which is performed as necessary.
• step (B) Other steps include heating the plant-based cheese dough obtained in step (B) to cook it into a plant-based cheese, and cooling the resulting plant-based cheese.
• the heating temperature in the process of heating the plant-based cheese dough is, for example, 70 to 110°C, preferably 80 to 100°C, and more preferably 85 to 95°C.
• the heating time in the process of heating the plant-based cheese dough is not particularly limited, but may be, for example, 5 to 30 minutes, and preferably 10 to 20 minutes.
• the obtained plant-based cheese can be cooled while being packed in a container of an appropriate size.
• the temperature in the cooling process is not particularly limited, but can be, for example, 2 to 5°C.
• the present invention also provides a method for imparting hardness and hot meltability to plant-based cheese, which comprises carrying out steps (A) of hydrolyzing a material containing a plant protein and enzymatically treating the material with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase, and (B) of mixing starch in the production of plant-based cheese.
• Plant-based cheese The plant-based cheese obtained by the production method shown in the above section "1. Production method of plant-based cheese” has both hardness when not heated and hot meltability. Therefore, the present invention also provides a plant-based cheese obtained by a production method of plant-based cheese including the steps of (A) subjecting a material containing a plant protein to hydrolysis treatment and enzymatic treatment with an enzyme selected from the group consisting of glycosyltransferase, maltotriohydrolase, and ⁇ -amylase, and (B) mixing with starch.
• the hardness of the plant-based cheese of the present invention is, for example, 3.2N or more, preferably 4N or more, more preferably 4.5N or more, and even more preferably 4.7N or more.
• the upper limit of the hardness of the plant-based cheese of the present invention is not particularly limited, and examples include 8.5N or less, 8N or less, 7.5 or less, or 7 or less. Since the plant-based cheese of the present invention has excellent hardness when not heated, it may be shaped into shreds, dices, slices, or the like, as is done with general animal milk cheeses, or it may be in a block shape that can be cut appropriately when used. In other words, the form of the plant-based cheese of the present invention may be any form found in general hard and semi-hard animal milk cheeses.
• the hardness of the plant-based cheese of the present invention is excellent in thermal melting properties, so it can be used as a plant-based cheese for cooking by thermal melting.
• Protease activity measurement method 5 mL of 0.6% (v/w) casein solution (0.05 mol/L sodium hydrogen phosphate, pH 8.0 [for bacterial protease] or 0.7% (v/w) lactic acid, pH 3.0 [for fungal protease]) was heated at 37°C for 10 minutes, and then 1 mL of a sample solution containing protease was added and immediately shaken.
• 0.6% (v/w) casein solution 0.05 mol/L sodium hydrogen phosphate, pH 8.0 [for bacterial protease] or 0.7% (v/w) lactic acid, pH 3.0 [for fungal protease]
• This solution was left at 37°C for 10 minutes, and then 5 mL of trichloroacetic acid solution (containing 1.8% trichloroacetic acid, 1.8% sodium acetate, and 0.33 mol/L acetic acid [for bacterial protease] or containing 0.44 mol/L trichloroacetic acid [for fungal protease]) was added and shaken, and the solution was left at 37°C for 30 minutes again and filtered.
• trichloroacetic acid solution containing 1.8% trichloroacetic acid, 1.8% sodium acetate, and 0.33 mol/L acetic acid [for bacterial protease] or containing 0.44 mol/L trichloroacetic acid [for fungal protease]
• the first 3 mL of filtrate was removed, and the next 2 mL of filtrate was measured, and 5 mL of 0.55 mol/L sodium carbonate solution and 1 mL of Folin's reagent (1 ⁇ 3) were added, shaken well, and left at 37 ° C for 30 minutes.
• this solution enzyme reaction solution
• water was used as a control, and the absorbance AT at a wavelength of 660 nm was measured.
• the Folin's reagent was a solution prepared by the following method.
• 1mg/mL tyrosine standard stock solution (0.2mol/L hydrochloric acid) was measured at 1mL, 2mL, 3mL and 4mL, and 0.2mol/L hydrochloric acid solution was added to each to make 100mL. 2mL of each solution was measured, and 5mL of 0.55mol/L sodium carbonate solution and 1mL of Folin's test solution (1 ⁇ 3) were added, and the solution was immediately shaken and left at 37°C for 30 minutes. For each of these solutions, 2mL of 0.2mol/L hydrochloric acid solution was measured and the solution obtained by the same procedure as above was used as a control, and the absorbance A1, A2, A3 and A4 at a wavelength of 660nm were measured.
• the absorbance A1, A2, A3 and A4 were plotted on the vertical axis and the amount of tyrosine ( ⁇ g) in 2mL of each solution on the horizontal axis, and a calibration curve was created to determine the amount of tyrosine ( ⁇ g) per absorbance difference of 1.
• the reaction was stopped by adding 10 mL of hydrochloric acid test solution (0.1 mol/L). 10 mL of iodine/potassium iodide test solution (0.4 mmol/L) was added to 1 mL of this reaction solution and mixed to prepare the test solution.
• the iodine/potassium iodide test solution was prepared by dissolving 10.0 g of potassium iodide and 1.0 g of iodine in water to make 100 mL, and then diluting 200 times with water.
• a comparative solution was prepared by using water instead of the reaction solution, and the absorbance at 660 nm of the test solution and the comparative solution was measured.
• the amount of enzyme that reduces the blue iodine color of starch by 1% in 1 minute was defined as 1 unit (U), and was calculated from the following formula.
• the first solution was prepared by weighing out 25 g of sodium carbonate, 25 g of (+)-potassium sodium tartrate tetrahydrate, 20 g of sodium hydrogen carbonate, and 200 g of sodium sulfate, and adding water to dissolve them and make up to 1000 mL.
• the second solution was prepared by weighing out 30 g of copper (II) sulfate pentahydrate, adding it to 150 mL of water to dissolve it, adding 4 drops of sulfuric acid, and further adding water to make up to 200 mL.
• a solution obtained by mixing 25 volumes of the first solution and 1 volume of the second solution was used as an alkaline copper test solution.
• An enzyme was allowed to act on the soluble starch used as a substrate, and the resulting reducing sugar was colorimetrically quantified by the Somogyi-Nelson method.
• 0.5 mL of soluble starch solution and 0.4 mL of 0.1 mol/L acetic acid-sodium acetate buffer (pH 6.0) (containing 0.05 mol/ L CaCl2) were weighed into a 50 mL Nessler tube, shaken well, and left at 40 ⁇ 0.5°C for 10 to 15 minutes, after which 0.1 mL of sample solution was added and immediately shaken.
• Potato starch was used as the substrate, and was dried at 105°C for 2 hours. 1.0 g of the dried material was weighed out, 20 mL of water was added, and 5 mL of sodium hydroxide TS (2 mol/L) was gradually added while stirring to form a paste. Next, the mixture was heated in a water bath for 3 minutes while stirring, and then 25 mL of water was added.
• hydrochloric acid TS (2 mol/L) and hydrochloric acid TS (0.1 mol/L) were added to neutralize, and 10 mL of 1 mol/L acetic acid-sodium acetate buffer (pH 5.0) was added, and water was added to make 100 mL to prepare the substrate solution.
• Fehling's test solution is a solution prepared just before use by mixing 1 volume of copper solution and 1 volume of alkaline tartrate solution, which is made by measuring 34.66 g of fine crystals of copper (II) sulfate pentahydrate and dissolving it in water to make 500 mL, and 173 g of (+)-potassium sodium tartrate tetrahydrate and 50 g of sodium hydroxide and dissolving it in water to make 500 mL.
• the potassium iodide test solution (for ⁇ -amylase/invertase activity testing) was a 30% by weight potassium iodide solution.
• the sulfuric acid (1 ⁇ 6) was a 16.7% by weight sulfuric acid solution.
• a comparative solution was prepared in the same manner as in the preparation of the test solution, except that 10 mL of water was used instead of the substrate solution.
• the liberated iodine in the test solution and comparative solution was titrated with 0.05 mol/L sodium thiosulfate solution.
• the end point was determined as the time when 1-2 drops of soluble starch test solution were added as the titration approached the end point, and the resulting blue color disappeared.
• the amount of enzyme that produces an increase in reducing power equivalent to 1 mg of glucose per minute is defined as 1 unit (1 U), and was calculated using the following formula.
• ⁇ -Amylase activity measurement method 10 mL of 1% potato starch substrate solution (0.1 mol/L acetic acid (pH 5.0)) was heated at 37°C for 10 minutes, and then 1 mL of sample solution containing ⁇ -amylase was added and immediately shaken. This solution was left at 37°C for 10 minutes, and then 1 mL of this solution was added to 10 mL of 0.1 mol/L hydrochloric acid test solution and immediately shaken.
• Example 5 250 ml (50 parts by weight) of pure water (RO water) was placed in a Thermomix mixer, and while stirring at 50°C and speed 3, a1, c, b, and d in Table 5 were mixed with a21 and a22 in the amounts indicated, and incubated at 50°C for 30 minutes. The temperature was then raised to 90°C and the enzymes (a21 and a22) were inactivated for 10 minutes. Then, 100 g was filled into each aluminum container (bottom inner diameter: diameter 5 cm), covered with plastic wrap, and stored in a refrigerator (4°C) for 7 days. After storage, the vegetable cheese sample was taken out of the refrigerator (4°C) and immediately cut (diced) into 20 mm cubes. This resulted in a diced vegetable cheese.
• RO water pure water
• Example 6 250 ml (50 parts by weight) of pure water (RO water) was placed in a Thermomix mixer, and while stirring at 50 ° C. and speed 3, a1 and a21 in Table 5 were mixed in the indicated amounts, incubated at 50 ° C. for 30 minutes, and then heated to 90 ° C. and inactivated the enzyme (a21) for 10 minutes. The temperature was then lowered from the inactivation temperature (90 ° C.) to the reaction temperature (50 ° C.), c and a22 in Table 5 were added, and incubated at 50 ° C. for 30 minutes. The temperature was then raised to 90 ° C. and inactivated the enzyme (a22) for 10 minutes.
• RO water pure water
• the plant-based cheeses (Examples 1 to 4) produced by hydrolysis (protease treatment) and specific enzyme treatment (treatment with cyclodextrin-forming enzyme, maltotriohydrolase, and ⁇ -amylase) achieved both thermal melting properties and hardness.
• the plant-based cheeses (Examples 1 to 3) produced by treatment with cyclodextrin-forming enzyme and maltotriohydrolase as the specific enzyme treatment in particular also achieved excellent cohesiveness, further improving the processing characteristics.
• the plant-based cheeses (Examples 1 and 2) produced by hydrolysis (protease treatment) and the specified enzyme treatment (cyclodextrin-forming enzyme) were found to have a reduced flavor of the peas, which are the raw material, compared to the plant-based cheese (Comparative Example 1) produced without hydrolysis and the specified enzyme treatment.
• Example 5 As shown in the comparison between Example 1 and Example 5 in Table 5, when the hydrolysis treatment (treatment with a21) and the specified enzyme treatment (treatment with a22) are carried out simultaneously in step (A), the method in which step (A) and step (B) are carried out simultaneously (Example 5) shows improved hardness when not heated and excellent thermal meltability, and therefore shows an even better compatibility between hardness when not heated and thermal meltability.
• Example 6 As shown in the comparison between Example 1 and Example 6 in Table 5, when steps (A) and (B) are performed in this order, performing the hydrolysis treatment (treatment with a21) and the specified enzyme treatment (treatment with a22) in step (A) in this order (Example 6) improved hardness when not heated and also had excellent thermal melting properties, and therefore achieved an even better compatibility between hardness when not heated and thermal melting properties.

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