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
  • 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
  • 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
  • A23C11/06—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing non-milk 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
  • 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
  • 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
  • A23C11/103—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 containing only proteins from pulses, oilseeds or nuts, e.g. nut milk
• • 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
  • 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
  • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
  • A23L11/60—Drinks from legumes, e.g. lupine drinks
• • 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
  • A23L25/00—Food consisting mainly of nutmeat or seeds; Preparation or treatment thereof
  • A23L25/30—Mashed or comminuted products, e.g. pulp, pastes, meal, powders; Products made therefrom, e.g. blocks, flakes, snacks; Liquid or semi-liquid products
• • 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
• • 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
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
  • C12P21/00—Preparation of peptides or proteins
  • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
• • 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)
  • C12Y304/23—Aspartic endopeptidases (3.4.23)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
  • C12Y305/01—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in linear amides (3.5.1)
  • C12Y305/01044—Protein-glutamine glutaminase (3.5.1.44)

Definitions

• the present invention relates to a method for producing a processed vegetable protein-containing liquid composition, and more specifically, to a method for producing a vegetable protein-containing liquid composition processed so as to improve solubility.
• Patent Document 1 shows that by treating vegetable milk with a protein deamidating enzyme, aggregation can be suppressed when it is added to a high-temperature liquid food or drink.
• an object of the present invention is to provide a processing technique that exhibits an excellent solubilizing effect on a liquid composition containing vegetable protein.
• the present inventor has found that the solubility is dramatically improved by treating the vegetable protein-containing liquid composition with a protease and a protein deamidating enzyme. Furthermore, it was unexpectedly found that when a specific protease is used, the change in taste can be suppressed while improving the solubility.
• the present invention has been completed by further studies based on these findings.
• Item 1 A method for producing a processed vegetable protein-containing liquid composition, which comprises a step of treating the vegetable protein-containing liquid composition with a protease and a protein deamidating enzyme.
• Item 2. The production method according to Item 1, wherein the vegetable protein-containing liquid composition is treated with the protease and then with the protein deamidating enzyme.
• Item 3. Item 2. The production method according to Item 1 or 2, wherein the protease is a protease derived from filamentous fungi.
• Item 6. The production method according to any one of Items 1 to 3, wherein the protease is derived from Aspergillus oryzae.
• Item 5. Item 6.
• Item 6. Item 2. The production method according to Item 1 to 5, wherein the vegetable protein-containing liquid composition is vegetable milk.
• Item 7. A solubilizer for vegetable protein-containing liquid compositions, including proteases and protein deamidating enzymes.
• Item 8. A solubilizer containing a neutral protease and used for solubilizing a vegetable protein-containing liquid composition treated with a protein deamidating enzyme while suppressing a change in taste.
• Item 9. A solubilizer containing a protease derived from a filamentous fungus and used for solubilizing a vegetable protein-containing liquid composition treated with a protein deamidating enzyme while suppressing a change in taste.
• a processing technique that exhibits an excellent solubilizing effect on a liquid composition containing vegetable protein.
• the method for producing a processed vegetable protein-containing liquid composition of the present invention comprises treating the vegetable protein-containing liquid composition with a protease and a protein deamidating enzyme. It is a feature.
• the method for producing the processed vegetable protein-containing liquid composition of the present invention will be described in detail.
• the vegetable protein-containing liquid composition used in the present invention is not particularly limited as long as it is a liquid in which vegetable protein is dissolved and / or dispersed in water.
• Specific examples of the vegetable protein-containing liquid composition include (i) a liquid obtained by dispersing a dry powder of a material containing vegetable protein (preferably a vegetable food material) in water; (ii) a plant. A material containing a sex protein (preferably a vegetable food material) is crushed and dispersed in water, and if necessary, an insoluble matter derived from the skin of the food material can be centrifuged, filtered, filtered, a sieve, or the like.
• the vegetable protein is not particularly limited, but for example, nuts such as oat, barley, wheat, rice, buckwheat, hie, foxtail millet, tef, and quinoa; nuts such as soybeans, pea, rupin beans, sora beans, and chick beans. Proteins of plants (vegetable food materials) such as canary seeds, flaxseed, almonds, cashew nuts, hazelnuts, pecan nuts, macadamia nuts, pistachios, walnuts, Brazilian nuts, peanuts, coconuts, chestnuts, sesame seeds, pine nuts, etc. Can be mentioned. These vegetable proteins may be used alone or in combination of two or more.
• proteins of oats, peas, chickpeas, rice, and almonds are preferable from the viewpoint of further enhancing the solubility improving effect. Further, from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect when a filamentous fungus-derived protease is used as the protease, proteins of pea, chickpea, rice, and almond are preferable.
• a preferred example of a vegetable protein-containing liquid composition is vegetable milk prepared from a vegetable food material.
• Preferred examples of vegetable milk include oat milk, pea milk, chick bean milk, rice milk, and almond milk from the viewpoint of further enhancing the solubility improving effect.
• examples of the oat milk include oat milk in the form of heat-treated autoslurry, and the temperature of the heat treatment is, for example, 55 to 100 ° C, preferably 57 to 80 ° C, more preferably 59 to 70 ° C, and further. The temperature is preferably 59 to 65 ° C.
• the vegetable milk is preferably almond milk, chick bean milk, rice milk, and Almond milk can be mentioned.
• the protein content in the vegetable protein-containing liquid composition used in the present invention is not particularly limited.
• the protein content in the liquid composition containing vegetable protein examples include 0.1 to 8% by weight, preferably 0.5 to 5% by weight. More specifically, the content of the autoprotein in the liquid composition containing the autoprotein is preferably 0.5 to 4% by weight, more preferably 1 to 3% by weight, and the liquid containing the pea protein.
• the content of pea protein in the composition is preferably 1 to 5% by weight, more preferably 2 to 4% by weight, and the content of chick bean protein in the liquid composition containing chick bean protein is high.
• the content of rice protein in the liquid composition containing rice protein is preferably 0.5 to 4% by weight.
• the content of the almond protein in the liquid composition containing the almond protein is preferably 1 to 5% by weight, more preferably 2 to 4% by weight, and more preferably 1 to 3% by weight.
• the amount of water used per part by weight of the material containing vegetable protein is, for example, 2-30.
• the amount may be parts by weight, preferably 3 to 25 parts by weight, more preferably 6 to 12 parts by weight.
• the amount of water used per 1 part by weight of auto is preferably 6 to 12 parts by weight, for example. Is 8 to 10 parts by weight, more preferably 8.5 to 9.5 parts by weight.
• the vegetable protein-containing liquid composition of cereals it is preferable to use one treated with ⁇ -amylase from the viewpoint of improving the solubility of the processed vegetable protein-containing liquid composition produced by the present invention.
• the ⁇ -amylase is not particularly limited, and examples thereof include ⁇ -amylase derived from the genus Aspergillus and the genus Bacillus, preferably derived from the genus Bacillus, Bacillus subtilis, and Bacillus amyloliquefaci. Examples thereof include Bacillus amyloliquefaciens, Bacillus licheniformis, and more preferably ⁇ -amylase of Bacillus amyloliquefaciens.
• Examples of the amount of ⁇ -amylase used per 1 part by weight of rice grains include 5 to 300 U.
• the amount of ⁇ -amylase used per 1 part by weight of auto is, for example, 5 to 300 U, preferably 10 to 150 U, more preferably 20 to. 70U, more preferably 30 to 50U.
• the amount of enzyme that reduces the coloration of potato starch by iodine by 10% per minute is 1 unit (1U).
• the protein deamidating enzyme used in the present invention is an enzyme exhibiting an action of decomposing an amide group-containing side chain of a protein without cleavage of a peptide bond and cross-linking of a protein, and its type and origin, etc. Is not particularly limited. Further, as long as the above action is the main activity, it may further have an action of degrading the amide group-containing side chain of the protein accompanied by cleavage of the peptide bond and cross-linking of the protein.
• protein deamidating enzymes are enzymes that deamidate glutamine residues in proteins and convert them to glutamic acid (eg protein glutaminase), and enzymes that deamidate asparagine residues in proteins and convert them to aspartic acid (eg). Protein asparaginase).
• protein deamidating enzymes include the genus Chryseobacterium, the genus Flavobacterium, the genus Empedobacter, the genus Sphingobacterium, and the genus Aureobacterium. Protein deamides derived from the genus Aureobacterium or Myroides, the genus Lutimiclobium, the genus Agromyces, the genus Microbacterium, or the genus Leifsonia. These protein deamidating enzymes are known, and for example, JP2000-50887A, JP2001-218590A, WO2006 / 075772A1, WO2015 / 133590 and the like can be referred to. These protein deamidating enzymes may be used alone or in combination of two or more.
• a protein deamidating enzyme derived from the genus Chryseobacterium is preferable from the viewpoint of further improving the solubilizing effect or, in addition, further improving the ability to suppress changes in taste. More preferably, a protein glutaminase derived from the genus Chryseobacterium, more preferably a protein glutaminase derived from the Chryseobacterium proteinicum species, and even more preferably a protein derived from the Chryseobacterium proteoricum strain 9670. Glutaminase can be mentioned.
• the protein deamidating enzyme can be prepared from the culture solution of the microorganism from which the above protein deamidating enzyme is derived.
• Specific preparation methods include a method of recovering protein deamidating enzyme from the above-mentioned microbial culture solution or cells.
• the enzyme can be separated and / or purified after collecting the cells from the culture solution by filtration, centrifugation or the like in advance, if necessary.
• the cells were recovered from the culture solution in advance as needed, and then the cells were crushed by pressure treatment, ultrasonic treatment, etc. to expose the enzyme.
• the enzyme can be separated and / or purified.
• a known protein separation and / or purification method can be used without particular limitation, and for example, a centrifugation method, a UF concentration method, a salting out method, an ion exchange resin, or the like can be used.
• Various chromatographic methods using the above can be mentioned.
• the separated and / or purified enzyme can be pulverized by a drying method such as freeze-drying or vacuum drying, and pulverized by using an excipient and / or a drying aid suitable for the drying method. You can also do it.
• the separated and / or purified enzyme can also be liquefied by adding an appropriate additive and sterilizing by filtration.
• a commercially available product can also be used as the protein deamidating enzyme, and an example of a preferable commercially available product is the protein glutaminase "Amano" 500 (derived from Chryseobacterium proteolyticum species) manufactured by Amano Enzyme Co., Ltd.
• the amount of the protein deamidating enzyme used is not particularly limited, but examples of the amount used per 1 g of vegetable protein include 0.01 U or more. From the viewpoint of further improving the solubilization effect or, in addition, further improving the ability to suppress changes in taste, the amount of the protein deamidating enzyme used per 1 g of vegetable protein is preferably 0.05 U or more. 0.1U or more, more preferably 0.5U or more, still more preferably 0.8U or more, still more preferably 1U or more, still more preferably 1.5U or more, 2U or more, 2.5U or more, 2.8U or more. Be done.
• the upper limit of the amount of the protein deamidating enzyme used per 1 g of vegetable protein is not particularly limited, but for example, 40 U or less, 30 U or less, 20 U or less, 15 U or less, 10 U or less, 5 U or less, 4 U or less, 3.2 U or less. 3, 3U or less can be mentioned.
• the autoprotein of the protein deamidating enzyme is further improved from the viewpoint of further improving the solubilization effect or, in addition, further improving the inhibitory effect on taste change.
• the preferable amount to be used per 1 g is, for example, 0.1 U or more, 0.5 U or more or 1 U or more, preferably 1.5 U or more, more preferably 2 U or more, still more preferably 2.5 U or more, still more preferably 2.8 U or more.
• Preferred upper limits of the range of use of the protein deamidating enzyme per 1 g of autoprotein include, for example, 40 U or less, 30 U or less, 20 U or less, 10 U or less, 5 U or less, 4 U or less, or 3.2 U or less.
• the vegetable protein is pea protein, chick bean protein, rice protein, and / or almond protein, from the viewpoint of further improving the solubilization effect, or in addition, from the viewpoint of further improving the taste change inhibitory property.
• Preferred amounts of the protein deamidating enzyme used per 1 g of these plant proteins include, for example, 0.1 U or more, 0.5 U or more or 1 U or more, preferably 1.5 U or more, and more preferably 2 U or more.
• Preferred upper limits of the range of the amount of the protein deamidating enzyme used per 1 g of these plant proteins include, for example, 40 U or less, 30 U or less, 20 U or less, 10 U or less, 5 U or less, 4 U or less, or 3 U or less.
• the amount of the protein deamidating enzyme used per 1 g of the vegetable protein material for example, 0.001 U or more can be mentioned. From the viewpoint of further improving the solubilizing effect of the vegetable protein-containing liquid composition, or further improving the ability to suppress changes in taste, a preferable amount of the protein deamidating enzyme used per 1 g of the vegetable protein material. 0.005U or more, 0.01U or more, more preferably 0.05U or more, 0.1U or more, 0.15U or more, 0.3U or more, 0.35U or more, 0.4U or more, 0.5U or more. 1U or more, 1.5U or more can be mentioned.
• the upper limit of the amount of the protein deamidating enzyme used per 1 g of the vegetable protein material is not particularly limited, but for example, 20 U or less, 10 U or less, 5 U or less, 4 U or less, 3 U or less, 2 U or less, 1.5 U or less, 1 U.
• examples thereof include 0.6U or less, 0.5U or less, 0.45U or less, 0.4U or less, and 0.3U or less.
• 1 g of the protein deamidating enzyme auto 1 g from the viewpoint of further improving the solubilization effect or, in addition, further improving the taste change inhibitory property.
• a preferable amount to be used per (auto whole grain equivalent amount) for example, 0.05 U or more, preferably 0.1 U or more, more preferably 0.15 U or more, still more preferably 0.3 U or more, still more preferably 0.35 U or more.
• a preferable upper limit of the usage range of the protein deamidating enzyme per 1 g (auto whole grain equivalent amount) for example, 4U or less, 3U or less, 2U or less, 1U or less, 0.6U or less, 0.4U or less, or 0. .45U or less can be mentioned.
• 1 g of rice of a protein deamidating enzyme is used from the viewpoint of further improving the solubilizing effect or, in addition, further improving the inhibitory effect on taste change.
• a preferable amount to be used per (dry brown rice flour equivalent amount) for example, 0.01 U or more or 0.05 U or more, preferably 0.1 U or more, more preferably 0.15 U or more can be mentioned.
• Preferred upper limits of the amount of the protein deamidating enzyme used per 1 g include, for example, 2 U or less, 1 U or less, 0.5 U or less, or 0.3 U or less.
• 1 g of almond (almond powder equivalent amount) of the protein deamidating enzyme is used from the viewpoint of further improving the solubilizing effect or, in addition, further improving the ability to suppress changes in taste.
• Preferred per-use amounts include, for example, 0.05 U or more or 0.1 U or more, preferably 0.3 U or more, and more preferably 0.4 U or more.
• Preferred upper limits of the range of use of the protein deamidating enzyme per 1 g (almond powder equivalent amount) include, for example, 5U or less, 4U or less, 2U or less, 1U or less, or 0.6U or less.
• the protein deamidating enzyme per 1 g of chickpea from the viewpoint of further improving the solubilizing effect or, in addition, further improving the inhibitory effect on taste change.
• the amount include 0.05 U or more or 0.1 U or more, preferably 0.3 U or more, and more preferably 0.4 U or more.
• Preferred upper limits of the range of use of the protein deamidating enzyme per 1 g of chickpea include, for example, 5U or less, 4U or less, 2U or less, 1U or less, or 0.6U or less.
• the protein deamidating enzyme per 1 g of pea from the viewpoint of further improving the solubilizing effect or, in addition, further improving the inhibitory effect on taste change.
• Preferred upper limits of the range of use of the protein deamidating enzyme per 1 g of pea include, for example, 20 U or less, 10 U or less, 5 U or less, or 3 U or less.
• benzyloxycarbonyl-L-glutaminylglycine (Z-Gln-Gly) is used as a substrate, and the amount of the enzyme that favors 1 ⁇ mol of ammonia per minute is 1 unit (1U).
• protease used in the present invention is not particularly limited as long as it is an enzyme that hydrolyzes a peptide bond of a protein.
• protease examples include a filamentous fungus-derived protease and a bacterial-derived protease when the classification based on the origin is followed. Either one of these proteases may be used, or both may be used in combination.
• filamentous fungus-derived proteases include Aspergillus, Mucor, Neurospora, Pencillium, Rhizopus, and Rhizopus. Examples thereof include proteases derived from the genus Sclerotinia and the like. These filamentous fungus-derived proteases may be used alone or in combination of two or more.
• proteases derived from the genus Aspergillus include Aspergillus oryzae, Aspergillus niger, Aspergillus melleus, Aspergillus japonicus Aspergillus aspergillus aspergillus. ⁇ (Aspergillus kawachii) ⁇ (Aspergillus sojae) ⁇ (Aspergillus tamarii) ⁇ (Aspergillus foetidus) ⁇ (Aspergillus fumigatus) ⁇ (Aspergillus nidulans) ⁇ Aspergillus aculeatus, Aspergillus candius, Aspergillus flavus, Aspergillus saitoi, Aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus aspergillus as
• Bacterial-derived proteases include proteases derived from the genus Bacillus (or the genus Geobacillus). These bacterial-derived proteases may be used alone or in combination of two or more.
• protease derived from the genus Bacillus include Bacillus amyloliquefaciens, Bacillus cereus, Bacillus clausi, and Bacillus clausi. ), Bacillus lentus, Bacillus licheniformis, Bacillus stearothermophilus, Bacillus subtilis, Bacillus subtilis , And these proteases from the genus Geobacillus.
• proteases derived from the genus Bacillus or the genus Geobacillus
• a protease derived from Bacillus stearothermophilus is preferable, and a protease derived from Geobacillus is more preferable, from the viewpoint of further improving the solubilizing effect of the vegetable protein-containing liquid composition.
• Proteases derived from stearothermophyllus can be mentioned.
• a filamentous fungus-derived protease and a bacterial-derived protease are preferably mentioned from the viewpoint of further enhancing the solubility improving effect.
• a protease derived from filamentous fungi is preferable from the viewpoint of further obtaining the effect of suppressing the change in taste.
• the vegetable protein is an autoprotein, it is preferable to use either a filamentous fungus-derived protease or a bacterial-derived protease from the viewpoint of further enhancing the solubility improving effect and / or further obtaining the taste change suppressing effect, and the vegetable protein.
• the protein is pea protein, chick bean protein, rice protein, and / or almond protein, it is derived from filamentous fungi from the viewpoint of further improving the effect of suppressing taste change, or in addition, further enhancing the effect of improving solubility. It is more preferable to use a protease.
• a protease derived from the genus Aspergillus is preferable from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• a protease derived from Aspergillus oryzae is preferable from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• the vegetable protein is an autoprotein
• proteases derived from the genus Aspergillus it is preferably derived from Aspergillus niga or Aspergillus oryzae from the viewpoint of further improving the solubilizing effect of the liquid composition containing vegetable protein.
• Proteases are mentioned, more preferably Aspergillus oryzae derived proteases.
• proteases examples include acidic proteases, neutral proteases, and alkaline proteases according to the classification based on the optimum pH.
• the protease one of these proteases may be used, or two or more of these proteases may be used in combination.
• acidic proteases and neutral proteases are preferable.
• the protease is preferably an acidic protease (protease derived from Aspergillus or Niga) and a neutral protease (Aspergillus.
• Orize-derived protease and the like more preferably a neutral protease, and further preferably an Aspergillus oryzae-derived neutral protease.
• a neutral protease protease derived from Aspergillus oryzae, etc.
• Preferred examples include neutral protease derived from Aspergillus oryzae.
• the vegetable protein is pea protein, chick bean protein, rice protein, and / or almond protein, among proteases, a neutral protease is preferable from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• acidic proteases and in some cases (eg, the vegetable protein may be rice protein, almond protein, chick bean protein), preferably neutral proteases.
• proteases examples include serine proteases, metalloproteinases, thiol proteases, and aspartic proteases when according to the classification based on the catalytic mechanism.
• protease one of these proteases may be used, or two or more of these proteases may be used in combination.
• Proteases can be prepared by known methods. For example, it can be easily prepared by culturing a microorganism derived from a protease and separating the produced protease by a known means, a method using a gene recombination technique, or the like. Moreover, you may use a commercially available product as a protease. As commercially available proteases, Protease M “Amano” (acidic protease derived from Aspergillus oryzae), Protease HF “Amano” 150SD (acidic protease derived from Aspergillus oryzae), Protease A "Amano” manufactured by Amano Enzyme Co., Ltd.
• the amount of protease used is not particularly limited, and examples of the amount used per 1 g of vegetable protein include 0.0005 U or more and 0.001 U or more. From the viewpoint of further improving the solubilization effect or, in addition, further improving the ability to suppress changes in taste, the amount of the protease used per 1 g of vegetable protein is preferably 0.003 U or more, 0.005 U. 0.01U or more, 0.03U or more, 0.05U or more, 0.1U or more, 0.2U or more, 0.5U or more, 1U or more, 2U or more, 3U or more, 4U or more, 6U or more, 8U or more, 10U or more can be mentioned.
• the upper limit of the range of the amount of protease used per 1 g of vegetable protein is not particularly limited, but for example, 100 U or less, 90 U or less, 80 U or less, 70 U or less, 65 U or less, 60 U or less, 50 U or less, 40 U or less, 30 U or less, 20 U or less. , 15U or less, 10U or less, 8U or less, 7U or less, 6U or less.
• the vegetable protein is an autoprotein, for example, 0. 01U or more or 0.03U or more, preferably 0.05U or more, 0.1U or more, or 0.2U or more, more preferably 0.5U or more, 1U or more, or 2U or more, still more preferably 4U or more, 6U or more, 8U or more, or 10U or more can be mentioned.
• As a preferable upper limit of the range of the amount of protease used per 1 g of autoprotein for example, 100 U or less, 90 U or less, 80 U or less or 70 U or less, preferably 65 U or less, more preferably 40 U or less, from the viewpoint of further improving the solubilizing effect. Further preferably, it is 30 U or less, more preferably 20 U or less, still more preferably 15 U or less, 10 U or less, or 7 U or less.
• the protease is used from the viewpoint of further improving the solubilization effect and / or further improving the taste change inhibitory property.
• the preferable amount of these vegetable proteins to be used per 1 g is, for example, 0.0005 U or more, 0.003 U or more, preferably 0.005 U or more, 0.01 U or more, 0.03 U or more, more preferably 0.05 U or more, still more preferable.
• the range of the amount of the protease used per 1 g of these vegetable proteins for example, 50 U or less, 30 U or less, preferably from the viewpoint of further improving the solubilizing effect and / or further improving the taste change inhibitory property. 20U or less, 10U or less, more preferably 8U or less, still more preferably 6U or less.
• examples of the amount of protease used per 1 g of vegetable protein material include 0.0001 U or more and 0.00013 U or more. From the viewpoint of further improving the solubilization effect or, in addition, further improving the ability to suppress changes in taste, the amount of the protease used per 1 g of the vegetable protein material is preferably 0.0003 U or more, 0.
• the upper limit of the range of the amount of the protease used per 1 g of the vegetable protein material is not particularly limited, but for example, 20 U or less, 15 U or less, 11 U or less, 10 U or less, 8.7 U or less, 8 U or less, 5 U or less, 4 U or less, 3 U.
• the vegetable protein is an autoprotein
• Preferred usage amounts are, for example, 0.002U or more or 0.004U or more, preferably 0.007U or more, 0.01U or more, or 0.025U or more, more preferably 0.07U or more, 0.1U or more, or 0. 25U or more, more preferably 0.5U or more, 0.75U or more, 1U or more, or 1.3U or more.
• the amount of protease used per 1 g of auto for example, from the viewpoint of further improving the solubilization effect, for example, 20 U or less, 15 U or less or 10 U or less, preferably 8.7 U or less. It is preferably 5 U or less, more preferably 4 U or less, still more preferably 2.5 U or less, still more preferably 2 U or less, 1.3 U or less, or 0.9 U or less.
• the vegetable protein is rice protein
• 0.0001 U is used as a preferable amount of protease per 1 g (dry brown rice flour equivalent amount) of protease from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• 0.0003U or more is preferable, and 0.003U or more is more preferable.
• the vegetable protein is an almond protein
• 0.001 U or more is preferably used per 1 g (almond powder equivalent amount) of the protease from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• 0.003U or more preferably 0.006U or more or 0.008U or more.
• Preferred upper limits of the range of the amount of protease used per 1 g of almond (almond powder equivalent amount) include, for example, 2U or less, 0.5U or less, 0.1U or less, 0.05U or less, or 0.03U or less.
• the amount of protease used per 1 g of chick bean is preferably 0.0003 U or more, more preferably from the viewpoint of further enhancing the solubility improving effect and / or the effect of suppressing taste change. Is 0.003U or more, more preferably 0.008U or more, 0.05U or more, 0.1U or more, 0.5U or more, or 0.8U or more. Preferred upper limits of the range of the amount of protease used per 1 g of chickpeas are, for example, 10 U or less, 5 U or less, 3 U or less, 2 U or less, 0.5 U or less, 0.1 U or less, 0.05 U or less, or 0.03 U or less. Can be mentioned.
• the amount of protease used per gram of pea is preferably 0.008 U or more, more preferably 0., from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect.
• 05U or more more preferably 0.1U or more, 0.5U or more, 1U or more, 2U or more, or 3U or more.
• a preferable upper limit of the range of the amount of protease used per 1 g of pea is, for example, 50 U or less, and from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect, it is preferably 20 U or less, 15 U or less, 12 U or less, or Examples thereof include 10 U or less, more preferably 8 U or less, still more preferably 5 U or less, still more preferably 4 U or less, 2 U or less, 1.5 U or less, 0.5 U or less, or 0.3 U or less.
• the usage ratio of the protein deamidating enzyme and the protease is determined based on the above-mentioned amount of each enzyme, but from the viewpoint of further improving the solubilization effect, or in addition, further improving the ability to suppress changes in taste.
• the amount of the protease used per 1 U of protein deamidating enzyme is, for example, 0.0001 U or more, 0.0005 U or more, 0.001 U or more, more preferably 0.002 U or more, 0.003 U or more, 0.006 U.
• examples thereof include 0.6U or more, 1U or more, 1.3U or more, 1.5U or more, 1.8U or more, 2U or more, 2.6U or more, and 3.3U or more.
• the upper limit of the amount of protease protein deamidating enzyme used per 1U is, for example, 50U or less, 40U or less, 33U or less, 30U or less, 26U or less, 25U or less, 20U or less, 15U or less, 13U or less, 10U or less, 8U or less. , 7U or less, 5U or less, 3.5U or less, 3U or less, 2.3U or less.
• the vegetable protein is an autoprotein
• the amount of the protease protein deamidating enzyme used per 1 U for example, from the viewpoint of further improving the solubilization effect, for example, 50 U or less, 40 U or less, 30 U or less or 25 U or less, preferably 20 U or less, more preferably 13 U.
• examples thereof include more preferably 10 U or less, still more preferably 7 U or less, still more preferably 5 U or less, 3 U or less, or 2.3 U or less.
• the protease is used from the viewpoint of further improving the solubilization effect and / or further improving the taste change inhibitory property.
• Preferred amounts of protein deamidating enzyme used per 1 U are, for example, 0.0001 U or more, 0.0005 U or more or 0.001 U or more, more preferably 0.0015 U or more or 0.002 U or more, still more preferably 0.006 U or more, and one layer.
• 0.015U or more, 0.05U or more, 0.1U or more, 0.15U or more, 0.5U or more, 1U or more, 1.5U or more or 1.8U or more can be mentioned.
• a preferable upper limit of the range of the amount of the protease protein deamidating enzyme used per 1 U is, for example, 20 U or less, and is preferably 15 U or less, more preferably 15 U or less, from the viewpoint of further enhancing the solubility improving effect and / or the taste change suppressing effect. 10U or less, more preferably 8U or less or 7U or less, still more preferably 5U or less or 3.5U or less.
• Protease activity shall be measured by the folin method using casein as a substrate. That is, for the activity of the protease, an enzymatic reaction is carried out by a conventional method using casein as a substrate, and the amount of the enzyme that causes an increase in the forin test solution coloring substance corresponding to 1 ⁇ g of tyrosine is 1 unit (1 U).
• the order in which the protease and the protein deamidating enzyme are allowed to act is not particularly limited, and each enzyme is sequentially acted on in any order. It may be allowed to act or both enzymes may be allowed to act at the same time, but from the viewpoint of further improving the solubilization effect, preferably, the vegetable protein-containing liquid composition is treated with a protease and then treated with a protein deamide enzyme. It is particularly preferred to treat.
• the treatment temperature with the protease and the protein deamidating enzyme is not particularly limited, and can be appropriately determined by those skilled in the art depending on the optimum temperature of the enzyme used and / or the thermal characteristics of the vegetable protein-containing liquid composition.
• 40 to 70 ° C., preferably 48 to 62 ° C. may be mentioned.
• examples of the treatment temperature with the protein deamidating enzyme include, for example, 40 to 60 ° C, preferably 45 to 55 ° C, and more preferably 48 to 52 ° C.
• the temperature of the treatment with the protease is, for example, 40 to 70 ° C, preferably 50 to 65 ° C, and more preferably 58 to 62 ° C.
• the enzyme treatment reaction time of the vegetable protein-containing liquid composition is not particularly limited and may be appropriately determined according to the preparation scale of the composition, the timing of adding the enzyme, etc., but for example, 30 minutes or more, preferably 50 minutes or more. The above can be mentioned.
• the upper limit of the range of the enzyme treatment reaction time is not particularly limited, and examples thereof include 12 hours or less, 6 hours or less, 3 hours or less, 2.5 hours or less, or 2 hours or less.
• the treatment time with the protease includes, for example, 5 minutes to 2 hours, preferably 5 minutes to 1 hour, more preferably 35 to 55 minutes or 40 minutes to 1.5 hours.
• the treatment time with the protein deamidating enzyme is preferably 20 minutes to 6 hours, more preferably 40 minutes to 1.5 hours.
• the vegetable protein-containing liquid composition after the completion of the enzyme treatment is subjected to an enzyme deactivation step as necessary, cooled, and further subjected to a post-treatment step such as filtration as necessary, and the processed vegetable protein-containing liquid composition is subjected to. Obtained as.
• the obtained processed vegetable protein-containing liquid composition is prepared as a solid vegetable protein composition having an improved solubility in water or, in addition, suppressing a change in taste, through a drying step. You can also do it.
• the drying method is not particularly limited, and examples thereof include freeze-drying, vacuum drying, spray drying and the like. Examples of the shape of the solid vegetable protein composition include powder, fine granules, and granules.
• Solubilizer for Vegetable Protein-Containing Liquid Compositions Combinations of protein deamidating enzymes and proteases can improve the solubility of vegetable protein-containing liquid compositions. Accordingly, the present invention also provides a solubilizer for vegetable protein-containing liquid compositions, including proteases and protein deamidating enzymes.
• Solubilizer for vegetable protein-containing liquid composition treated with protein deamidating enzyme Neutral protease or filamentous fungus-derived protease is used to change the taste of vegetable protein-containing liquid composition treated with protein deamidating enzyme. It can be solubilized while being suppressed. Specifically, when a vegetable protein-containing liquid composition treated with a protein deamidating enzyme is solubilized with a neutral protease or a protease derived from a filamentous fungus, the protease treatment causes a change in taste that can normally occur. It can be solubilized without solubilization.
• the present invention is used to solubilize a vegetable protein-containing liquid composition treated with a protein deamidating enzyme, including a neutral protease or a filamentous fungus-derived protease, while suppressing taste changes.
• a protein deamidating enzyme including a neutral protease or a filamentous fungus-derived protease
• solubilizer examples include a solubilizer containing a neutral protease and used for solubilizing an autoprotein-containing liquid composition treated with a protein deamidating enzyme while suppressing a change in taste.
• solubilizer it can be used for solubilizing a vegetable protein-containing liquid composition treated with a protein deamidating enzyme containing a protease derived from filamentous fungi while suppressing a change in taste.
• a solubilizer in which the vegetable protein is a pea protein, a chick bean protein, a rice protein, and / or an almond protein.
• solubilizer has the property of further increasing the amount of protein that dissolves in water with respect to the vegetable protein-containing liquid composition, as compared with the case where it is solubilized only by the protein deamidating enzyme.
• specific embodiments of the solubilizer include a mode of treating a vegetable protein-containing liquid composition by simultaneously using a solubilizer and a protein deamidating enzyme, and a mode of treating a vegetable protein-containing liquid composition. It includes both an embodiment of treatment with an amidase and then a solubilizer, and an embodiment of a vegetable protein-containing liquid composition treated with a solubilizer and then treated with a protein deamidating enzyme.
• KSSD-8 (Crystase SD8): ⁇ -amylase derived from Bacillus amyloliquefaciens ⁇ PR-ASD (Protease A “Amano” SD): Neutral protease derived from Aspergillus oryzae ⁇ TH-PC10F (Samoase PC10F): Metal protease derived from Geobacillus stearothermophilus ⁇ PR-UFSD (acidic protease UF "Amano” SD): Aspergillus niger-derived acidic protease PR-HF150SD (protease HF "Amano" 150SD): Aspergillus oryzae-derived acidic protease PG-500 (Protein-glutaminase "Amano” 500) : Chryseobacterium proteolyticum-derived protein glutaminase (protein deamidating enzyme)
• Enzyme activity measurement method (1) Method for measuring protease activity 0.6% (v / w) casein solution (0.05 mol / L sodium hydrogen phosphate, pH 8.0 [in the case of TH-PC10F] or pH 6.0 [in the case of PR-ASD] ), Or 0.6% (v / w) casein solution (0.7% (v / w) lactic acid, pH 3.0 [for PR-UFSD or PR-HF150SD]) 5 mL is added at 37 ° C. for 10 minutes. After warming, 1 mL of a sample solution containing protease was added and immediately shaken. After allowing this solution to stand at 37 ° C.
• trichloroacetic acid test solution (1.8% trichloroacetic acid, 1.8% sodium acetate and 0.33 mol / L acetic acid-containing trichloroacetic acid [in the case of TH-PC10F], or 0. .44 mol / L trichloroacetic acid [for PR-ASD, PR-UFSD or PR-HF150SD]) 5 mL was added and shaken, left at 37 ° C. for 30 minutes again, and filtered.
• the amount of enzyme that causes an increase in the forin test solution color-developing substance corresponding to 1 ⁇ g of tyrosine in 1 minute was defined as 1 unit (1 U).
• Ammonia test Wako (Fujifilm Wako Pure Chemical Industries, Ltd.) was used for the solution obtained above to measure the amount of ammonia generated in the reaction solution.
• the ammonia concentration in the reaction solution was determined from a calibration curve showing the relationship between the ammonia concentration and the absorbance (630 nm) prepared using an ammonia standard solution (ammonium chloride).
• the activity of the protein deamidating enzyme was calculated from the following formula, with the amount of the enzyme producing 1 ⁇ mol of ammonia per minute as 1 unit (1 U).
• the amount of the reaction solution is 2.1
• the amount of the enzyme solution is 0.1
• Df is the dilution ratio of the enzyme solution.
• 17.03 is the molecular weight of ammonia.
• “Milk feeling” is a milky flavor. The results are shown in Table 1. Regarding the taste of processed oat milk when treated in the same manner without using any protease or protein deamidating enzyme, no creamy texture was observed with a rough texture. There was no change in taste ... +1 point Creamy was slightly reduced and slightly lighter ... -1 point Creamy was reduced and lighter was produced ... -2 points Milkiness was slightly reduced ... -1 Point The feeling of milk decreased ...-2 points
• Test Example 2 Processed oat milk was prepared in the same manner as in Test Example 1 except that the enzyme shown in Table 2 was used as a protease in the indicated amount, and solubilization evaluation and taste change inhibitory evaluation were performed. The results are shown in Table 2.
• Test Example 3 Processed oat milk was prepared in the same manner as in Test Example 1 except that the enzyme shown in Table 3 was used as a protease in the indicated amount, and solubilization evaluation and taste change inhibitory evaluation were performed. The results are shown in Table 3.

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