Method for producing processed plant protein-containing composition

Abstract

The purpose of the present invention is to provide a processing technique for improving the solubility of a liquid composition containing a vegetable protein. By treating a liquid composition containing a vegetable protein with a protein deamidase and a transglutaminase, the solubility of a liquid composition containing a vegetable protein or a liquid composition containing a vegetable protein obtained by redispersing a dried product thereof in a liquid can be improved.

Description

Technical Field

[0001] The present invention relates to a method for producing a processed vegetable protein-containing composition. More specifically, the present invention relates to a method for increasing the solubility of a liquid vegetable protein-containing composition. Background Art

[0002] Beverages rich in nutrients such as protein have been widely popular in the past because they allow for easy intake of nutrients. On the other hand, in recent years, due to the increase in vegetarians, allergy issues, and religious reasons, beverages made from soybeans, oats, almonds, etc., which are rich in plant proteins, have become widely popular as an alternative to animal milk, such as cow's milk.

[0003] On the other hand, when replacing milk protein raw materials with plant protein raw materials, the types of proteins, functionality, or components that constitute aroma and taste are different, so direct replacement is often not possible. Therefore, various technologies related to the processing of plant protein raw materials have been proposed. For example, Patent Document 1 states: α -Amylase and β - Amylase treatment of oat suspension to solve the high viscosity problem while maintaining protein and β -Oat dispersion of glucan. Patent Document 2 states that by treating vegetable milk with protein deamidase, dispersion stability and solubility are improved. On the other hand, transglutaminase is known as an enzyme for modifying protein. Transglutaminase is an enzyme that has the function of cross-linking proteins, and a technology related to the processing of dairy products has been proposed. For example, Patent Document 3 states that by treating raw milk with transglutaminase, the physical properties of yogurt and cheese can be improved.

[0004] Prior art literature Patent Literature Patent Document 1: U.S. Patent No. 6451369 Patent Document 2: International Publication No. 2022 / 071418 Patent Document 3: Japanese Patent Application Publication No. 2002-369653 Summary of the invention Technical problem to be solved by the invention From the viewpoint of nutritional value and storage stability, liquid compositions containing vegetable proteins are highly useful and can be expected to be used in various applications. On the other hand, the control of the solubility (hereinafter, solubility refers to the solubility of protein in water) of liquid compositions containing vegetable proteins has not been fully studied.

[0005] Therefore, an object of the present invention is to provide a processing technology for improving the solubility of a liquid composition containing vegetable protein.

[0006] The present inventors have conducted in-depth research and found that the solubility of the liquid composition containing vegetable protein can be improved by treating the liquid composition containing vegetable protein with protein deamidase and transglutaminase. In addition, the present inventors also found that after the liquid composition containing vegetable protein is temporarily dried, the liquid composition containing vegetable protein obtained by redispersing it in a liquid (specifically, water) has a tendency to decrease in solubility compared to the liquid composition containing vegetable protein that has not been dried. However, since the solubility improvement effect brought about by the treatment with protein deamidase and transglutaminase is high, the solubility of the liquid composition containing vegetable protein caused by redispersion after drying can also be effectively improved. Further, the present inventors found that when a liquid composition containing vegetable protein derived from a specific plant is selected as the treatment object among protein deamidase and transglutaminase, dispersion stability, emulsification, emulsification stability, foaming property, foam stability, oil retention, and / or smoothness are also improved. The present invention has been completed through further studies based on these findings.

[0007] That is, the present invention provides the invention of the following disclosed aspects.

[0008] Item 1. A method for producing a processed vegetable protein-containing composition, comprising the step of treating a liquid vegetable protein-containing composition with a protein deamidase and a transglutaminase to obtain the processed vegetable protein-containing liquid composition.

[0009] Item 2. The method for producing a processed vegetable protein-containing composition according to Item 1, further comprising the step of drying the processed vegetable protein-containing liquid composition to obtain a processed vegetable protein-containing dry composition for redispersion in a liquid (water and / or oil).

[0010] Item 3. A method for producing a processed composition containing vegetable protein according to Item 1 or 2, wherein the vegetable protein is a protein derived from plants, and the plants are selected from soybeans, peas, mung beans, broad beans, chickpeas, lentils, lupines, rice, barley, oats, sorghum, rye, corn, potatoes, hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, chia seeds and hemp seeds.

[0011] Item 4. The method for producing a processed vegetable protein-containing composition according to any one of Items 1 to 3, wherein a protein deamidase and a transglutaminase are allowed to act simultaneously.

[0012] Item 5. The method for producing a processed vegetable protein-containing composition according to any one of Items 1 to 4, wherein the activity ratio of protein deamidase to transglutaminase (protein deamidase activity: transglutaminase activity) is 0.05:0.95 to 0.9:0.1.

[0013] Item 6. A solubilizing agent for a liquid composition containing a vegetable protein, the solubilizing agent comprising a protein deamidase and a transglutaminase.

[0014] Item 7. The solubilizing agent according to Item 6, wherein the activity ratio of protein deamidase to transglutaminase (protein deamidase activity: transglutaminase activity) is 0.05:0.95 to 0.9:0.1.

[0015] Item 8. The solubilizing agent according to Item 6, wherein the solubilizing agent is used to improve the dispersion stability of a liquid composition containing a vegetable protein derived from oats.

[0016] Item 9. The solubilizing agent according to Item 8, wherein the activity ratio of protein deamidase to transglutaminase (protein deamidase activity: transglutaminase activity) is 0.05:0.95 to 0.9:0.1.

[0017] Item 10. A solubilizer according to Item 6 or 7, which is used to improve the emulsification of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from soybeans, peas, mung beans, broad beans, chickpeas, lentils, rice, corn, cashews, almonds, coconuts, pistachios, walnuts and chia seeds.

[0018] Item 11. A solubilizer according to Item 6 or 7, which is used to improve the emulsification stability of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from soybeans, peas, beans, lentils, rice, barley, sorghum, potatoes, hazelnuts, almonds, coconuts, peanuts, pistachios and hemp seeds.

[0019] Item 12. The solubilizer according to Item 6 or 7, which is used for improving the foaming property of a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from peas, mung beans, chickpeas and almonds.

[0020] Item 13. The solubilizing agent according to Item 6 or 7, which is used for improving the foam stability of a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from soybeans, broad beans, rice and potatoes.

[0021] Item 14. A solubilizer according to Item 6 or 7, which is used to improve the oil retention of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds.

[0022] Item 15. The solubilizer according to Item 6 or 7, which is used for improving the smoothness of a liquid composition containing a vegetable protein derived from a plant, wherein the plant is selected from the group consisting of soybeans, peas, mung beans, lupines, rice, and almonds.

[0023] Item 16. A plant protein-containing food or beverage comprising a processed plant protein-containing composition obtained by the production method according to any one of Items 1 to 5.

[0024] Item 17. (a) A method for improving the solubility of a liquid composition containing a vegetable protein, comprising the step of treating the liquid composition containing a vegetable protein with a protein deamidase and a transglutaminase to obtain a processed liquid composition containing a vegetable protein.

[0025] (b) The method according to (a) above, wherein the method is a method for solubilizing and improving dispersion stability, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from oats.

[0026] (c) The method according to (a), wherein the method is a method for solubilizing and improving emulsification properties, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, peas, mung beans, broad beans, chickpeas, lentils, rice, corn, cashews, almonds, coconuts, pistachios, walnuts and chia seeds.

[0027] (d) The method according to (a), wherein the method is a method for solubilizing and improving emulsion stability, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, peas, broad beans, lentils, rice, barley, sorghum, potatoes, hazelnuts, almonds, coconuts, peanuts, pistachios and hemp seeds.

[0028] (e) The method according to (a) above, wherein the method is a method for solubilizing and improving foaming properties, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from plants selected from peas, mung beans, chickpeas and almonds.

[0029] (f) The method according to (a) above, wherein the method is a method for solubilizing and improving foam stability, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, broad beans, rice and potatoes.

[0030] (g) The method according to (a), wherein the method is a method for solubilizing and improving oil retention, and the liquid composition containing vegetable protein is a solubilized liquid composition containing vegetable protein derived from plants, and the plants are selected from broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds.

[0031] (h) The method according to (a), wherein the method is a method for solubilizing and improving smoothness, and the liquid composition containing vegetable protein is a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, peas, mung beans, lupines, rice, and almonds.

[0032] Item 18. Use of protein deaminases and transglutaminases in: (a) solubilization of a liquid composition containing vegetable protein; (b) improving the solubilization and dispersion stability of a liquid composition containing vegetable protein derived from oats; (c) improving the solubilization and emulsification of a liquid composition containing vegetable protein derived from a plant selected from the group consisting of soybean, pea, mung bean, broad bean, chickpea, lentil, rice, corn, cashew, almond, coconut, pistachio, walnut and chia seed; (d) improving the solubilization and emulsification stability of a liquid composition containing vegetable protein derived from a plant selected from the group consisting of soybean, pea, bean, lentil, rice, barley, sorghum, potato, hazelnut, almond, coconut, peanut, pistachio and hemp seed; (e) improving the solubilization and foaming properties of a liquid composition containing vegetable protein derived from a plant selected from the group consisting of peas, mung beans, chickpeas and almonds; (f) improving the solubilization and foam stability of a liquid composition containing vegetable protein derived from a plant selected from the group consisting of soybean, broad bean, rice and potato; (g) solubilization and oil retention enhancement of a liquid composition containing vegetable protein derived from a plant selected from beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds; or (h) Solubilization and smoothness of a liquid composition containing vegetable protein derived from a plant selected from the group consisting of soybean, pea, mung bean, lupine, rice and almond are improved.

[0033] Item 19. Protein deamidase and transglutaminase are used as reagents for: (a) a solubilizing agent for a liquid composition containing vegetable protein; (b) an agent for improving the solubilization and dispersion stability of a liquid composition containing a vegetable protein derived from oats; (c) a solubilizing and emulsifying agent for a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from soybean, pea, mung bean, broad bean, chickpea, lentil, rice, corn, cashew, almond, coconut, pistachio, walnut and chia seed; (d) a solubilizing and emulsion stability enhancing agent for a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from soybean, pea, bean, lentil, rice, barley, sorghum, potato, hazelnut, almond, coconut, peanut, pistachio and hemp seed; (e) a solubilizing and foaming enhancing agent for a liquid composition containing vegetable protein derived from a plant, the plant being selected from peas, mung beans, chickpeas and almonds; (f) a solubilizing and foam stability enhancing agent for a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from the group consisting of soybean, broad bean, rice and potato; (g) a solubilizing and oil-retention enhancing agent for a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds; or (h) A solubilizing and smoothness enhancing agent for a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from the group consisting of soybean, pea, mung bean, lupine, rice and almond.

[0034] Effects of the Invention According to the present invention, a processing technology for improving the solubility of a liquid composition containing vegetable protein is provided. In addition, as a liquid composition containing vegetable protein, when a liquid composition containing vegetable protein derived from oats is selected, a processing technology for improving dispersion stability is also provided; as a liquid composition containing vegetable protein, when a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, mung bean, broad bean, chickpea, lentil, rice, corn, cashew, almond, coconut, pistachio, walnut and chia seed is selected, a processing technology for improving emulsification is also provided; as a liquid composition containing vegetable protein, when a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, broad bean, lentil, rice, barley, sorghum, potato, hazelnut, almond, coconut, peanut, pistachio and hemp seed is selected, a processing technology for improving emulsification stability is also provided; as a liquid composition containing vegetable protein, when a liquid composition containing vegetable protein derived from a plant selected from pea is selected, a processing technology for improving emulsification stability is also provided. In the case of a liquid composition containing vegetable protein derived from a plant selected from soybean, broad bean, rice and potato, a processing technology for improving foaming property is also provided; as a liquid composition containing vegetable protein, in the case of a liquid composition containing vegetable protein derived from a plant selected from soybean, broad bean, rice and potato, a processing technology for improving foam stability is also provided; as a liquid composition containing vegetable protein, in the case of a liquid composition containing vegetable protein derived from a plant selected from broad bean, chickpea, lentil, rice, potato, cashew, peanut, pistachio, walnut, chia seed and hemp seed, a processing technology for improving oil retention is also provided; as a liquid composition containing vegetable protein, in the case of a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, mung bean, lupine, rice and almond, a processing technology for improving smoothness is also provided. DETAILED DESCRIPTION

[0035] 1. Method for producing a processed vegetable protein-containing composition The method for producing a processed vegetable protein-containing composition of the present invention is characterized in that it comprises a step (enzyme treatment step) of treating a liquid composition containing vegetable protein with protein deamidase and transglutaminase. The solubility of the protein in the liquid composition containing vegetable protein can be improved by the enzyme treatment step, so according to the production method of the present invention, a vegetable protein-containing composition processed to improve solubility can be obtained. In addition, as an enzyme treatment object, when a liquid composition containing vegetable protein derived from a specific plant is selected, in addition to solubility, dispersion stability, emulsification, emulsion stability, foaming, foam stability, oil retention, and / or smoothness can be improved. Therefore, according to the production method of the present invention, in addition to solubility, a vegetable protein-containing composition processed to improve dispersion stability, emulsification, emulsion stability, foaming, foam stability, oil retention, and / or smoothness can be obtained. Below, the production method of the processed vegetable protein-containing composition of the present invention is described in detail.

[0036] 1-1. Liquid composition containing vegetable protein The liquid composition containing vegetable protein used in the present invention is not particularly limited as long as it is a liquid containing vegetable protein in water. Specific examples of the liquid composition containing vegetable protein include: (i) a liquid obtained by dispersing a dry powder of a food material containing vegetable protein in water; (ii) a liquid obtained by crushing and dispersing a food material containing vegetable protein in water, and removing insoluble matter such as skin of the food material by any method such as centrifugation, filtration, filter bag, sieve, etc. as needed; (iii) a liquid obtained by removing components other than vegetable protein from the liquid of (i) or (ii) above to increase the content of vegetable protein; (iv) a liquid obtained by mixing a dry powder prepared from any of the liquids (i) to (iii) above with water, etc. As a preferred example of the liquid composition containing vegetable protein, vegetable milk can be mentioned.

[0037] In addition, when describing "the content of a vegetable protein material" below, it means the dry weight of the component derived from the plant containing vegetable protein in the liquid composition containing vegetable protein.

[0038] There are no particular limitations on the plant protein, and examples thereof include: beans such as soybeans, peas, mung beans, broad beans, chickpeas, lentils, black beans, lupines, and kidney beans; cereals such as rice, wheat, barley, oats, sorghum, rye, buckwheat, barnyard grass, millet, teff, corn, and potatoes; nuts such as hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, pecan kernels, macadamia nuts, Brazil nuts, pili nuts, chestnuts, sesame seeds, and pine nuts; proteins (plant-derived proteins, i.e., natural proteins) contained in seeds such as chia seeds, hemp seeds (industrial hemp that does not contain tetrahydrocannabinol (THC)), quinoa, amaranth seeds, canary grass seeds, and flax seeds; chemical partial decomposition of the above proteins using acids, alkalis, and the like; chemically modified proteins and synthetic peptides using various reagents, etc.

[0039] In the present invention, the above-mentioned plant proteins may be used alone or in combination of two or more.

[0040] Among the above-mentioned plant proteins, from the viewpoint of further improving solubility, preferred examples include proteins derived from at least any one of soybeans, peas, mung beans, broad beans, chickpeas, lentils, lupins, rice, barley, oats, sorghum, rye, corn, potatoes, hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, chia seeds and hemp seeds; more preferred examples include proteins derived from at least any one of soybeans, broad beans, lupins, rice, rye, corn, potatoes, coconuts, peanuts and hemp seeds; further preferred examples include proteins derived from at least any one of lupins, corn, potatoes and peanuts; further preferred examples include proteins derived from at least any one of lupins, potatoes and peanuts; and particularly preferred examples include proteins derived from lupins.

[0041] Among the above-mentioned vegetable proteins, from the viewpoint of further improving dispersion stability, oats are preferably used.

[0042] Among the above-mentioned vegetable proteins, from the viewpoint of further improving the emulsifying properties, preferred examples include proteins derived from at least any one of soybeans, peas, mung beans, broad beans, chickpeas, lentils, rice, corn, cashews, almonds, coconuts, pistachios, walnuts and chia seeds, more preferred examples include proteins derived from at least any one of corn, coconuts and walnuts, further preferred examples include proteins derived from at least any one of corn and walnuts, and particularly preferred examples include proteins derived from corn.

[0043] Among the above-mentioned vegetable proteins, from the viewpoint of further improving the emulsion stability, preferred examples include proteins derived from at least any one of soybeans, peas, broad beans, lentils, rice, barley, sorghum, potatoes, hazelnuts, almonds, coconuts, peanuts, pistachios and hemp seeds; more preferred examples include proteins derived from at least any one of soybeans, peas, broad beans, lentils, rice, barley, sorghum, potatoes, coconuts and pistachios; further preferred examples include proteins derived from at least any one of soybeans, peas, broad beans, lentils, rice, sorghum and pistachios; particularly preferred examples include proteins derived from at least any one of lentils, rice and pistachios.

[0044] Among the above-mentioned plant proteins, from the viewpoint of further improving the foaming property, preferably, a protein derived from at least any one of peas, mung beans, chickpeas and almonds can be mentioned, more preferably, a protein derived from at least any one of chickpeas and almonds can be mentioned, and particularly preferably, a protein derived from almonds can be mentioned.

[0045] Among the above-mentioned vegetable proteins, from the viewpoint of further improving foam stability, preferred examples include proteins derived from at least any one of soybeans, broad beans, rice and potatoes, more preferred examples include proteins derived from at least any one of soybeans, broad beans and potatoes, and particularly preferred examples include proteins derived from soybeans.

[0046] Among the above-mentioned plant proteins, from the viewpoint of further improving the oil retention property, preferred examples include proteins derived from at least any one of broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds; more preferred examples include proteins derived from at least any one of lentils, potatoes, cashews, pistachios, chia seeds and hemp seeds; further preferred examples include proteins derived from at least any one of potatoes, cashews, pistachios and chia seeds; and particularly preferred examples include proteins derived from at least any one of potatoes and chia seeds.

[0047] Among the above-mentioned plant proteins, from the viewpoint of further improving smoothness, preferred examples include proteins derived from at least any one of soybeans, peas, mung beans, lupins, rice, and almonds, and more preferred examples include proteins derived from at least any one of soybeans, peas, mung beans, lupins, and rice.

[0048] The content of the vegetable protein in the liquid composition containing the vegetable protein is not particularly limited, and examples thereof include 0.01% to 50% by weight, 0.05% to 40% by weight, or 0.1% to 20% by weight, preferably 0.25% to 10% by weight, or 0.5% to 5.0% by weight, and more preferably 1.0% to 2.0% by weight, or 1.2% to 1.8% by weight.

[0049] In addition, the content of the vegetable protein material in the liquid composition containing vegetable protein is not particularly limited, and examples thereof include 0.05% to 50% by weight, 0.1% to 40% by weight, or 0.5% to 30% by weight, preferably 1% to 25% by weight, or 3% to 20% by weight, and more preferably 5% to 15% by weight, or 10% to 13% by weight.

[0050] It should be noted that, when the vegetable protein contained in the liquid composition containing vegetable protein is a protein of a starchy plant (preferably cereals), such a liquid composition containing vegetable protein is preferably a liquid composition pretreated with amylase. Examples of amylase include α -Amylase and β -Amylase.

[0051] As the α -Amylase is not particularly limited, and examples thereof include those derived from Aspergillus (e.g., Aspergillus oryzae, Aspergillus niger, etc.), Bacillus (e.g., Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, etc.) α -Amylase, preferably derived from Bacillus α - amylase, more preferably derived from Bacillus amyloliquefaciens α -Amylase.

[0052] about α The amount of the amylase used may be, for example, 0.5 U to 100 U, 1 U to 50 U, 2 U to 30 U, or 5 U to 20 U, preferably 8 U to 12 U, based on 1 g of starch contained in the liquid composition containing vegetable protein.

[0053] about α -Amylase activity, the amount of enzyme that reduces the iodine color of potato starch by 10% within 1 minute is defined as 1 unit (1U).

[0054] As the β -Amylase is not particularly limited, and examples thereof include those derived from plants (wheat, soybean) and those derived from Bacillus spp. β -Amylase, preferably derived from Bacillus β -Amylase, more preferably amylase derived from Bacillus flexus β -Amylase.

[0055] about β The amount of the -amylase used is, for example, 0.001 U to 5 U, 0.01 U to 1 U, 0.02 U to 0.50 U, or 0.03 U to 0.25 U, preferably 0.05 U to 0.15 U, relative to 1 g of starch contained in the liquid composition containing vegetable protein.

[0056] about β -Amylase activity is defined as the amount of enzyme that produces an increase in reducing power equivalent to 1 mg of glucose in 1 minute as 1 unit (1U).

[0057] The pH (25° C.) of the liquid composition containing vegetable protein may be appropriately determined depending on the optimal pH of protein deamidase and transglutaminase, and is, for example, 4.0 to 9.0, preferably 5.0 to 8.5, more preferably 5.5 to 8.0, and even more preferably 5.8 to 7.0.

[0058] 1-2. Protein deamidase The protein deamidase used in the present invention is not particularly limited in type or origin as long as it is an enzyme that decomposes the amide group-containing side chain of a protein without cleavage of peptide bonds or cross-linking of proteins.

[0059] Examples of protein deaminases include enzymes that deamidate glutamine residues in proteins and convert them into glutamate (e.g., protein glutaminase), and enzymes that deamidate asparagine residues in proteins and convert them into aspartic acid (e.g., protein asparaginase). Among these protein deaminases, protein glutaminase is preferred.

[0060] As a more specific example of protein deamidase, there can be mentioned: protein deamidase derived from Chryseobacterium, Flavobacterium, Empedobacter, Sphingobacterium, Aureobacterium, Myroides, Luteimicrobium, Agromyces, Microbacterium, or Leifsonia. These protein deamidase are well known, for example, JP2000-50887A, JP2001-218590A, WO2006 / 075772A1, WO2015 / 133590, etc. These protein deamidase can be used alone or in combination.

[0061] Among these protein deaminases, from the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming property, foam stability, oil retention and / or smoothness, preferably, a protein deamidase derived from the genus Chryseobacterium can be mentioned, more preferably, a protein glutaminase derived from the genus Chryseobacterium can be mentioned, further preferably, a protein glutaminase derived from the species Chryseobacterium proteolyticum can be mentioned, and more preferably, a protein glutaminase derived from Chryseobacterium proteolyticum 9670 strain can be mentioned.

[0062] Protein deamidase can be prepared from the culture solution of the microorganism that is the source of the above-mentioned protein deamidase. As a specific preparation method, a method for recovering protein deamidase from the culture solution or bacterial cell of the above-mentioned microorganism can be cited. For example, in the case of using a protein deamidase secretory microorganism, the bacterial cell can be recovered from the culture solution by filtering, centrifugation, etc. in advance as needed, and the enzyme is separated and / or purified. In addition, in the case of using a protein deamidase non-secreting microorganism, the bacterial cell can be recovered from the culture solution in advance as needed, and the enzyme is exposed by crushing the bacterial cell by pressure treatment, ultrasonic treatment, etc., and then the enzyme is separated and / or purified. As an enzyme separation and / or purification method, a known protein separation and / or purification method can be used without particular limitation, for example, centrifugation, UF concentration method, salting-out method, various chromatography methods using ion exchange resins, etc. can be cited. The enzyme obtained by separation and / or purification can be powdered by drying methods such as freeze drying and reduced pressure drying, and in addition, it can also be powdered using appropriate excipients and / or drying aids in the drying method. Alternatively, the isolated and / or purified enzyme may be liquefied by adding appropriate additives and sterilizing by filtration.

[0063] As the protein deamidase, commercially available products may be used, and examples of preferred commercial products include protein glutaminase (derived from Chryseobacterium proteolyticus) manufactured by AMANO ENZYME CO., LTD.

[0064] The amount of the protein deamidase used is not particularly limited, and as an amount per 1 g of vegetable protein, for example, 0.1 U or more can be cited. From the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming properties, foam stability, oil retention and / or smoothness, the amount of the protein deamidase used per 1 g of vegetable protein is preferably 0.5 U or more, or 1 U or more, more preferably 3 U or more, or 4 U or more, further preferably 10 U or more, further preferably 15 U or more, 30 U or more, 50 U or more, 70 U or more, 90 U or more, 130 U or more, or 170 U or more.

[0065] The upper limit of the range of the amount of protein deamidase used relative to 1 g of vegetable protein is not particularly limited, and examples thereof include 4000 U or less, 3000 U or less, 2000 U or less, 1000 U or less, 500 U or less, 400 U or less, 300 U or less, 200 U or less, 150 U or less, 100 U or less, 90 U or less, 80 U or less, 60 U or less, 50 U or less, 40 U or less, 30 U or less, or 25 U or less.

[0066] In addition, the amount of the protein deamidase used per 1 g of the vegetable protein material (in terms of dry weight) is, for example, 0.01 U or more. From the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming properties, foam stability, oil retention and / or smoothness, the amount of the protein deamidase used per 1 g of the vegetable protein material (in terms of dry weight) is preferably 0.05 U or more, or 0.1 U or more, more preferably 0.5 U or more, further preferably 0.8 U or more, further preferably 1 U or more, and further preferably 2 U or more. The upper limit of the range of the amount of protein deamidase used relative to 1 g of the vegetable protein material (dry weight conversion) is not particularly limited, and examples thereof include 400 U or less, 300 U or less, 200 U or less, 100 U or less, 50 U or less, 40 U or less, 30 U or less, 25 U or less, 20 U or less, 15 U or less, 10 U or less, 9 U or less, or 8 U or less.

[0067] Regarding the activity of protein deamidase, benzyloxycarbonyl-L-glutamine glycine (Z-Gln-Gly) was used as substrate and 1 μ The amount of enzyme per mol of ammonia is taken as 1 unit (1U).

[0068] 1-3. Transglutaminase The transglutaminase used in the present invention is an enzyme having transglutaminase activity (EC 2.3.2.13). Examples of transglutaminase include calcium-dependent transglutaminase that requires calcium to express its activity and calcium-independent transglutaminase that does not require calcium to express its activity. Transglutaminase is an enzyme that has the ability to catalyze the cleavage of glutamine residues in proteins. γ -Carboxyamide groups and lysine residues ε -An enzyme that cross-links proteins by acyl transfer reactions between amino groups.

[0069] Specific examples of the transglutaminase used in the present invention are not particularly limited. Specifically, examples of the transglutaminase include transglutaminase derived from microorganisms, and specifically, examples include transglutaminase derived from the genus Streptomyces such as Streptomyces mobaraensis, Streptomyces ladakanum, Streptomyces cinnamoneus, Streptomyces griseocarneus, Streptomyces lavendulae, or Streptomyces lydicus (for example, see Japanese Patent Application Laid-Open No. 64-27471), transglutaminase derived from Kutzneria albicans, and transglutaminase derived from Streptomyces lydicus. albida) and other Kutzneria genus (for example, refer to Japanese Patent Publication No. 2020-195397), transglutaminase derived from Longimycelium genus (Longimycelium tulufanense) and other Longimycelium genus (Longimycelium tulufanense); transglutaminase derived from mammals (for example, refer to Japanese Patent Publication No. 1-50382); transglutaminase derived from fish (for example, refer to Japanese Patent Publication No. 06-113844); recombinant (recombinant) transglutaminase obtained by recombinant DNA technology (for example, refer to Japanese Patent Publication No. 5-199883, Japanese Patent Publication No. 2004-97099); transglutaminase having a structure in which the pre-sequence peptide of transglutaminase is bound to the mature transglutaminase (for example, refer to International Publication No. 2009 / 101762), etc. These transglutaminases may be used alone or in combination of two or more.

[0070] Among these transglutaminases, from the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming properties, foam stability, oil retention and / or smoothness, preferably, a transglutaminase derived from a microorganism can be mentioned, more preferably, a transglutaminase derived from the genus Streptomyces can be mentioned, and even more preferably, a transglutaminase derived from the species Streptomyces mobaraensis can be mentioned.

[0071] The amount of transglutaminase used is not particularly limited, and as an amount relative to 1 g of vegetable protein, for example, 0.1 U or more can be cited. From the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming properties, foam stability, oil retention and / or smoothness, the amount of transglutaminase used relative to 1 g of vegetable protein is preferably 0.3 U or more, or 0.5 U or more, more preferably 1 U or more, 2.5 U or more, or 5 U or more, further preferably 8 U or more, further preferably 10 U or more, 20 U or more, 30 U or more, 40 U or more, 50 U or more, 60 U or more, 70 U or more, or 80 U or more.

[0072] The upper limit of the range of the amount of transglutaminase used relative to 1 g of vegetable protein is not particularly limited, and examples thereof include 4000 U or less, 3000 U or less, 2000 U or less, 1000 U or less, 500 U or less, 400 U or less, 300 U or less, 200 U or less, 150 U or less, 100 U or less, 90 U or less, 80 U or less, 60 U or less, 50 U or less, 40 U or less, 30 U or less, or 25 U or less.

[0073] In addition, the amount of transglutaminase used per 1 g of the vegetable protein material (in terms of dry weight) is, for example, 0.01 U or more. From the viewpoint of further improving the solubility-enhancing effect, or from this viewpoint and the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming properties, foam stability, oil retention and / or smoothness, the amount of transglutaminase used per 1 g of the vegetable protein material (in terms of dry weight) is preferably 0.05 U or more, or 0.1 U or more, more preferably 0.5 U or more, further preferably 0.8 U or more, further preferably 1 U or more, and even more preferably 2.5 U or more, or 3 U or more. The upper limit of the range of the amount of transglutaminase used relative to 1 g of the vegetable protein material (dry weight conversion) is not particularly limited, and examples thereof include 400 U or less, 300 U or less, 200 U or less, 100 U or less, 50 U or less, 40 U or less, 30 U or less, 20 U or less, 15 U or less, 10 U or less, 9 U or less, or 8 U or less.

[0074] The ratio of protein deamidase to transglutaminase used is determined based on the above-mentioned usage amounts of each enzyme. For example, the activity ratio of protein deamidase activity to transglutaminase activity (protein deamidase activity: transglutaminase activity) is 0.01:0.99 to 0.99:0.01. From the viewpoint of further improving the solubility-enhancing effect, or from the viewpoint of improving dispersion stability, emulsification, emulsification stability, foaming property, foam stability, oil retention and / or smoothness, a ratio of 0.05:0.95 to 0.9:0.1 is preferred. From the viewpoint of further improving the solubility-enhancing effect, or from the viewpoint of improving emulsification, emulsification stability, foaming property, foam stability, oil retention and / or smoothness, a ratio of 0.1:0.9 to 0.9:0.1 is preferred. The ratio of the dispersion stability of the polyols is preferably 0.05:0.1 to 0.1, more preferably 0.3:0.7 to 0.9:0.1, further preferably 0.45:0.55 to 0.8:0.2, further preferably 0.6:0.4 to 0.75:0.25, and particularly preferably 0.65:0.35 to 0.7:0.3; from the viewpoint of further improving the dispersion stability improving effect Starting from, preferably, the ratio is 0.05:0.95 to 0.75:0.25, more preferably, the ratio is 0.08:0.92 to 0.7:0.3 or 0.08:0.92 to 0.4:0.6, further preferably, the ratio is 0.08:0.92 to 0.25:0.75, and further preferably, the ratio is 0.08:0.92 to 0.15:0.85.

[0075] In addition, regarding the activity of transglutaminase, when benzyloxycarbonyl-L-glutamineglycine and hydroxylamine were used as substrates, 1 μ The enzyme activity of 1 mol of hydroxamic acid was set as 1 unit (U).

[0076] 1-4. Reaction conditions, etc. In the enzyme treatment step, a reaction of improving the solubility of protein in the liquid composition containing vegetable protein, or a reaction of improving the solubility and dispersion stability, emulsification, emulsion stability, foaming property, foam stability, oil retention and / or smoothness is carried out through the treatment.

[0077] The order in which the protein deamidase and the transglutaminase are allowed to act is not particularly limited, and the enzymes may be allowed to act sequentially in any order, or both enzymes may be allowed to act simultaneously. However, it is preferred that both enzymes be allowed to act simultaneously.

[0078] The conditions (temperature, pH, time, etc.) of the enzyme treatment step can be appropriately selected according to the characteristics of the liquid composition containing the enzyme and the vegetable protein, and the desired solubility improvement effect, or the degree of the solubility improvement effect and the effect of improving dispersion stability, emulsification, emulsion stability, foaming properties, foam stability, oil retention and / or smoothness.

[0079] The temperature for the enzyme treatment step is not particularly limited, and those skilled in the art can appropriately determine it based on the optimal temperature for using the enzyme and / or the thermal properties of the liquid composition containing vegetable protein, and for example, 30°C to 90°C can be cited, preferably 40°C to 80°C can be cited, more preferably 48°C to 70°C can be cited, and further preferably 50°C to 65°C can be cited.

[0080] The pH of the reaction system for the enzyme treatment step is not particularly limited, and can be appropriately determined by a person skilled in the art based on the optimal pH for the enzyme and / or the pH characteristics of the liquid composition containing the vegetable protein. The pH at 25° C. may be, for example, 2 to 13, preferably 5 to 11, and more preferably 5 to 10, 6 to 10, 7 to 9, or 6 to 8.

[0081] The time for performing the enzyme treatment step may be, for example, 0.1 to 96 hours, preferably 0.25 to 72 hours, and more preferably 0.5 to 30 hours.

[0082] The liquid composition containing vegetable protein after the enzyme treatment is subjected to an enzyme inactivation step as required, cooled, and further subjected to a post-treatment step such as filtration as required to obtain a processed liquid composition containing vegetable protein.

[0083] Furthermore, the obtained processed vegetable protein-containing liquid composition can also be prepared as a solid processed vegetable protein-containing composition (processed vegetable protein-containing dry composition) through a drying step.

[0084] In general, when a liquid composition containing vegetable protein is redispersed in a liquid (specifically, water) after temporary drying, the solubility of the liquid composition containing vegetable protein redispersed tends to decrease compared to the liquid composition containing vegetable protein that has not been dried. However, the solubility improvement effect brought about by the treatment with protein deamidase and transglutaminase is high, so even if the processed liquid composition containing vegetable protein is temporarily dried, the solubility of the liquid composition containing vegetable protein redispersed can be effectively improved. In addition, in general, when a liquid composition containing vegetable protein is redispersed in a liquid (specifically, water and / or oil) after temporary drying, the dispersion stability, emulsification, emulsification stability, foaming, foam stability, oil retention, and / or smoothness of the liquid composition containing vegetable protein redispersed tend to decrease compared to the liquid composition containing vegetable protein that has not been dried. However, the effect of improving the dispersion stability, emulsification, emulsion stability, foaming property, foam stability, oil retention, and / or smoothness brought about by the treatment with protein deamidase and transglutaminase is high. Therefore, even when the obtained processed liquid composition containing vegetable protein is temporarily dried, the dispersion stability, emulsification, emulsion stability, foaming property, foam stability, oil retention, and / or smoothness of the redispersed liquid composition containing vegetable protein can be effectively improved.

[0085] The drying method is not particularly limited, and examples thereof include freeze drying, vacuum drying, spray drying, etc. In addition, examples of the shape of the solid processed vegetable protein-containing composition (processed vegetable protein-containing dry composition) include powder, granules, and pellets.

[0086] 2. Solubilizer for liquid composition containing vegetable protein The combination of protein deamidase and transglutaminase can improve the solubility of protein in a liquid composition containing vegetable protein. Therefore, the present invention also provides a solubilizing agent for a liquid composition containing vegetable protein, which comprises protein deamidase and transglutaminase. The solubilizing agent for a liquid composition containing vegetable protein can be in the form of an enzyme preparation comprising protein deamidase and transglutaminase.

[0087] From the viewpoint of further improving solubility, the above-mentioned vegetable protein preferably includes proteins derived from at least any one of soybeans, peas, mung beans, broad beans, chickpeas, lentils, lupins, rice, barley, oats, sorghum, rye, corn, potatoes, hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, chia seeds and hemp seeds; more preferably, proteins derived from at least any one of soybeans, broad beans, lupins, rice, rye, corn, potatoes, coconuts, peanuts and hemp seeds; further preferably, proteins derived from at least any one of lupins, corn, potatoes and peanuts; further preferably, proteins derived from at least any one of lupins, potatoes and peanuts; particularly preferably, proteins derived from lupins.

[0088] The types and amounts of the components used in the solubilizing agent are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0089] In a preferred embodiment, the solubilizer of the liquid composition containing vegetable protein can be the following agents: an agent for solubilizing and improving dispersion stability (hereinafter referred to as a "solubilizer and dispersion stability improver"); an agent for other than solubilizing and improving emulsification (hereinafter referred to as a "solubilizer and emulsification improver"); an agent for solubilizing and improving emulsification stability (hereinafter referred to as a "solubilizer and emulsification stability improver"); an agent for solubilizing and improving foaming properties (hereinafter referred to as a "solubilizer and foaming improver"); an agent for solubilizing and improving foam stability (hereinafter referred to as a "solubilizer and foam stability improver"); an agent for solubilizing and improving oil retention (hereinafter referred to as a "solubilizer and oil retention improver"); or an agent for solubilizing and improving smoothness (hereinafter referred to as a "solubilizer and smoothness improver").

[0090] 2-1. Solubilizing and dispersion stability improving agents In a preferred embodiment, the combination of protein deamidase and transglutaminase can improve the dispersion stability in addition to solubilizing the liquid composition containing vegetable protein. Therefore, the present invention also provides a solubilizing and dispersion stability improving agent for a liquid composition containing vegetable protein, comprising protein deamidase and transglutaminase.

[0091] From the viewpoint of further improving dispersion stability, the vegetable protein preferably includes oat-derived protein.

[0092] The types and amounts of the components used in the above-mentioned solubilizing and dispersion stability improving agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0093] 2-2. Solubilizing and emulsifying agents The combination of protein deamidase and transglutaminase can improve the emulsification property of a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, mung bean, broad bean, chickpea, lentil, rice, corn, cashew, almond, coconut, pistachio, walnut and chia seed in addition to solubilizing. Therefore, the present invention also provides a solubilizing and emulsifying agent for a liquid composition containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0094] From the viewpoint of further improving the emulsifying properties, the above-mentioned vegetable protein preferably includes proteins derived from at least any one of corn, coconut and walnut, more preferably includes proteins derived from at least any one of corn and walnut, and particularly preferably includes proteins derived from corn.

[0095] The types and amounts of the components used in the above-mentioned solubilizing and emulsifying agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0096] 2-3. Solubilizer and emulsion stability enhancer The combination of protein deamidase and transglutaminase can improve the emulsion stability in addition to solubilization of a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, bean, lentil, rice, barley, sorghum, potato, hazelnut, almond, coconut, peanut, pistachio and hemp seed. Therefore, the present invention also provides a solubilizing and emulsion stability improving agent for liquid compositions containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0097] From the viewpoint of further improving the emulsion stability, the above-mentioned vegetable protein preferably includes proteins derived from at least any one of soybeans, peas, broad beans, lentils, rice, barley, sorghum, potatoes, coconuts and pistachios, more preferably includes proteins derived from at least any one of soybeans, peas, broad beans, lentils, rice, sorghum and pistachios, and particularly preferably includes proteins derived from at least any one of lentils, rice and pistachios.

[0098] The types and amounts of the components used in the above-mentioned solubilizing and emulsion stability improving agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0099] 2-4. Solubilizing and foaming enhancers The combination of protein deamidase and transglutaminase can improve the foaming property of a liquid composition containing vegetable protein derived from a plant selected from peas, mung beans, chickpeas and almonds in addition to solubilizing the liquid composition. Therefore, the present invention also provides a solubilizing and foaming property improving agent for liquid compositions containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0100] From the viewpoint of further improving the foaming property, the vegetable protein preferably includes a protein derived from at least one of chickpea and almond, and particularly preferably includes a protein derived from almond.

[0101] The types and amounts of the components used in the above-mentioned solubilizing and foaming property enhancing agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0102] 2-5. Solubilizer and foam stability enhancer The combination of protein deamidase and transglutaminase can improve foam stability in addition to solubilization of a liquid composition containing vegetable protein derived from a plant selected from soybean, broad bean, rice and potato. Therefore, the present invention also provides a solubilizing and foam stability improving agent for liquid compositions containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0103] From the viewpoint of further improving foam stability, the vegetable protein preferably includes proteins derived from at least any one of soybeans, broad beans, and potatoes, and particularly preferably includes proteins derived from soybeans.

[0104] The types and amounts of the components used in the above-mentioned solubilizing and foam stability improving agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0105] 2-6. Solubilizer and oil retention enhancer The combination of protein deamidase and transglutaminase can improve the oil retention of a liquid composition containing vegetable protein derived from a plant selected from broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds in addition to solubilizing. Therefore, the present invention also provides a solubilizing and oil retention improving agent for liquid compositions containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0106] From the viewpoint of further improving the oil retention property, the above-mentioned vegetable protein preferably includes proteins derived from at least any one of lentils, potatoes, cashews, pistachios, chia seeds and hemp seeds, more preferably includes proteins derived from at least any one of potatoes, cashews, pistachios and chia seeds, and particularly preferably includes proteins derived from at least any one of potatoes and chia seeds.

[0107] The types and amounts of the components used in the above-mentioned solubilizing and oil-retaining property-enhancing agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0108] 2-7. Solubilizing and smoothness enhancing agents The combination of protein deamidase and transglutaminase can improve the smoothness of a liquid composition containing vegetable protein derived from a plant selected from soybean, pea, mung bean, lupine, rice and almond in addition to solubilizing the liquid composition. Therefore, the present invention also provides a solubilizing and smoothness improving agent for a liquid composition containing vegetable protein derived from these specific plants, comprising protein deamidase and transglutaminase.

[0109] From the viewpoint of further improving the smoothness, the vegetable protein preferably includes a protein derived from at least any one of soybean, pea, mung bean, lupin, and rice.

[0110] The types and amounts of the components used in the above-mentioned solubilizing and smoothness-improving agents are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0111] 3. Solubilizing agent for liquid composition containing vegetable protein obtained by protein deamidation enzyme treatment Transglutaminase can solubilize the protein in the liquid composition containing vegetable protein obtained by treatment with protein deamidase. Therefore, the present invention also provides a solubilizing agent for the liquid composition containing vegetable protein obtained by treatment with protein deamidase, which contains transglutaminase. The solubilizing agent for the liquid composition containing vegetable protein obtained by treatment with protein deamidase can be in the form of an enzyme preparation containing transglutaminase.

[0112] It should be noted that, in the above-mentioned solubilizing agent, "solubilization" means that, compared with the case where the solubilization is performed only by protein deamidase, the liquid composition containing vegetable protein is given a property of further increasing the amount of protein dissolved in water (i.e., improvement of solubility). In addition, the specific use of the solubilizing agent includes a method of treating the liquid composition containing vegetable protein with a solubilizing agent and a protein deamidase at the same time, a method of treating the liquid composition containing vegetable protein with a protein deamidase and then treating it with a solubilizing agent, and a method of treating the liquid composition containing vegetable protein with a solubilizing agent and then treating it with a protein deamidase.

[0113] From the viewpoint of further improving solubility, the above-mentioned vegetable protein preferably includes proteins derived from at least any one of soybeans, peas, mung beans, broad beans, chickpeas, lentils, lupins, rice, barley, oats, sorghum, rye, corn, potatoes, hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, chia seeds and hemp seeds; more preferably, proteins derived from at least any one of barley, oats, sorghum, corn, potatoes, lupins, hazelnuts and hemp seeds; further preferably, proteins derived from at least any one of barley, corn, potatoes and hemp seeds; further preferably, proteins derived from at least any one of corn and hemp seeds; particularly preferably, proteins derived from corn.

[0114] The types and amounts of the components used in the solubilizing agent are as described in the above-mentioned section "1. Method for producing a processed vegetable protein-containing composition".

[0115] 4. Dispersion stability of a liquid composition containing vegetable protein obtained by protein deamidase treatment Sexual Enhancers Transglutaminase can improve the dispersion stability of a liquid composition containing vegetable protein treated with a protein deamidase. Therefore, the present invention also provides an agent for improving the dispersion stability of a liquid composition containing vegetable protein treated with a protein deamidase, comprising transglutaminase.

[0116] It should be noted that in the above-mentioned dispersion stability improver, "improvement of dispersion stability" means that for a liquid composition containing vegetable protein, compared with the case where the dispersion stability is improved only by protein deamidase, the property of further suppressing the sedimentation of insoluble matters contained in the liquid composition containing vegetable protein is imparted. In addition, in the specific usage mode of this dispersion stability improver, it includes any one of the following modes: a mode of treating a liquid composition containing vegetable protein by simultaneously using a dispersion stability improver and protein deamidase; a mode of treating a liquid composition containing vegetable protein with protein deamidase and then treating it with a dispersion stability improver; and a mode of treating a liquid composition containing vegetable protein with a dispersion stability improver and then treating it with protein deamidase.

[0117] From the viewpoint of further improving the dispersion stability, as the above-mentioned vegetable protein, preferably, proteins derived from oats can be cited.

[0118] In the above-mentioned dispersion stability improver, regarding the type and amount of components used, etc., as described in the column of "1. Method for producing a processed composition containing vegetable protein" above.

[0119] 5. Foods containing plant protein The food or drink containing vegetable protein of the present invention contains a processed composition containing vegetable protein obtained by the above-mentioned "1. Method for producing a processed composition containing vegetable protein". Regarding the processed composition containing vegetable protein, as described in the above-mentioned "1. Method for producing a processed composition containing vegetable protein".

[0120] Regarding the specific form of the food or drink containing vegetable protein of the present invention, it can be selected from any form of food or drink. In addition, when the food or drink containing vegetable protein of the present invention is provided for consumption in a fluid form such as a beverage, as its form, not only a liquid state (for example, a liquid beverage) can be cited, but also a dry state (for example, a powder beverage and a freeze-dried beverage, etc.) can be cited.

[0121] As a specific example of the food or drink containing vegetable protein, as long as it is an alternative food or drink category in which the animal protein raw material is replaced with a vegetable protein raw material, there is no particular limitation. For example, vegetable alternative milk, yogurt substitute, cheese substitute, ice cream substitute, cream substitute, coffee creamer substitute, alternative meat (including fish meat), alternative egg, alternative aquatic minced meat (the Japanese original of "aquatic minced meat" is "suirenri") products, etc. can be cited.

[0122] The food and drink that contains vegetable protein can use the composition that contains vegetable protein of processing, directly obtains or obtains through any cooking process.In such cooking process, select the cooking method corresponding to the form of the food and drink that contains vegetable protein, specifically, can carry out seasoning, form adjustment, molding, heating cooking, fermentation, freezing etc.

[0123] Example The present invention will be specifically described below with reference to examples, but the present invention should not be construed as being limited to the following examples.

[0124] [Enzymes used] In the following examples, the following enzymes were used.

[0125] [Table 1] [Enzyme activity assay] (1) Protein deamidase activity assay 0.1 mL of a sample solution containing protein deamidase was added to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, and the mixture was allowed to stand at 37°C for 10 minutes, followed by the addition of 1 mL of 0.4 M TCA solution to stop the reaction. As a blank, 1 mL of a 0.4 M TCA solution was added to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, and 0.1 mL of a sample solution containing protein deamidase was further added, followed by the addition of 1 mL of the solution, and the mixture was allowed to stand at 37°C for 10 minutes.

[0126] The amount of ammonia generated in the reaction solution was measured using Ammonia-test Wako (Fujifilm Wako Pure Chemical Industries, Ltd.). The ammonia concentration in the reaction solution was determined from a calibration curve showing the relationship between ammonia concentration and absorbance (630 nm) prepared using an ammonia standard solution (ammonium chloride).

[0127] Will generate 1 in 1 minute μ The activity of protein deamidase was calculated by the following formula, with the amount of enzyme per mol of ammonia as 1 unit (1U). In the formula, the amount of reaction solution is 2.1, the amount of enzyme solution is 0.1, and Df is the dilution ratio of the enzyme solution. In addition, 17.03 is the molecular weight of ammonia.

[0128] [Number 1] Protein deamidase activity (U / mL) = ammonia concentration in reaction solution (mg / L) × (1 / 17.03) × (reaction solution volume / enzyme solution volume) × (1 / 10) × Df (2) Transglutaminase activity assay The enzyme activity of transglutaminase was measured by the method described below using benzyloxycarbonyl-L-glutamine glycine and hydroxylamine as substrates.

[0129] A substrate solution was prepared by dissolving 2.42 g of 2-amino-2-hydroxymethyl-1,3-propanediol, 0.70 g of hydroxylammonium hydrochloride, 0.31 g of reduced glutathione, and 1.01 g of Z-Gln-Gly (benzyloxycarbonyl-L-glutamine glycine) in distilled water to a total volume of 100 mL (pH 6.0).

[0130] A color developing solution was prepared by mixing 30 mL of a 3 M hydrochloric acid solution, 30 mL of a 12 wt % trichloroacetic acid solution, and 30 mL of a 5 wt % iron (III) chloride solution.

[0131] The enzyme was diluted to an appropriate concentration using 200 mM MES buffer (pH 6.0) to prepare a sample solution.

[0132] In 10 μ Add 100 L of sample solution and mix μ After adding 100 L of substrate solution, react at 37°C for 10 minutes. μ After the reaction was stopped by adding L-chromogenic solution and the Fe complex was formed, the absorbance at 525 nm was measured. As a control, the sample solution that was preheated and inactivated was used for the same reaction and the absorbance was measured to find the difference in absorbance with the non-inactivated sample solution. γ -monohydroxamic acid was used as a standard curve instead of the sample solution to determine the amount of hydroxamic acid generated from the above absorbance difference. The activity of transglutaminase was defined as the amount of hydroxamic acid generated in 1 minute. μ 1 mol of hydroxamic acid is 1 unit (1U).

[0133] (3) α -Amylase activity assay Potato starch was used as a substrate, dried at 105°C for 2 hours in advance, 1.0 g of the dried product was weighed, 20 mL of water was added, and 5 mL of sodium hydroxide test solution (2 mol / L) was slowly added while stirring to form a paste. Then, after heating in a boiling water bath for 3 minutes while stirring, 25 mL of water was added. After cooling, hydrochloric acid test solution (2 mol / L) and hydrochloric acid test solution (0.1 mol / L) were added for neutralization, 10 mL of 1 mol / L acetic acid·sodium acetate buffer (pH 5.0) was added, and water was further added to reach 100 mL, which was used as a 1% potato starch substrate solution (0.1 mol / L acetic acid (pH 5.0)).

[0134] After heating 10 mL of 1% potato starch substrate solution (0.1 mol / L acetic acid (pH 5.0)) at 37°C for 10 minutes, add α -1mL of amylase sample solution, shake and mix immediately. After placing the liquid at 37°C for 10 minutes, add 1mL of the liquid to 10mL of 0.1mol / L hydrochloric acid test solution and shake and mix immediately. Next, weigh 0.5mL of the liquid, add 10mL of 0.0002mol / L iodine test solution (Japanese Pharmacopoeia), shake and mix, use water as a control, and measure the absorbance (AT) at a wavelength of 660nm. In addition, add 1mL of water instead of the sample solution, perform the same operation, and measure the absorbance (AB). α -Amylase activity was calculated according to the following formula, and the amount of enzyme that reduced the iodine color development of potato starch by 10% within 1 minute was defined as 1 unit (1U).

[0135] [Number 2] α -Amylase activity (U / g, U / mL) = (AB-AT) / AB×1 / W AT: absorbance of the reaction solution AB: absorbance of blank solution W: The amount of sample in 1 mL of sample solution (g or mL) (4) β -Amylase activity assay Potato starch was used as a substrate, dried at 105°C for 2 hours in advance, 1.0 g of the dried product was weighed, 20 mL of water was added, and 5 mL of sodium hydroxide test solution (2 mol / L) was slowly added while stirring to make a paste. Then, after heating in a boiling water bath for 3 minutes while stirring, 25 mL of water was added. After cooling, hydrochloric acid test solution (2 mol / L) and hydrochloric acid test solution (0.1 mol / L) were added for neutralization, 10 mL of 1 mol / L acetic acid sodium acetate buffer (pH 5.0) was added, and water was further added to reach 100 mL, which was used as a substrate solution.

[0136] Weigh 10 mL of substrate solution, heat at 37°C for 10 minutes, add 1 mL of sample solution and immediately shake and mix, heat at the same temperature for 10 minutes, further add 4 mL of Fehling's reagent and gently shake and mix, heat in a boiling water bath for 15 minutes, cool to below 25°C, add 2 mL of potassium iodide test solution (a solution prepared by dissolving 30 g of potassium iodide in 70 mL of water) and 2 mL of 3 mol / L sulfuric acid, and prepare a test solution. It should be noted that Fehling's reagent is a reagent prepared by weighing 34.66 g of fine crystals of copper sulfate (II) pentahydrate and dissolving them in water to prepare 500 mL of copper solution, and weighing 173 g of (+)-sodium potassium tartrate tetrahydrate and 50 g of sodium hydroxide and dissolving them in water to prepare 500 mL of alkaline tartrate solution, and mixing them at a ratio of 1 volume of copper solution to 1 volume of alkaline tartrate solution. In addition, use 10 mL of water instead of the substrate solution, and perform the same operation as the preparation of the test solution as a comparative solution. The free iodine of the test solution and the comparative solution was titrated with 0.05 mol / L sodium thiosulfate solution. When the titration was close to the endpoint, 1-2 drops of soluble starch test solution were added, and the point when the generated blue color disappeared was regarded as the endpoint.

[0137] The amount of enzyme that increases the reducing power of 1 mg of glucose in 1 minute is defined as 1 unit (1U) and the calculation is based on the following formula: β -Amylase activity.

[0138] [Number 3] β -Amylase activity (U / g, U / mL) = amount of glucose (mg) × 1 / 10 × 1 / M Amount of glucose (mg) = (ba) × 1.6 × f a: Titration value of enzyme reaction solution (mL) b: titration value of blank solution (mL) 1.6: 1mL of 0.05mol / L sodium thiosulfate solution is equivalent to 1.6mg of glucose 1 / 10: Unit conversion factor for reaction time (minutes) M: The amount of sample in 1 mL of sample solution (g or mL) f: Factor of 0.05 mol / L sodium thiosulfate solution (for quantitative use) [Plant protein materials used] In the following examples, the following vegetable protein materials were used.

[0139] Oat flour: "Premium oat flour" (manufactured by SlowFood), protein content 13.1% by weight, carbohydrate content 67.7% by weight [Test Example 1] (1) Manufacturing of processed oat milk 18.1 g of oatmeal powder was mixed with 150 g of water and suspended in a 200 mL conical flask. The suspension was adjusted to pH 6.5 and 10 U / g-starch was added. α -amylase and 0.09U / g-starch β -amylase, react at 54°C for 1 hour. Protein deamidase (PG) and transglutaminase (TG) with the activity ratio shown in Tables 2-1 and 2-2 were added in such a way that the total amount became 0.063% by weight, and after adjusting to pH 8.0, the reaction was carried out at 60°C for 1 hour. After the reaction, the enzyme was inactivated by heating at 95°C for 5 minutes. Centrifugation was performed at 1000 rpm for 1 minute, and the supernatant was recovered. The recovered supernatant was adjusted to pH 6.0 (25°C) to obtain processed oat milk (Examples 1 to 3, Comparative Examples 2 and 3). In addition, without adding enzymes, processed oat milk (Comparative Example 1) was obtained in the same manner.

[0140] (2) Characteristic test of processed oat milk The following property tests were performed on the obtained processed oat milk.

[0141] (2-1) Protein solubility (solubleness) Preparation method of BCA solution Prepare a BCA solution by thoroughly mixing 50 mL of BCA Protein Assay Reagent (Reagent A Pierce) and 1 mL of BCA Protein Assay Reagent (Reagent A Pierce).

[0142] Protein solubility determination method Weigh 4 mL of BCA solution, place it at 37±0.5℃ for 10 minutes, add 0.2 mL of sample diluent (50-fold diluted processed oat milk), and immediately shake to mix. Place the liquid at 37±0.5℃ for 30 minutes, and then cool it in running water (20℃~25℃). For this liquid, measure the absorbance (AT) at a wavelength of 562nm using water as a reference. In addition, place 4 mL of BCA solution at 37±0.5℃ for 10 minutes, add 0.2 mL of water and shake to mix, then perform the same operation to measure the absorbance (AB).

[0143] The albumin concentration Tmg in the sample dilution was determined from the absorbance difference (AT-AB) and the albumin standard curve. The protein solubility (mg / g) in the processed oat milk was determined based on the obtained albumin concentration Tmg. The results are shown in Table 2-1.

[0144] (2-2) Dispersion stability The processed oat milk was refrigerated and left to stand for 24 hours. At this time, the height of the entire liquid and the height of the sedimentation layer were measured respectively, and the dispersion stability was calculated based on the following formula. The higher the dispersion stability value, the higher the dispersion stability. The results are shown in Table 2-2.

[0145] [Number 4] Dispersion stability (%) = 100 × (height of sedimentation layer) / (height of the entire liquid) (3) Test results [Table 2-1] As shown in Table 2-1, although the solubility of the protein decreased when TG was used alone (Comparative Example 2), the effect of improving the solubility of the protein was significantly enhanced by combining TG with PG (Examples 1 to 3) compared to the case where PG was used alone (Comparative Example 3). For example, although only 1 / 5 (additional activity) of the amount of PG used in Comparative Example 3 was used in Example 1, and TG, which reduces the solubility of the protein, was used in an amount of about 9 times that of PG, the same protein solubility as that of Comparative Example 3 was achieved. In addition, although only a smaller amount of PG (additional activity) than that used in Comparative Example 3 was used in Examples 2 and 3, the protein solubility was improved compared to Comparative Example 3.

[0146] [Table 2-2] As shown in Table 2-2, in all of Comparative Examples 2 and 3 and Examples 1 to 3, although the total weight of PG and TG was the same, when PG and TG were combined (Examples 1 to 3), the effect of improving dispersion stability was observed.

[0147] [Test Example 2] (1) Test method In the same manner as in Example 3 of Test Example 1 (PG activity: TG activity = 0.67: 0.33), processed oat milk was prepared and the protein solubility and dispersion stability were measured. The amount of each enzyme added is shown in Table 3. The relative value of protein solubility and the relative value of dispersion stability were derived when the protein solubility and dispersion stability of Example 5 (retest of Example 3) were set to 1, respectively. The results are shown in Table 3.

[0148] (2) Test results [Table 3] As shown in Table 3, in any of Examples 4 to 6, improvement in protein solubility and improvement in dispersion stability were confirmed.

[0149] [Test Example 3] (1) Test method As shown in Table 4, except that the pH of the processed oat milk and the amount of each enzyme added were changed, the same process as in Comparative Example 1 (no enzyme), Comparative Example 3 (PG activity:TG activity=1:0) or Example 3 (PG activity:TG activity=0.67:0.33) of Test Example 1 was carried out to prepare processed oat milk and evaluate the dispersion stability. The results are shown in Table 4.

[0150] (2) Test results [Table 4] As shown in Table 4, in Example 7 in which the PG addition amount and the TG addition amount were only 18U and 9U, respectively, relative to 1g of protein, the dispersion stability was equivalent to that of Comparative Example 6 in which the PG addition amount was 180U relative to 1g of protein; in Example 9 in which the PG addition amount and the TG addition amount were only 0.9U and 0.45U, respectively, relative to 1g of protein, the dispersion stability was improved compared with that of Comparative Example 9 in which the PG addition amount was 1.8U relative to 1g of protein; in Example 11 in which the PG addition amount and the TG addition amount were only 18U and 9U, respectively, relative to 1g of protein, the dispersion stability was improved compared with that of Comparative Example 10 in which the PG addition amount was 180U relative to 1g of protein. Therefore, it can be confirmed that by using PG and TG in combination, the effect of significantly improving the dispersion stability can be obtained at any pH.

[0151] [Test Example 4] (1) Production of processed vegetable protein-containing compositions The vegetable protein material (powder. If necessary, the powder was crushed by a grinder to obtain the same particle size) shown in Table 5 was suspended in water to a 10% by weight ratio to prepare a liquid composition containing vegetable protein. In the case of using whole grain flour of cereals as the vegetable protein material, the water suspension of the whole grain flour was adjusted to pH 6.5, and 10 U / g-starch was added. α -amylase and 0.09U / g-starch β-amylase, and pre-treated at 54°C for 1 hour to prepare a liquid composition containing vegetable protein. Protein deamidase (PG) is added in an amount of 18U per 1g of protein, and transglutaminase (TG) is added in an amount of 9U per 1g of protein, and after adjusting the pH at 25°C to 6-7, the mixture is reacted at 50°C for 1 night. After the reaction, the mixture is heated at 100°C for 5 minutes to inactivate the enzyme, thereby obtaining a processed liquid composition containing vegetable protein. The processed liquid composition containing vegetable protein obtained is freeze-dried to obtain a processed dry composition containing vegetable protein (Examples 13 to 34). In addition, a processed dry composition containing vegetable protein (Comparative Examples 13 to 34 with subnumbers) is obtained by the same operation except that at least one of PG and TG is missing.

[0152] [Table 5] (2) Test on properties of liquid compositions containing vegetable protein redispersed in water The following property tests were performed on the obtained processed vegetable protein-containing dry composition.

[0153] (2-1) Protein solubility (solubleness) The obtained processed dry composition containing vegetable protein was redispersed in water to prepare a redispersion liquid containing 10% by weight of the dry composition, and allowed to stand at room temperature for 30 minutes. After standing, centrifuge at 15500×g for 5 minutes to recover the supernatant. The protein solubility (mg / mL) of the supernatant was measured using the method (2-1) of Test Example 1. In addition, the relative values ​​of the protein solubility of each embodiment (relative protein solubility value / relative to no enzyme) were derived when the protein solubility of the comparative example (“no enzyme”) prepared without using both PG and TG was set to 1. The higher the relative value of the protein solubility, the higher the solubilization effect (i.e., solubility improvement effect). The results are shown in Tables 6-1 to 6-4.

[0154] (2-2) Emulsification The processed vegetable protein-containing dry composition was redispersed in deionized water to prepare 30 mL of a redispersed liquid containing 1% by weight of protein. 30 mL of the redispersed liquid was mixed with 10 mL of canola oil and homogenized at 10,000 rpm for 2 minutes to prepare an emulsified composition. 50 mL of the emulsified composition was taken shortly after preparation. μ L was added to 5 mL of 0.1 wt% SDS solution. The turbidity (A0) was measured at an absorbance of 500 nm, and the emulsification (m 2 / g). In addition, relative values ​​of emulsification properties of each example were derived when the emulsification property of the comparative example ("no enzyme") prepared without using both PG and TG was set to 1 (relative emulsification property value / relative to no enzyme). The higher the relative emulsification property value, the higher the effect of improving emulsification properties. The results are shown in Tables 6-1 to 6-4.

[0155] [Number 5] Emulsification (m 2 / g) = (2 × 2.303 × A0) / (0.25 × protein weight) (2-3) Emulsion stability After the preparation in (2-2) above, 50% of the emulsified composition was left to stand for 10 minutes. μ L, added to 5mL of 0.1 wt% SDS solution. The turbidity (A10) was measured at an absorbance of 500nm. The emulsion stability (%) was calculated using the following formula. In addition, the value obtained by subtracting the emulsion stability of the comparative example prepared without using both PG and TG from the emulsion stability of each example (emulsion stability increment) was also derived. The higher the emulsion stability increment, the higher the effect of improving the emulsion stability. The results are shown in Tables 6-1 to 6-4.

[0156] [Number 6] Emulsion stability (%) = {(A10×10) / (A0-A10)}×100 (2-4) Foaming properties The processed dry composition containing vegetable protein was redispersed in deionized water to prepare 50 mL of a redispersed liquid containing 0.5% by weight of the dry composition. The redispersed liquid was homogenized at 18,000 rpm for 30 minutes and immediately transferred to a 100 mL measuring cylinder. The volume VF0 of the redispersed liquid containing foam was measured, and the foaming property (%) was calculated using the following calculation formula. In addition, the relative value of the foaming property of each embodiment (relative value of foaming property / relative to no enzyme) when the foaming property of the comparative example ("no enzyme") prepared without using both PG and TG was set to 1 was also derived. The higher the relative value of foaming property, the higher the foaming property improvement effect. The results are shown in Tables 6-1 to 6-4.

[0157] [Number 7] Foaming property (%) = 100 × (VF0-50) / 50 (2-5) Foam stability The redispersion liquid homogenized in (2-4) was transferred to a 100 mL graduated cylinder and then left for 30 minutes. The volume VF30 of the redispersion liquid including foam was measured in the same manner, and the foam stability (%) was calculated using the following calculation formula. In addition, the value obtained by subtracting the foam stability of the comparative example prepared without using both PG and TG from the foam stability of each example was derived (foam stability increment). The higher the foam stability increment, the higher the foam stability improvement effect. The results are shown in Tables 6-1 to 6-4.

[0158] [Number 8] Foam stability (%) = 100 × (VF30 / VF0) (2-6) Oil retention 0.1 g of the processed dry composition containing vegetable protein was suspended in 1 g of canola oil and vortexed for 30 seconds to prepare an oil suspension. After standing for 30 minutes, the oil suspension was centrifuged at 2000×g for 10 minutes to recover the supernatant. The weight of the recovered supernatant was measured, and the measured value was subtracted from 1 g (the weight of the canola oil used for suspension) to calculate the weight of the oil absorbed by the protein. Furthermore, 1 g of the processed dry composition containing vegetable protein was set to 100%, and the ratio of the weight (g) of the oil absorbed per 1 g was taken as the oil retention (%). In addition, the relative value of the oil retention of each example was derived when the oil retention of the comparative example (“enzyme-free”) prepared without using both PG and TG was set to 1 (relative value of oil retention / relative to enzyme-free). The higher the relative value of oil retention, the higher the effect of improving oil retention. The results are shown in Tables 6-1 to 6-4.

[0159] (2-7) Smoothness The processed vegetable protein-containing dry composition obtained was redispersed in water to prepare a redispersion liquid containing 10% by weight of the dry composition. Three trained test subjects put the redispersion liquid in their mouths to confirm the mouthfeel (tongue touch), and the rough tongue touch and the degree of smoothness imparted compared with the comparative example (PG alone) prepared in the same manner except for the lack of TG and the comparative example (TG alone) prepared in the same manner except for the lack of PG were classified based on the following criteria. The examples with improved smoothness compared with PG alone and improved smoothness compared with TG alone were evaluated as having obtained an improved smoothness effect by the combination of PG and TG. The results are shown in Tables 6-1 to 6-4.

[0160] Feeling roughness... "Y" No roughness felt... "N" Compared with PG or TG alone, the smoothness is not improved... "-" Compared with PG or TG alone, the smoothness is improved… "+" Compared with PG or TG alone, the smoothness is significantly improved... "++" (3) Test results [Table 6-1] [Table 6-2] [Table 6-3] [Table 6-4] As shown in Tables 6-1 to 6-4, in all of Examples 13 to 34, the effect of improving solubility was confirmed by combining PG and TG.

[0161] For liquid compositions containing vegetable proteins derived from soybeans, peas, mung beans, broad beans, chickpeas, lentils, rice, corn, cashews, almonds, coconuts, pistachios, walnuts, or chia seeds, improved solubilization and improved emulsification properties were confirmed (Examples 13 to 19, 23, 26 to 28, 30 to 32).

[0162] For liquid compositions containing vegetable proteins derived from soybeans, peas, beans, lentils, rice, barley, sorghum, potatoes, hazelnuts, almonds, coconuts, peanuts, pistachios, or hemp seeds, improved solubilization and improved emulsion stability were confirmed (Examples 13, 14, 16, 18 to 21, 24, 25, 27 to 30, 33).

[0163] Regarding the liquid composition containing the vegetable protein derived from peas, mung beans, chickpeas, or almonds, improvement in solubilization and improvement in foaming properties were observed (Examples 14, 15, 17, and 27).

[0164] Regarding the liquid composition containing vegetable protein derived from soybean, broad bean, rice, or potato, improvement in solubilization and improvement in foam stability were observed (Examples 13, 16, 19, and 24).

[0165] For liquid compositions containing vegetable proteins derived from broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds, or hemp seeds, improved solubilization and improved oil retention were confirmed (Examples 16 to 19, 24, 26, 29, 30 to 33).

[0166] Improved solubilization and improved smoothness were observed in the liquid composition containing vegetable protein derived from soybean, pea, mung bean, lupin, rice, or almond (Examples 13 to 15, 19, 27, and 34).

Claims

1. A method for producing a processed vegetable protein-containing composition, characterized in that: The method comprises the step of treating a liquid composition containing vegetable protein with protein deamidase and transglutaminase to obtain a processed liquid composition containing vegetable protein.

2. The method for producing a processed vegetable protein-containing composition according to claim 1, wherein: The method for producing the processed vegetable protein-containing composition further comprises the step of drying the processed vegetable protein-containing liquid composition to obtain a processed vegetable protein-containing dry composition for redispersion in a liquid.

3. The method for producing a processed vegetable protein-containing composition according to claim 1, wherein: The vegetable protein is a protein derived from plants, and the plants are selected from soybeans, peas, mung beans, broad beans, chickpeas, lentils, lupines, rice, barley, oats, sorghum, rye, corn, potatoes, hazelnuts, cashews, almonds, coconuts, peanuts, pistachios, walnuts, chia seeds and hemp seeds.

4. The method for producing a processed vegetable protein-containing composition according to claim 1, wherein: Allow protein deamidase and transglutaminase to act simultaneously.

5. The method for producing a processed vegetable protein-containing composition according to claim 1, wherein: The activity ratio of protein deamidase to transglutaminase is 0.05:0.95 to 0.9:0.

1.

6. A solubilizing agent for a liquid composition containing vegetable protein, characterized in that: Contains protein deamidase and transglutaminase.

7. The solubilizing agent according to claim 6, wherein The activity ratio of protein deamidase to transglutaminase is 0.05:0.95 to 0.9:0.

1.

8. The solubilizing agent according to claim 6, wherein The solubilizing agent is used to improve the dispersion stability of a liquid composition containing vegetable protein derived from oats.

9. The solubilizing agent according to claim 8, wherein The activity ratio of protein deamidase to transglutaminase is 0.05:0.95 to 0.9:0.

1.

10. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used to improve the emulsification of a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, peas, mung beans, broad beans, chickpeas, lentils, rice, corn, cashews, almonds, coconuts, pistachios, walnuts and chia seeds.

11. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used for improving the emulsification stability of a liquid composition containing vegetable protein derived from plants, and the plants are selected from soybeans, peas, beans, lentils, rice, barley, sorghum, potatoes, hazelnuts, almonds, coconuts, peanuts, pistachios and hemp seeds.

12. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used to improve the foaming property of a liquid composition containing vegetable protein derived from a plant, wherein the plant is selected from peas, mung beans, chickpeas and almonds.

13. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used to improve the foam stability of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from soybeans, broad beans, rice and potatoes.

14. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used for improving the oil retention of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from broad beans, chickpeas, lentils, rice, potatoes, cashews, peanuts, pistachios, walnuts, chia seeds and hemp seeds.

15. The solubilizing agent according to claim 6 or 7, wherein The solubilizer is used to improve the smoothness of a liquid composition containing vegetable protein derived from plants, wherein the plants are selected from soybeans, peas, mung beans, lupines, rice and almonds.

16. A food or beverage containing vegetable protein, characterized in that: A composition containing a processed vegetable protein obtained by the production method according to claim 1.

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