Manufacturing method for gel-like vegetable protein composition, and application thereof

Abstract

The present invention addresses the problem of providing a vegetable protein composition based on a protein derived from a vegetable raw material, with said vegetable protein composition being sufficiently gelled. The present invention relates to: a manufacturing method for a gel-like vegetable protein composition including causing a filamentous fungus–derived protease to act on a vegetable protein–containing raw material, and performing heat treatment after the action of the filamentous fungus–derived protease; and a gelling method for a vegetable protein–containing raw material.

Description

Method for producing gel-like vegetable protein composition and its application

[0001] The present invention relates to a method for producing a gelatinous vegetable protein composition, a method for gelling a vegetable protein-containing raw material, and a gelling agent for a pea protein-containing raw material.

[0002] In recent years, plant-based cheese has been gaining attention as a sustainable and allergen-free alternative to traditional dairy cheese. Plant-based cheese is made from plant-based ingredients such as cashew nuts, soybeans, and coconuts.

[0003] For example, Patent Document 1 discloses a gelled food obtained by gelling a proteinaceous colloidal solution using an enzyme derived from koji mold without thermal denaturation. Patent Document 1 is characterized in that no heat treatment is performed for gelation. Furthermore, Patent Document 2 discloses a method for producing plant-based cheese, which includes the steps of treating a material containing plant protein with a protease, inactivating the protease, and mixing with starch. Patent Document 2 also considers producing plant-based cheese with excellent stretchability.

[0004] JP 2009-178117 A International Publication No. 2023 / 228954

[0005] However, there is a problem that the degree of gelation is not sufficient in products based on proteins derived from plant materials.

[0006] Therefore, in order to solve these problems of the conventional technology, the inventors conducted research with the aim of providing a vegetable protein composition based on protein derived from vegetable raw materials, which is a sufficiently gelled vegetable protein composition.

[0007] Examples of specific embodiments of the present invention are given below.

[0008] [1] A method for producing a gelatinous plant protein composition, comprising allowing a filamentous fungus-derived protease to act on a plant protein-containing raw material, and performing a heat treatment after the action of the filamentous fungus-derived protease. [2] A method for producing the gelatinous plant protein composition according to [1], wherein the heating temperature in the heat treatment is above 65°C. [3] A method for producing the gelatinous plant protein composition according to [1] or [2], wherein the water content of the plant protein-containing raw material is 60% by mass or more. [4] A method for producing the gelatinous plant protein composition according to any of [1] to [3], wherein the plant protein-containing raw material contains a plant protein content of 5 to 14% by mass. [5] A method for producing the gelatinous plant protein composition according to any of [1] to [4], wherein the plant protein-containing raw material is a dispersion of a plant protein isolate. [6] A method for producing the gelatinous plant protein composition according to any of [1] to [5], wherein the protein contained in the plant protein-containing raw material is pea protein. [7] A method for producing a gelatinous plant protein composition according to any one of [1] to [6], wherein the filamentous fungus-derived protease is a filamentous fungus-derived acidic protease. [8] A method for producing a gelatinous plant protein composition according to any one of [1] to [7], wherein the act of a filamentous fungus-derived protease comprises acti- vating the filamentous fungus-derived protease on a mixed raw material containing a plant protein-containing raw material and starch, and the gelatinous plant protein composition is plant-based cheese. [9] A method for gelling a plant protein-containing raw material, comprising: acti- vating a filamentous fungus-derived protease on the plant protein-containing raw material; and performing a heat treatment after the acti- vation of the filamentous fungus-derived protease.

[10] The method for gelling a plant protein-containing raw material according to [9], wherein the heating temperature in the heat treatment is above 65°C.

[11] The method for gelling a plant protein-containing raw material according to [9] or

[10] , wherein the water content of the plant protein-containing raw material is 60% by mass or more.

[12] The method for gelling a vegetable protein-containing raw material according to any one of [9] to

[11] , wherein the vegetable protein content in the vegetable protein-containing raw material is 5 to 14% by mass.

[13] The method for gelling a vegetable protein-containing raw material according to any one of [9] to

[12] , wherein the vegetable protein-containing raw material is a dispersion of vegetable protein isolate.

[14] The method for gelling a vegetable protein-containing raw material according to any one of [9] to

[13] , wherein the protein contained in the vegetable protein-containing raw material is pea protein.

[15] The method for gelling a vegetable protein-containing raw material according to any one of [9] to

[14] , wherein the filamentous fungus-derived protease is a filamentous fungus-derived acidic protease.

[16] The method for gelling a vegetable protein-containing raw material according to any one of [9] to

[15] , wherein the act of the filamentous fungus-derived protease comprises acti- vating the filamentous fungus-derived protease on a mixed raw material containing the vegetable protein-containing raw material and starch.

[17] A gelling agent for a pea protein-containing raw material, comprising a filamentous fungus-derived protease.

[18] The gelling agent according to

[17] , wherein the filamentous fungus-derived protease is a filamentous fungus-derived acidic protease.

[19] A gel-like pea protein composition obtained by allowing the gelling agent according to

[17] or

[18] to act on a pea protein-containing raw material.

[0009] According to the present invention, a vegetable protein composition based on a protein derived from a vegetable raw material can be obtained, which is a well-gelled vegetable protein composition.

[0010] Figure 1 is a photograph showing the gelation state of the vegetable protein compositions obtained in Examples and Comparative Examples. Figure 2 is a photograph showing the gelation state of the vegetable protein compositions obtained in Examples and Comparative Examples.

[0011] The present invention will be described in detail below. The following description may be based on representative embodiments or specific examples, but the present invention is not limited to such embodiments. In this specification, a numerical range expressed using "to" means a range that includes the numerical values ​​before and after "to" as the lower and upper limits.

[0012] (Method for producing a gel-like vegetable protein composition / Method for gelling a vegetable protein-containing raw material) This embodiment relates to a method for producing a gel-like vegetable protein composition, which includes allowing a filamentous fungus-derived protease to act on a vegetable protein-containing raw material and performing a heat treatment after the action of the filamentous fungus-derived protease. This embodiment also relates to a method for gelling a vegetable protein-containing raw material, which includes allowing a filamentous fungus-derived protease to act on the vegetable protein-containing raw material and performing a heat treatment after the action of the filamentous fungus-derived protease.

[0013] This embodiment provides a new method for gelling a plant protein-containing raw material using an enzyme derived from a filamentous fungus. Needs for gelatinous plant protein compositions are diversifying, and there is a demand for gelatinous plant protein compositions made solely from plant-derived raw materials, or gelatinous plant protein compositions that do not contain additives. In this embodiment, by using an enzyme derived from a filamentous fungus, it is possible to gel a plant protein-containing raw material without using gelling agents such as polysaccharides (e.g., starch or thickening polysaccharides) or animal-derived enzymes. In this way, this embodiment provides an innovative and sustainable gelatinous plant protein composition.

[0014] The present embodiment has the above-described configuration, and thus can provide a plant protein composition based on a protein derived from a plant material, which is sufficiently gelled. The sufficiently gelled plant protein composition is self-supporting and can maintain its shape even after being removed from a mold.

[0015] Furthermore, because the vegetable protein gel composition obtained in this embodiment can be substantially free of gelling agents such as polysaccharides (e.g., starch or thickening polysaccharides), it is possible to produce a vegetable protein gel composition that has poor stretchability and reduced tensile elasticity. Thus, this embodiment makes it possible to provide a vegetable protein gel composition with a novel texture.

[0016] Furthermore, when the gelatinous vegetable protein composition obtained in this embodiment is vegetable cheese, the vegetable cheese can exhibit physical properties similar to those of animal cheese due to its thermal melting properties.

[0017] <Vegetable Protein-Containing Raw Material> The vegetable protein-containing raw material used in this embodiment is preferably a liquid in which vegetable protein is dissolved or dispersed in water. Specific examples of vegetable protein-containing raw materials include: (i) a liquid obtained by dispersing in water a dry powder of a plant (typically a food material) from which the vegetable protein is derived; (ii) a liquid obtained by dispersing in water a dry powder of a plant (typically a food material) from which the vegetable protein is derived, the protein content of which has been increased by removing at least any component other than the protein; (iii) a liquid obtained by crushing and dispersing in water a plant (typically a food material, a form of vegetable protein material) from which the vegetable protein is derived, and optionally removing insoluble matter derived from the skins of these plants by any means such as centrifugation, filtration, a filter bag, or a sieve; (iv) a liquid obtained by removing at least any component other than the vegetable protein from any of the liquids (i) to (iii) above to increase the protein concentration; and (v) a liquid obtained by mixing with water a dry powder (a form of vegetable protein material) prepared from any of the liquids (i) to (iv) above. Examples of the liquids (i) to (v) include vegetable milk, vegetable protein concentrates, and vegetable protein isolate dispersions. Among these, the vegetable protein-containing raw material is preferably a vegetable protein isolate dispersion, and more preferably an aqueous vegetable protein isolate dispersion. In this specification, vegetable protein isolate refers to a vegetable protein-containing raw material that has been separated and purified so that the vegetable protein content is 60% by mass or more, preferably 70% by mass or more.

[0018] The content of vegetable protein contained in the vegetable protein-containing raw material is not particularly limited. For example, the vegetable protein content is preferably more than 5% by mass, more preferably 5.5% by mass or more, 5.8% by mass or more, 6.0% by mass or more, 6.3% by mass or more, 6.5% by mass or more, 6.8% by mass or more, 7.0% by mass or more, 7.2% by mass or more, or 7.3% by mass or more, based on the total mass of the vegetable protein-containing raw material. Furthermore, the vegetable protein content is preferably 30% by mass or less, more preferably 25% by mass or less, 20% by mass or less, 18% by mass or less, 16% by mass or less, 14% by mass or less, or 12% by mass or less, based on the total mass of the vegetable protein-containing raw material. By setting the vegetable protein content contained in the vegetable protein-containing raw material within the above range, gelation of the vegetable protein-containing raw material can be more effectively promoted.

[0019] The vegetable protein content in the vegetable protein-containing raw material is preferably 1% by mass or more, more preferably 3% by mass or more, 5% by mass or more, 10% by mass or more, 15% by mass or more, 20% by mass or more, 30% by mass or more, 40% by mass or more, 50% by mass or more, 60% by mass or more, 70% by mass or more, or 75% by mass or more, based on the total solid mass of the vegetable protein-containing raw material. Furthermore, the vegetable protein content is preferably 99% by mass or less, more preferably 95% by mass or less, 90% by mass or less, or 85% by mass or less, based on the total solid mass of the vegetable protein-containing raw material. By setting the vegetable protein content relative to the total solid mass of the vegetable protein-containing raw material within the above range, gelation of the vegetable protein-containing raw material can be more effectively promoted.

[0020] The water content of the vegetable protein-containing raw material is preferably 60% by mass or more, more preferably 65% ​​by mass or more, even more preferably 70% by mass or more, even more preferably 75% by mass or more, still more preferably 80% by mass or more, and particularly preferably 85% by mass or more, based on the total mass of the vegetable protein-containing raw material. The water content is preferably 95% by mass or less, based on the total mass of the vegetable protein-containing raw material.

[0021] In this embodiment, the content of polysaccharides in the vegetable protein-containing raw material is preferably 0.6 parts by mass or less, more preferably 0.5 parts by mass or less, even more preferably 0.4 parts by mass or less, and particularly preferably 0.3 parts by mass or less, per part by mass of protein. In particular, the vegetable protein-containing raw material is preferably substantially free of polysaccharides. In this specification, "substantially free of polysaccharides" refers to a polysaccharide content of 0.1 parts by mass or less per part by mass of protein. Examples of polysaccharides that can be used as gelling agents include starch and thickening polysaccharides.

[0022] Furthermore, the oil content in the vegetable protein-containing raw material is preferably 15% by mass or less, more preferably 10% by mass or less, even more preferably 5% by mass or less, even more preferably 3% by mass or less, even more preferably 1% by mass or less, and particularly preferably 0.5% by mass or less, relative to the total mass of the vegetable protein-containing raw material. Among these, the vegetable protein-containing raw material is preferably composed of vegetable protein and water, and preferably contains substantially no oil other than water as a solvent. In this specification, "substantially no oil" means that the oil content is 0.1% by mass or less, relative to the total mass of the vegetable protein-containing raw material.

[0023] The origin of the vegetable protein is not particularly limited, and examples thereof include pulses such as soybeans, broad beans, peas, chickpeas, mung beans, lupin beans, and kidney beans; cereals such as barley, rice, wheat, rye, oats, buckwheat, barnyard millet, foxtail millet, teff, quinoa, and corn; nuts and seeds such as industrial hemp, canary seeds, flaxseed, almonds, cashew nuts, hazelnuts, pecan nuts, macadamia nuts, pistachios, walnuts, Brazil nuts, peanuts, coconuts, pili nuts, chestnuts, sesame seeds, and pine nuts; and algae. The vegetable protein may be one of the above vegetable proteins or a combination of multiple proteins. Among these, pulse-derived protein is preferred, and pea protein is particularly preferred.

[0024] <Enzyme> In this embodiment, protease refers to an endopeptidase. The origin of the protease is not particularly limited, and for example, proteases derived from filamentous fungi such as those of the genus Aspergillus, Mucor, Neurospora, Penicillium, Rhizomucor, Rhizopus, and Sclerotinia can be used. Preferred examples include proteases derived from Aspergillus oryzae, Aspergillus melleus, and Aspergillus oryzae. These proteases may be used singly or in combination of two or more.

[0025] The protease derived from a filamentous fungus is preferably an acidic protease derived from a filamentous fungus, and is particularly preferably a protease derived from Aspergillus oryzae or Aspergillus oryzae, with a protease derived from Aspergillus oryzae being particularly preferred.

[0026] The filamentous fungal protease is preferably used so that its protease activity per gram of vegetable protein is, for example, 10 to 300,000 U, preferably 50 to 200,000 U, 100 to 100,000 U, 200 to 50,000 U, or 500 to 30,000 U. The protease activity is measured by the Folin method using casein as a substrate. Specifically, the protease activity is measured by a standard enzyme reaction using casein as a substrate at pH 3.0 (or pH 6.0 or 8.0), where 1 unit (1 U) is the amount of enzyme that causes an increase in the Folin test solution color substance equivalent to 1 μg of tyrosine per minute. The pH used for measurement may be the pH at which the filamentous fungal protease exhibits the highest activity.

[0027] The filamentous fungal protease can be prepared from a culture medium of a microorganism from which the protease is derived. Specific preparation methods include recovering the protease from the culture medium or cells of the microorganism. For example, when a protease-secreting microorganism is used, the cells can be recovered from the culture medium by filtration, centrifugation, or the like, as necessary, and the enzyme can then be separated and / or purified. When a protease-nonsecreting microorganism is used, the cells can be recovered from the culture medium by pressure treatment, ultrasonication, or the like, as necessary, and then disrupted to expose the enzyme, after which the enzyme can be separated and / or purified. The enzyme can be separated and / or purified by any known protein separation and / or purification method, without any particular limitation. Examples of the enzyme separation and / or purification method include centrifugation, UF concentration, salting out, and various chromatography methods using ion exchange resins. The separated and / or purified enzyme can be powdered by drying methods such as lyophilization and vacuum drying, or by using an appropriate excipient and / or drying aid in the drying method. The isolated and / or purified enzyme can also be liquefied by adding an appropriate additive and sterilizing by filtration.

[0028] Commercially available proteases derived from filamentous fungi can also be used, and preferred examples of commercially available proteases include Aspergillus oryzae-derived acidic protease, Aspergillus oryzae-derived neutral protease, and Aspergillus melleus-derived alkaline protease, all of which are manufactured by Amano Enzyme Inc.

[0029] <Optional Components> In this embodiment, in addition to the protease described above, a specific compound can be used as a gelling agent to further improve gelation. Examples of gelling agents include polysaccharides such as starch, gellan gum, agar, carrageenan, xanthan gum, and locust bean gum. However, in a preferred embodiment of the present invention, it is preferable to gel the vegetable protein without using a gelling agent. Therefore, in this embodiment, it is also possible to obtain a gel vegetable protein composition in which only the vegetable protein is gelled.

[0030] In this embodiment, the vegetable protein gel composition may contain, as optional ingredients, for example, fats and oils, flavorings, sweeteners, acidulants, bittering agents, coloring agents, antioxidants, pH adjusters, vitamins, amino acids, minerals, antifoaming agents, emulsifiers (glycerin fatty acid esters, sucrose fatty acid esters, lecithin, saponin, etc.), salts (table salt, calcium salts, phosphates, etc.), etc. In this embodiment, polysaccharides (for example, starch or thickening polysaccharides) may be added to the vegetable protein gel composition for purposes other than gelation.

[0031] <Step of Applying Filamentous Fungal Protease> The method for producing a gelatinous plant protein composition and the method for gelling a plant protein-containing raw material according to this embodiment include a step of applying a filamentous fungal protease to a plant protein-containing raw material. The reaction time, temperature, and pH of the reaction solution for applying the filamentous fungal protease to the plant protein-containing raw material are not particularly limited. The reaction temperature is, for example, 10 to 80°C, preferably 20 to 70°C, and more preferably 40 to 60°C. The pH of the reaction solution is, for example, 3 to 9, preferably 4 to 8, and more preferably 5 to 7. The reaction time is, for example, 30 seconds to 24 hours, preferably 1 minute to 12 hours, more preferably 30 minutes to 6 hours, and more preferably 1 to 3 hours. These reaction conditions are appropriately selected depending on the desired plant protein gel composition. The optimal reaction conditions can be determined through preliminary experiments.

[0032] <Heat Treatment Step> The method for producing a gelatinous vegetable protein composition and the method for gelling a vegetable protein-containing raw material according to this embodiment further include a step of performing a heat treatment (heat treatment step) after the action of the filamentous fungus-derived protease. In this embodiment, such a heat treatment step promotes gelation of the vegetable protein composition. For this reason, the heat treatment step may also be referred to as a gelation step in this specification.

[0033] The heating time, temperature, pH of the reaction solution, etc. in the heat treatment step are not particularly limited. For example, the heating temperature in the heat treatment is preferably above 60°C, more preferably 61°C or higher, 63°C or higher, 65°C or higher, more preferably above 65°C, 66°C or higher, 67°C or higher, or 69°C or higher. For the purpose of further promoting gelation, the heating temperature in the heat treatment may be 70°C or higher, 75°C or higher, 80°C or higher, 85°C or higher, or 90°C or higher. Furthermore, the heating temperature in the heat treatment is preferably, for example, 100°C or lower, more preferably 99°C or lower, 98°C or lower, 97°C or lower, or 96°C or lower. For the purpose of reducing the influence of heat, the heating temperature in the treatment may be 95°C or lower, 90°C or lower, 85°C or lower, 80°C or lower, or 75°C or lower. The pH of the reaction solution is, for example, 3 to 9, preferably 4 to 8, and more preferably 5 to 7. The heating time is, for example, 30 seconds to 6 hours, preferably 1 minute to 4 hours, more preferably 10 minutes to 3 hours, more preferably 15 minutes to 2 hours, or 20 minutes to 1 hour.

[0034] <Other Steps> The method for producing a gelled vegetable protein composition and the method for gelling a vegetable protein-containing raw material of this embodiment include the following steps (1) and (2). In this embodiment, a cooling step may be performed after step (2). Furthermore, a step of dispersing the powdered vegetable protein-containing raw material in water (dispersion step) or a step of homogenizing the vegetable protein-containing raw material dispersed in water (homogenization step) may be performed before step (1). (1) A step of allowing a filamentous fungus-derived protease to act on the vegetable protein-containing raw material (enzyme treatment step). (2) A step of performing heat treatment after enzyme treatment (heat treatment step).

[0035] In the method for producing a gelatinous vegetable protein composition and the method for gelling a vegetable protein-containing raw material according to this embodiment, a cooling step is preferably performed after the heat treatment step (2). The cooling step further promotes gelation of the gelatinous vegetable protein composition. The cooling time and cooling temperature in the cooling step are not particularly limited. The cooling temperature is preferably above 0°C, more preferably 1°C or higher, 2°C or higher, or 3°C or higher. The cooling temperature is preferably 20°C or lower, more preferably 15°C or lower, 13°C or lower, 10°C or lower, 8°C or lower, or 6°C or lower. The cooling time is preferably 10 minutes or longer, more preferably 20 minutes or longer, 30 minutes or longer, 1 hour or longer, 2 hours or longer, 4 hours or longer, 8 hours or longer, or 12 hours or longer. While a longer cooling time is not problematic, the upper limit is preferably 30 days or shorter, more preferably 20 days or shorter, 10 days or shorter, 5 days or shorter, 3 days or shorter, or 24 hours or shorter.

[0036] When a step of dispersing the powdered vegetable protein-containing raw material in water (dispersion step) or a step of homogenizing the vegetable protein-containing raw material dispersed in water (homogenization step) is carried out before step (1), it is preferable to perform the treatment at 500 bar, for example, two or more times.

[0037] (Gelling Agent) This embodiment relates to a gelling agent for a vegetable protein-containing raw material, which contains a protease derived from a filamentous fungus. In particular, the gelling agent of this embodiment is preferably a gelling agent for a pea protein-containing raw material, which contains a protease derived from a filamentous fungus.

[0038] Examples of the filamentous fungal protease contained in the gelling agent of this embodiment include proteases derived from Aspergillus oryzae, Aspergillus melleus, and Aspergillus oryzae. Acidic proteases derived from filamentous fungi are preferred. Of these, proteases derived from filamentous fungi are preferably proteases derived from Aspergillus oryzae and Aspergillus oryzae, and particularly preferably proteases derived from Aspergillus oryzae.

[0039] The gelling agent may be any agent containing a protease derived from a filamentous fungus, or may consist of a protease derived from a filamentous fungus. The gelling agent may be in any form, such as powder, solid, gel, or liquid.

[0040] (Gel-like plant protein composition) This embodiment relates to a gel-like plant protein composition produced by the above-mentioned method for producing a gel-like plant protein composition. The gel-like plant protein composition produced by the above-mentioned method for producing a gel-like plant protein composition is a sufficiently gelled plant protein composition. Furthermore, the gel-like plant protein composition of this embodiment may be a gel-like plant protein composition that is substantially free of gelling agents such as polysaccharides (e.g., starch or thickening polysaccharides), has no stretchability, and has reduced tensile elasticity. Furthermore, the gel-like plant protein composition of this embodiment may be a plant protein composition that has heat melting properties. Thus, the gel-like plant protein composition of this embodiment is a gel-like plant protein composition with a novel texture.

[0041] The protein content of the vegetable protein gel composition of this embodiment is preferably greater than 5% by mass, more preferably 5.5% by mass or more, 5.8% by mass or more, 6.0% by mass or more, 6.3% by mass or more, 6.5% by mass or more, 6.8% by mass or more, 7.0% by mass or more, 7.2% by mass or more, or 7.3% by mass or more, based on the total mass of the vegetable protein gel composition. The protein content of the vegetable protein gel composition is preferably 30% by mass or less, more preferably 25% by mass or less, 20% by mass or less, 18% by mass or less, 16% by mass or less, 14% by mass or less, or 12% by mass or less, based on the total mass of the vegetable protein gel composition.

[0042] The gelatinous vegetable protein composition of this embodiment is a protein gel. In this specification, "protein gel" means that a gel is formed by protein. Specifically, the polysaccharide content in the protein gel is preferably 0.6 parts by mass or less, more preferably 0.5 parts by mass or less, even more preferably 0.4 parts by mass or less, and particularly preferably 0.3 parts by mass or less, per part by mass of protein. In particular, the protein gel is preferably one that is substantially free of polysaccharides as gelling agents other than proteins. "Substantially free of polysaccharides" refers to a polysaccharide content of 0.1 parts by mass or less per part by mass of protein. Examples of polysaccharides that serve as gelling agents include starch and thickening polysaccharides.

[0043] Furthermore, the oil content of the gelatinous vegetable protein composition of this embodiment is preferably 15% by mass or less, more preferably 10% by mass or less, even more preferably 5% by mass or less, even more preferably 3% by mass or less, even more preferably 1% by mass or less, and particularly preferably 0.5% by mass or less, relative to the total mass of the gelatinous vegetable protein composition. It is also preferable that the gelatinous vegetable protein composition is substantially oil-free, and the oil content may be 0% by mass. It is presumed that a gel with greater retention is more easily formed when the gelatinous vegetable protein composition is substantially oil-free.

[0044] The vegetable protein gel composition of this embodiment is substantially free of polysaccharides and oils, and therefore lacks stretchability and exhibits reduced tensile elasticity. Specifically, when the vegetable protein gel composition obtained in this embodiment is subjected to the following stretchability evaluation, the stretch length is preferably 100 mm or less, more preferably 80 mm or less, even more preferably 60 mm or less, and particularly preferably 40 mm or less. Here, the stretch length is a length measured by the following method. First, the vegetable protein gel composition is heated in a steam oven set at 110°C for 30 minutes, then removed from the steam oven. After confirming that the internal temperature of the sample has reached 70°C, the sample is stirred with a fork. After ensuring that the fork is covered with the sample, the tip of the fork is lifted at a rate of 5 cm / sec as if scooping up the sample, and the distance (stretch length (mm)) between the start point of lifting the tip of the fork and the point at which the sample no longer stretches is measured.

[0045] The vegetable protein gel composition of this embodiment is preferably a pea protein gel composition, i.e., the vegetable protein gel composition of this embodiment is preferably a pea protein gel composition obtained by allowing a filamentous fungus-derived protease to act on a pea protein-containing raw material.

[0046] The vegetable protein gel composition of this embodiment can be used in gel or solid vegetable protein-containing foods. Specific forms of vegetable protein-containing foods include meat-like processed foods (foods that mimic processed meat, poultry, and / or fish paste), and dairy substitute foods. Specific examples include meat substitutes, vegetable yogurt, vegetable cheese, etc.

[0047] <Plant-based cheese> The plant protein gel composition of the present embodiment may be plant-based cheese. Plant-based cheese has heat-melting properties and self-supporting properties, but does not have stretchability. Therefore, it has physical properties similar to those of hard animal-based cheese (e.g., cheddar cheese).

[0048] The present embodiment relates to a method for producing plant-based cheese, which includes allowing a filamentous fungus-derived protease to act on a vegetable protein-containing raw material and performing a heat treatment after the action of the filamentous fungus-derived protease. When allowing the filamentous fungus-derived protease to act on a vegetable protein-containing raw material, the filamentous fungus-derived protease may be allowed to act on a mixed raw material obtained by adding other raw materials (vegetable oils and fats, starch, etc.) and water to the vegetable protein-containing raw material. In other words, the present embodiment may relate to a method for producing plant-based cheese, which includes allowing a filamentous fungus-derived protease to act on a mixed raw material containing the vegetable protein-containing raw material and other raw materials, and performing a heat treatment after the action of the filamentous fungus-derived protease.

[0049] Other ingredients used in the method for producing plant-based cheese include starch, vegetable oils and fats, thickening polysaccharides, salt, calcium salts, organic acids, etc. In the method for producing plant-based cheese of this embodiment, both self-sustaining properties and thermal melting properties can be achieved without using thickening polysaccharides. Therefore, in the method for producing plant-based cheese of this embodiment, it is possible to not use thickening polysaccharides.

[0050] In particular, the other ingredients preferably include starch, and the method for producing plant-based cheese of this embodiment preferably includes allowing a filamentous fungus-derived protease to act on a mixed ingredient of a plant protein-containing ingredient and starch, and performing a heat treatment after the action of the filamentous fungus-derived protease. The filamentous fungus-derived protease used in the plant-based cheese production method is the same as the enzyme described in the method for producing a gelatinous plant protein composition described above. The plant protein-containing ingredients used in the plant-based cheese production method are the same as the ingredients described in the method for producing a gelatinous plant protein composition described above.

[0051] The starch is not particularly limited. Specific examples of plants from which starch is derived include cassava, potato, sweet potato, and arrowroot. One type of starch may be used alone, or two or more types may be used in combination. The amount of starch to be mixed is not particularly limited, but is preferably 5% by mass or more, more preferably 7% by mass or more, 10% by mass or more, or 15% by mass or more, based on the total mass of the plant-based cheese dough after mixing. The upper limit of the amount of starch to be mixed is not particularly limited, but is, for example, 30% by mass or less, or 25% by mass or less.

[0052] In this embodiment, the starch is preferably added before heat treatment at a temperature above 60° C. Adding the starch before heat treatment makes it easier to obtain a plant-based cheese that does not have stretchability. The timing of addition is not particularly limited as long as it is before heat treatment, but it is preferably added during the protease treatment step.

[0053] The vegetable oil is not particularly limited, but examples thereof include canola oil (rapeseed oil), coconut oil, corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, sunflower seed oil, safflower oil, flaxseed oil, palm oil, palm kernel oil, palm fruit oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, and rice bran oil. These vegetable oils may be used alone or in combination of two or more. Preferred examples include canola oil (rapeseed oil), coconut oil, and sunflower oil, and more preferred examples include canola oil (rapeseed oil) and coconut oil. The amount of vegetable oil mixed is not particularly limited, but is preferably 5 to 30% by mass, more preferably 7 to 27% by mass, even more preferably 10 to 25% by mass, and even more preferably 15 to 23% by mass, based on the total mass of the vegetable cheese dough after mixing.

[0054] The moisture content of the mixed raw material containing the vegetable protein-containing raw material and other raw materials is preferably 30% by mass or more, more preferably 35% by mass or more, 40% by mass or more, or 45% by mass or more, based on the total mass of the mixed raw material. The moisture content of the mixed raw material is preferably 90% by mass or less, more preferably 80% by mass or less, 70% by mass or less, or 60% by mass or less, based on the total mass of the mixed raw material.

[0055] The starch content in the mixed raw material is preferably 0.1 parts by mass or more, more preferably 0.5 parts by mass or more, 1.0 parts by mass or more, 1.5 parts by mass or more, or 2.0 parts by mass or more, per part by mass of the vegetable protein. The starch content in the mixed raw material is preferably 10 parts by mass or less, more preferably 8 parts by mass or less, 6 parts by mass or less, 4 parts by mass or less, or 3 parts by mass or less, per part by mass of the vegetable protein.

[0056] The method for producing plant-based cheese of this embodiment is characterized by including the steps of (1) preparing a mixed ingredient containing a plant protein-containing ingredient and other ingredients, (2) treating the prepared mixed ingredient with a filamentous fungus-derived protease, and (3) heat-treating the mixed ingredient. When starch is mixed as the other ingredient, the starch may be added during step (1) or step (2). The plant-based cheese obtained in this embodiment preferably has heat-melting properties and self-supporting properties, but does not have stretchability.

[0057] The method for producing plant-based cheese of this embodiment may include the following steps, and this embodiment may relate to plant-based cheese produced through the following steps: (1) a step of preparing a mixed raw material containing a plant protein-containing raw material and other raw materials, (2) a step of allowing a filamentous fungus-derived protease to act on the prepared mixed raw material, and (3) a step of heat-treating the protease-treated mixed raw material.

[0058] The method for producing plant-based cheese of this embodiment may also include the following steps, and this embodiment may relate to plant-based cheese produced through the following steps: (1) a step of preparing a mixed raw material containing a plant protein-containing raw material and other raw materials, (2) a step of allowing a filamentous fungus-derived protease to act on the prepared mixed raw material, (3) a step of adding starch during the step of allowing the protease to act, (4) a step of allowing the filamentous fungus-derived protease to act again after adding the starch, and (5) a step of heat-treating the protease-treated mixed raw material.

[0059] The features of the present invention will be explained in more detail below with reference to examples and comparative examples. The materials, amounts used, ratios, treatment contents, treatment procedures, etc. shown in the following examples can be changed as appropriate without departing from the spirit of the present invention. Therefore, the scope of the present invention should not be construed as being limited by the specific examples shown below.

[0060] <Test Example 1> <Materials used> Plant protein-containing raw material: pea protein isolate (powder, protein content 80% by mass, manufactured by Ingredion) Filamentous fungus-derived protease: Aspergillus oryzae-derived acid protease (manufactured by Amano Enzyme Inc.)

[0061] <Method for measuring enzyme activity> [Method for measuring protease activity] 5 mL of 0.6% (v / w) casein solution (0.7% (v / w) lactic acid, pH 3.0) was heated at 37°C for 10 minutes, and then 1 mL of a sample solution containing protease was added and immediately shaken. This solution was left at 37°C for 10 minutes, and then 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added and shaken, and the solution was left at 37°C for another 30 minutes and filtered. The first 3 mL of filtrate was discarded, and 2 mL of the next filtrate was measured, to which 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin's test solution (1→3) were added, shaken well, and left at 37°C for 30 minutes. The absorbance AT of this solution (enzyme reaction solution) at a wavelength of 660 nm was measured, using water as a control. Separately, 1 mL of sample solution containing protease was measured, 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added, and the mixture was shaken. 5 mL of 0.6% (v / w) casein solution (0.7% (v / w) lactic acid, pH 3.0) was then added, and the mixture was immediately shaken and left at 37°C for 30 minutes. The absorbance AB of this blank solution was measured in the same manner as the enzyme reaction solution described above, except that it was left at 37°C for 30 minutes. The amount of enzyme that produces an increase in the Folin test solution color substance equivalent to 1 μg of tyrosine per minute was defined as 1 unit (1 U). 1 mL, 2 mL, 3 mL, or 4 mL of a 1 mg / mL tyrosine standard stock solution (0.2 mol / L hydrochloric acid) was measured, and 0.2 mol / L hydrochloric acid test solution was added to each to make a total volume of 100 mL. 2 mL of each solution was measured, and 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin's test solution (1 → 3) were added. The mixture was immediately shaken and left at 37°C for 30 minutes. The absorbances A1, A2, A3, and A4 at a wavelength of 660 nm were measured for these solutions. Similarly, a control (blank solution) was measured using 2 mL of 0.2 mol / L hydrochloric acid test solution. 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin's test solution (1 → 3) were added, immediately shaken, and left at 37°C for 30 minutes. A calibration curve was created with absorbances A1, A2, A3, and A4 plotted on the vertical axis and the amount of tyrosine (μg) in 2 mL of each solution plotted on the horizontal axis, and the amount of tyrosine (μg) per absorbance difference of 1 was calculated.

[0062] Protease activity (U / g, U / mL) = (AT - AB) x F x 11 / 2 x 1 / 10 x 1 / M AT: absorbance of enzyme reaction solution AB: absorbance of blank F: amount of tyrosine (µg) when the absorbance difference is 1 as determined from the tyrosine calibration curve 11 / 2: conversion coefficient to total solution volume after reaction has stopped 1 / 10: conversion coefficient per minute of reaction time M: amount of sample (g or mL) in 1 mL of sample solution

[0063] <Method> Step 1 (dispersing step): Pea protein isolate (protein content 80%) was dispersed in water to a concentration of 7.5% by mass or 10% by mass. Step 2 (homogenizing step): The dispersion was treated twice with a high-pressure homogenizer (500 bar) to obtain a homogenized liquid. Step 3 (enzyme treatment step): The amount of protease shown in the table was added to the homogenized liquid, and the homogenized liquid was treated at 50°C for 2 hours. Step 4 (heat treatment step): The enzyme-treated liquid was heat-treated at 70°C or 95°C for 30 minutes. Step 5 (cooling step): The heat-treated liquid was cooled at 4°C overnight.

[0064] <Evaluation> The vegetable protein compositions obtained through the cooling process were evaluated for gelation. Specifically, when the container containing the vegetable protein composition was inverted, if liquid flowed out, it was evaluated as "absent" gelation, and if liquid did not flow out, it was evaluated as "present" gelation.

[0065]

[0066]

[0067] It was confirmed that protein gelation occurred in the Examples compared to the Comparative Examples. However, stretchability (gel elongation) was not confirmed in any of the gels.

[0068] <Test Example 2> <Materials used> Vegetable protein-containing raw material: pea protein isolate (powder, protein content 80% by mass, manufactured by Ingredion) Filamentous fungus-derived protease: Aspergillus oryzae-derived acidic protease (manufactured by Amano Enzyme Inc.) Filamentous fungus-derived protease: Aspergillus oryzae-derived neutral protease (manufactured by Amano Enzyme Inc.) Filamentous fungus-derived protease: Aspergillus melleus-derived alkaline protease (manufactured by Amano Enzyme Inc.) Filamentous fungus-derived peptidase: Aspergillus oryzae-derived peptidase (manufactured by Amano Enzyme Inc.) Bacterial-derived protease: Bacillus licheniformis-derived protease (manufactured by Amano Enzyme Inc.)

[0069] <Method for measuring enzyme activity> [Method for measuring protease activity] 5 mL of 0.6% (v / w) casein solution (pH 3.0: lactic acid / sodium hydroxide buffer (pH 3.0); pH 6.0: sodium phosphate buffer (pH 6.0); pH 8.0: sodium phosphate buffer (pH 8.0)) was heated at 37°C for 10 minutes, and then 1 mL of a sample solution containing protease was added and immediately shaken. This solution was then left at 37°C for 10 minutes, after which 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added and shaken, and the solution was again left at 37°C for 30 minutes and filtered. The first 3 mL of filtrate was discarded, and 2 mL of the next filtrate was measured, to which 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin's test solution (1→3) were added, shaken well, and left at 37°C for 30 minutes. For this solution (enzyme reaction solution), water was used as a control, and the absorbance AT at a wavelength of 660 nm was measured. Separately, 1 mL of sample solution containing protease was measured, and 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added and shaken, followed by 5 mL of 0.6% (v / w) casein solution (for pH 3.0, lactic acid / sodium hydroxide buffer (pH 3.0), for pH 6.0, sodium phosphate buffer (pH 6.0), for pH 8.0, sodium phosphate buffer (pH 8.0)). The solution (blank) was treated in the same manner as the enzyme reaction solution described above, except that it was left at 37 ° C for 30 minutes. The absorbance AB was measured. The amount of enzyme that causes an increase in the Folin test solution color substance equivalent to 1 μg of tyrosine per minute was defined as 1 unit (1 U). 1 mL, 2 mL, 3 mL, or 4 mL of 1 mg / mL tyrosine standard stock solution (0.2 mol / L hydrochloric acid) was measured, and 0.2 mol / L hydrochloric acid test solution was added to each solution to make 100 mL. 2 mL of each solution was measured, and 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin test solution (1 → 3) were added. The solution was immediately shaken and left at 37 °C for 30 minutes. The absorbances A1, A2, A3, and A4 at a wavelength of 660 nm were measured for these solutions. In addition, 2 mL of 0.2 mol / L hydrochloric acid test solution was measured, and 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin test solution (1 → 3) were added. The solution obtained by immediately shaking and leaving at 37 °C for 30 minutes was used as a control (blank solution), and the same measurements were performed.A calibration curve was prepared with absorbances A1, A2, A3, and A4 on the vertical axis and the amount of tyrosine (μg) in 2 mL of each solution on the horizontal axis, and the amount of tyrosine (μg) was determined for an absorbance difference of 1. Protease activity (U / g, U / mL) = (AT - AB) x F x 1 1 / 2 x 1 / 10 x 1 / M AT: absorbance of enzyme reaction solution AB: absorbance of blank F: amount of tyrosine (μg) when the absorbance difference was 1, determined from the tyrosine calibration curve 1 1 / 2: conversion coefficient for total solution volume after reaction was stopped 1 / 10: conversion coefficient for reaction time per minute M: amount of sample (g or mL) in 1 mL of sample solution.

[0070] [Method for measuring peptidase activity] An appropriate amount of enzyme was weighed and dissolved or uniformly dispersed in pH 7.0 phosphate buffer (0.01 mol / L) to a total volume of 50 mL. This solution was then further diluted 10-fold, 100-fold, or 1000-fold with buffer to prepare a sample solution. 40 mg of L-leucyl-p-nitroanilide hydrochloride was weighed and dissolved in pH 7.0 phosphate buffer (0.01 mol / L, containing 12.5 μmol / L zinc sulfate) to prepare a 100 mL substrate solution. 2 mL of the substrate solution was measured and heated at 37°C for 5 minutes. 0.5 mL of the sample solution was added, shaken, and heated at the same temperature for 15 minutes. 2.5 mL of 0.2 mol / L hydrochloric acid was added and mixed to terminate the reaction, creating an enzyme reaction solution. A comparison solution (enzyme blank solution) was prepared in the same manner as in the preparation of the test solution, except that a pH 7.0 phosphate buffer (0.01 mol / L) was used instead of the enzyme reaction solution. The absorbance of the enzyme reaction solution and the enzyme blank solution was measured at a wavelength of 405 nm, and the peptidase activity was calculated using the following formula. If the test solution or comparison solution for which absorbance was to be measured was turbid, it was centrifuged and the supernatant was measured. The activity required to produce 1 μmol of p-nitroaniline per minute was defined as 1 unit (1 U).

[0071]

[0072] <Method> Step 1 (dispersing step): Pea protein isolate (protein content 80%) was dispersed in water to a concentration of 10% by mass. Step 2 (homogenizing step): The dispersion was treated twice with a high-pressure homogenizer (500 bar) to obtain a homogenized liquid. Step 3 (enzyme treatment step): The amount of protease shown in the table was added to the homogenized liquid, and the homogenized liquid was treated at 50°C for 2 hours. Step 4 (heat treatment step): The enzyme-treated liquid was heat-treated at 95°C for 30 minutes. Step 5 (cooling step): The liquid was cooled at 4°C for 24 hours.

[0073] <Evaluation> The vegetable protein compositions obtained through the cooling process were evaluated for gelation. Specifically, when the container containing the vegetable protein composition was inverted, if liquid flowed out, it was evaluated as "absent" gelation, and if liquid did not flow out, it was evaluated as "present" gelation.

[0074]

[0075] Gelation of plant proteins was observed when proteases derived from filamentous fungi were used, and it was found that particularly high gel strength was obtained when acidic proteases derived from Aspergillus oryzae were used.

[0076] Test Example 3 Materials Used Vegetable protein-containing raw material: pea protein isolate (powder, protein content 80% by mass, manufactured by Ingredion) Fungal acid protease: Aspergillus oryzae acid protease (manufactured by Amano Enzyme Inc.) Bacterial protease: Bacillus licheniformis protease (manufactured by Amano Enzyme Inc.)

[0077] <Method for measuring enzyme activity> [Method for measuring protease activity] 5 mL of 0.6% (v / w) casein solution (lactic acid / sodium hydroxide buffer (pH 3.0) for pH 3.0, sodium phosphate buffer (pH 8.0) for pH 8.0) was heated at 37°C for 10 minutes, and then 1 mL of a sample solution containing protease was added and immediately shaken. This solution was left at 37°C for 10 minutes, and then 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added and shaken, and the solution was again left at 37°C for 30 minutes and filtered. The first 3 mL of filtrate was discarded, and 2 mL of the next filtrate was measured, to which 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin's test solution (1→3) were added, shaken well, and left at 37°C for 30 minutes. The absorbance AT of this solution (enzyme reaction solution) at a wavelength of 660 nm was measured, using water as a control. Separately, 1 mL of sample solution containing protease was measured, 5 mL of trichloroacetic acid test solution (0.44 mol / L trichloroacetic acid) was added, and the mixture was shaken. 5 mL of 0.6% (v / w) casein solution (for pH 3.0, lactic acid / sodium hydroxide buffer (pH 3.0) or sodium phosphate buffer (pH 6.0) was added; for pH 8.0, sodium phosphate buffer (pH 8.0) was added), immediately shaken, and the mixture was left at 37°C for 30 minutes. The absorbance AB of a blank solution was measured in the same manner as the enzyme reaction solution described above, except that the blank was left at 37°C for 30 minutes. The amount of enzyme that increases the amount of Folin test solution colored substance equivalent to 1 μg of tyrosine per minute was defined as 1 unit (1 U). 1 mL, 2 mL, 3 mL, or 4 mL of a 1 mg / mL tyrosine standard stock solution (0.2 mol / L hydrochloric acid) was measured, and 0.2 mol / L hydrochloric acid test solution was added to each to make a total volume of 100 mL. 2 mL of each solution was measured, and 5 mL of 0.55 mol / L sodium carbonate TS and 1 mL of Folin's TS (1 → 3) were added. The mixture was immediately shaken and left at 37°C for 30 minutes. The absorbances A1, A2, A3, and A4 at a wavelength of 660 nm were measured for these solutions. 2 mL of 0.2 mol / L hydrochloric acid TS was measured, and 5 mL of 0.55 mol / L sodium carbonate TS and 1 mL of Folin's TS (1 → 3) were added. The mixture was immediately shaken and left at 37°C for 30 minutes. The resulting solution was used as a control (blank solution) and similar measurements were performed.A calibration curve was prepared with absorbances A1, A2, A3, and A4 on the vertical axis and the amount of tyrosine (μg) in 2 mL of each solution on the horizontal axis, and the amount of tyrosine (μg) was determined for an absorbance difference of 1. Protease activity (U / g, U / mL) = (AT - AB) x F x 1 1 / 2 x 1 / 10 x 1 / M AT: absorbance of enzyme reaction solution AB: absorbance of blank F: amount of tyrosine (μg) when the absorbance difference was 1, determined from the tyrosine calibration curve 1 1 / 2: conversion coefficient for total solution volume after reaction was stopped 1 / 10: conversion coefficient for reaction time per minute M: amount of sample (g or mL) in 1 mL of sample solution.

[0078] <Method> 10 parts by weight of pea protein isolate (protein content 80%), 20 parts by weight of coconut oil, and 47.5 parts by weight of water were mixed and homogenized, and then treated at 50°C for 30 minutes while stirring. An enzyme was added to the mixture to achieve the activity indicated in the table below, and the mixture was treated at 50°C for 2 hours while stirring. 20 parts by weight of starch was then added, and the mixture was treated at 50°C for 10 minutes while stirring. The enzyme-treated composition was heat-treated at 95°C for 20 minutes while stirring, followed by addition of lactic acid until a pH of 4.3 was reached, and then heat-treated at 95°C for an additional 10 minutes. The heat-treated composition was placed in a mold and cooled at 4°C for 24 hours to obtain a plant-based cheese. The plant-based cheese was removed from the mold and cut into pieces 1 cm high and 1.3 cm in diameter. To evaluate the thermal meltability of the plant-based cheese, the cut pieces were placed in a 180°C oven and left for 10 minutes. The cut pieces were then cooled to room temperature. The presence or absence of thermal meltability and self-supporting ability after heat treatment was confirmed for each plant-based cheese.

[0079] <Evaluation> <Heat-melting property> The heat-melting property of the plant-based cheese was determined by the following method. Heat-melting property was evaluated by the Schreiber test. Specifically, a sample was cut using a round stainless steel mousse ring with a diameter of 3.2 cm and a height of 1 cm. A target-type template with concentric numbers (the innermost circle (number 0) had a diameter of 3.2 cm, followed by circles with diameters increasing by 0.2 cm each) was placed at the bottom of a Petri dish, and the sample was placed so that it fit within the circle numbered 0. The sample was heated in an oven at 180°C for 15 minutes and then cooled to room temperature. The heat-melting property of the sample was evaluated by measuring the spreading distance and area of ​​the sample after heating. Note that if the sample melted, lost its shape, and spread upon heating, it was determined to have heat-melting property.

[0080] <Self-Standing Ability> The self-standing ability of the plant-based cheese was determined by the following method. Specifically, a sample was cut using a round stainless steel mousse ring with a diameter of 3.2 cm and a height of 1 cm. If the sample maintained its shape and was self-standing when removed from the mousse ring after cutting, it was determined to be self-standing.

[0081]

[0082] The plant-based cheese produced using bacterial protease retained its self-supporting property after heat treatment but did not have heat-melting properties. The plant-based cheese produced using fungal protease retained its self-supporting property and had improved heat-melting properties. However, stretchability was not improved. The plant-based cheese obtained in the examples was able to achieve heat-melting properties without adding additives such as gums that have the effect of increasing solubility during heating.

Claims

1. A method for producing a gel-like vegetable protein composition, comprising: allowing a filamentous fungus-derived protease to act on a vegetable protein-containing raw material; and performing a heat treatment after the action of the filamentous fungus-derived protease.

2. The method for producing a gelatinous vegetable protein composition according to claim 1, wherein the heating temperature in the heat treatment is above 65°C.

3. A method for producing a gel-like vegetable protein composition according to claim 1 or 2, wherein the moisture content of the vegetable protein-containing raw material is 60% by mass or more.

4. A method for producing a gel-like vegetable protein composition according to claim 1 or 2, wherein the vegetable protein content contained in the vegetable protein-containing raw material is 5 to 14 mass %.

5. A method for producing a gelatinous vegetable protein composition according to claim 1 or 2, wherein the vegetable protein-containing raw material is a dispersion of vegetable protein isolate.

6. A method for producing a gelatinous vegetable protein composition according to claim 1 or 2, wherein the protein contained in the vegetable protein-containing raw material is pea protein.

7. A method for producing a gel-like vegetable protein composition according to claim 1 or 2, wherein the protease derived from a filamentous fungus is an acidic protease derived from a filamentous fungus.

8. A method for producing a gel-like vegetable protein composition according to claim 1 or 2, wherein the act of the filamentous fungus-derived protease is acted on a mixed raw material containing a vegetable protein-containing raw material and starch, and the gel-like vegetable protein composition is vegetable cheese.

9. A method for gelling a vegetable protein-containing raw material, comprising: allowing a filamentous fungus-derived protease to act on the vegetable protein-containing raw material; and performing a heat treatment after the action of the filamentous fungus-derived protease.

10. A method for gelling a vegetable protein-containing material according to claim 9, wherein the heating temperature in the heat treatment is above 65°C.

11. A method for gelling a vegetable protein-containing raw material according to claim 9 or 10, wherein the moisture content of the vegetable protein-containing raw material is 60% by mass or more.

12. A method for gelling a vegetable protein-containing raw material according to claim 9 or 10, wherein the vegetable protein content of the vegetable protein-containing raw material is 5 to 14 mass %.

13. A method for gelling a vegetable protein-containing material according to claim 9 or 10, wherein the vegetable protein-containing material is a dispersion of vegetable protein isolate.

14. A method for gelling a vegetable protein-containing material according to claim 9 or 10, wherein the protein contained in the vegetable protein-containing material is pea protein.

15. A method for gelling a vegetable protein-containing material according to claim 9 or 10, wherein the protease derived from a filamentous fungus is an acidic protease derived from a filamentous fungus.

16. A method for gelling a vegetable protein-containing material as described in claim 9 or 10, wherein the action of the filamentous fungus-derived protease is to act on a mixed material containing a vegetable protein-containing material and starch.

17. A gelling agent for pea protein-containing raw materials, containing a protease derived from a filamentous fungus.

18. The gelling agent according to claim 17, wherein the filamentous fungal protease is a filamentous fungal acid protease.

19. A pea protein gel composition obtained by allowing the gelling agent according to claim 17 or 18 to act on a pea protein-containing raw material.

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