Method for producing vegetable cheese

Abstract

The purpose of the present invention is to provide a technique for producing a vegetable cheese capable of imparting improved extensibility to a vegetable cheese. The extensibility of the vegetable cheese obtained by a method for producing a vegetable cheese, the method comprising (a) a step for causing a protease to act on a material containing a vegetable protein, (b) a step for inactivating the protease, and (c) a step for mixing starch.

Description

Technical Field

[0001] The present invention relates to a method for producing vegetable cheese. More specifically, the present invention relates to a method for producing vegetable cheese having extensibility due to heating. Background Art

[0002] Plant-based protein foods have become increasingly popular as an alternative to animal-based protein foods due to various reasons, including the recent health craze, responses to allergy problems, and religious reasons.

[0003] The composition of plant protein materials is very different from that of animal protein materials. Therefore, in the creation of plant protein foods, various processing technologies have been studied to make the flavor and taste of plant protein foods closer to those of animal protein foods.

[0004] Among the properties of cheese made from animal milk, the most characteristic property is the property of stretching when heated (hereinafter, this property is also described as "extensibility"). This property is related to casein contained in animal milk and is one of the reasons why cheese is appetizing. On the other hand, plant-based cheese, which has a completely different protein composition, does not have extensibility.

[0005] Until now, studies have been conducted on imparting to vegetable cheese the property of stretching not limited to the heated state. Patent Document 1 discloses that, for the purpose of providing a cheese-like food that exhibits good stringiness even in a temperature range of 4°C to 60°C, an acetylated or etherified processed starch is used in a cheese-like food, the water content is adjusted to a range of 47 to 90% by weight, and the hardness based on a rheometer measurement value at 5°C is adjusted to 1 g to 300 g / 0.785 cm 2 (1 cm diameter plunger, table speed 5 cm / min, manufactured by Fudo Industry Co., Ltd.) Prior art literature Patent Literature

[0006] Patent Document 1: Japanese Patent Application Publication No. 2006-254742 Summary of the invention Technical problem to be solved by the invention

[0007] In order to impart stretching properties to vegetable cheese, processed starch and water have been adjusted to give the vegetable cheese stretchability. However, such adjustments alone have limited effects on imparting stretchability to vegetable cheese, and therefore a technology that can further improve this property is desired.

[0008] Therefore, an object of the present invention is to provide a technology for producing vegetable cheese that can impart improved extensibility to vegetable cheese. Technical solutions for solving technical problems

[0009] The present inventors have found that the extensibility of the obtained vegetable cheese is improved by adding protease to a material containing vegetable protein and then mixing starch after heat-inactivating the protease. The present invention has been completed after further studies based on this finding.

[0010] That is, the present invention provides the following aspects. Item 1. A method for producing vegetable cheese, comprising: (a) allowing a protease to act on a material containing vegetable protein; (b) deactivating the protease; and (c) mixing starch. Item 2. The production method according to Item 1, wherein at least a protease derived from a filamentous fungus is used as the protease. Item 3. The production method according to Item 1, wherein the protease is a protease derived from filamentous fungi and / or a protease derived from bacteria. Item 4. The production method according to Item 2 or 3, wherein the protease derived from filamentous fungi is a protease derived from the genus Aspergillus. Item 5. The production method according to any one of Items 1 to 4, wherein a peptidase is further used in the step (a), and the peptidase is also inactivated in the step (b). Item 6. The production method according to any one of Items 1 to 5, wherein in the step (a), the material containing plant protein contains an organic acid. Item 7. The production method according to any one of Items 1 to 6, wherein the amount of the starch used in the step (c) is 0.2 to 1 part by weight per 1 part by weight of the vegetable protein. Item 8. The production method according to any one of Items 1 to 7, wherein the protease activity of the protease is 50 to 26,000 U per 1 g of the vegetable protein. Item 9. A method for improving the extensibility of vegetable cheese, wherein, in the production of vegetable cheese, the following steps are performed: (a) a step of allowing a protease to act on a material containing vegetable protein; (b) a step of inactivating the protease; and (c) a step of mixing starch. Item 10. A plant-based cheese obtained by the production method according to any one of Items 1 to 8. Effects of the Invention

[0011] According to the present invention, a technology for producing vegetable cheese capable of imparting improved extensibility to vegetable cheese is provided. DETAILED DESCRIPTION

[0012] 1. Method for producing plant-based cheese The method for producing vegetable cheese of the present invention is characterized in that it includes the following steps: (a) a step of allowing protease to act on a material containing vegetable protein (hereinafter, also described as "step (a)"); (b) a step of inactivating the above-mentioned protease (hereinafter, also described as "step (b)"); and (c) a step of mixing starch (hereinafter, also described as "step (c)"). The production method of the present invention includes steps (a), (b) and (c) in sequence. According to the present invention, the extensibility of the obtained vegetable cheese can be improved. In addition, in a preferred embodiment of the present invention, for the obtained vegetable cheese, in addition to the extensibility, the hot meltability can also be improved. The following is a detailed description of the method for producing the extensible vegetable cheese of the present invention.

[0013] 1-1.(a) Process In the step (a), a protease is allowed to act on a material containing a vegetable protein to obtain an enzyme-treated product.

[0014] 1-1-1. Ingredients containing plant protein There are no particular limitations on the plants that are the source of the vegetable protein, and examples thereof include beans such as peas, soybeans, broad beans, chickpeas, and lentils; cereals such as barley, wheat, oats, rice, buckwheat, barnyard grass, and chestnuts; and nuts such as almonds, cashews, hazelnuts, pecans, macadamia nuts, pistachios, walnuts, Brazil nuts, peanuts, and coconuts. As the vegetable protein derived from these plants, one kind may be used alone, or two or more kinds from different sources may be used in combination.

[0015] Among them, from the viewpoint of further improving the extensibility, or from the viewpoint of improving the hot melt property in addition to this viewpoint, preferably, protein from beans, more preferably, protein from peas, broad beans, chickpeas, and lentils, and even more preferably, protein from peas.

[0016] The content of the vegetable protein in the material containing the vegetable protein is not particularly limited, and for example, 1 to 30% by weight can be cited. From the viewpoint of further improving the extensibility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the content of the vegetable protein in the material is preferably 4 to 25% by weight, more preferably 9 to 20% by weight, and even more preferably 14 to 20% by weight.

[0017] The material containing vegetable protein may contain any material component used for vegetable cheese (hereinafter, also described as "other material components") as a component other than vegetable protein. Examples of other material components include vegetable oils and fats, thickening polysaccharides, starch, water, salt, organic acids, and calcium salts, and one or more of these components may be contained in the material containing vegetable protein.

[0018] When the material containing vegetable protein contains other material components, the other material components preferably contain organic acid and water from the viewpoint of further improving the elongation and the heat-melting property. It should be noted that the organic acid may be mixed into the enzyme-treated product after the enzyme is inactivated in step (c) instead of being included in the material containing vegetable protein in this step, but it is more preferable to include it in the material containing vegetable protein in this step from the viewpoint of further improving the elongation and the heat-melting property.

[0019] As organic acid, there is no particular limitation, and lactic acid, citric acid, acetic acid, succinic acid, malic acid, fumaric acid, propionic acid, pyruvic acid, orotic acid etc. can be mentioned. These organic acids can be used alone or in combination. Among these organic acids, lactic acid is preferably mentioned.

[0020] When the material containing vegetable protein contains an organic acid, the content of the organic acid in the material is not particularly limited, but from the viewpoint of further improving the elongation, or from the viewpoint of improving the hot melt property in addition to this viewpoint, it can be, for example, 0.1 to 1% by weight, more preferably 0.3 to 0.5% by weight.

[0021] When the material containing vegetable protein contains water, the water content in the material is not particularly limited, but from the viewpoint of further improving extensibility or from the viewpoint of improving thermal meltability in addition to this viewpoint, it can be, for example, 45 to 70% by weight, preferably 50 to 65% by weight, and more preferably 55 to 60% by weight.

[0022] In this process, among the above-mentioned other material components, components other than organic acid and water (vegetable oil, thickening polysaccharide, starch, salt and calcium salt) are preferably not included in the material containing vegetable protein. However, the present invention does not exclude the situation that the components other than organic acid and water are included in the material containing vegetable protein. For example, as the amount in the case of containing starch, it is preferred to cite an amount less than the amount usually contained in vegetable cheese, and as such an amount, for example, less than 4% by weight, preferably less than 2% by weight, more preferably less than 1% by weight, and further preferably less than 0.1% by weight can be cited. It should be noted that more specific examples of vegetable oil, thickening polysaccharide (excluding starch), starch, salt and calcium salt are described in detail in "1-3. (c) process".

[0023] 1-1-2. Protease In the present invention, protease refers to endopeptidase. There is no particular limitation on the source of protease, for example, protease derived from filamentous fungi such as Aspergillus, Mucor, Neurospora, Penicillium, Rhizomucor, Rhizopus, Sclerotinia, etc.; protease derived from yeast of Saccharomyces; protease derived from bacteria such as Bacillus and Geobacillus; protease derived from actinomycetes of Streptomyces. These proteases can be used alone or in combination.

[0024] Among these proteases, from the viewpoint of further improving the extensibility, or from the viewpoint of improving the thermal meltability in addition to this viewpoint, it is preferred to use at least a protease derived from filamentous fungi, and more preferably a protease derived from filamentous fungi and a protease derived from bacteria are used in combination. Furthermore, among the proteases derived from filamentous fungi, from the viewpoint of further improving the extensibility, or from the viewpoint of improving the thermal meltability in addition to this viewpoint, it is preferred to cite proteases derived from Aspergillus oryzae and Aspergillus niger, and it is more preferred to cite proteases derived from Aspergillus oryzae. Furthermore, among proteases derived from bacteria, from the viewpoint of further improving extensibility, or from the viewpoint of improving hot meltability in addition to this viewpoint, preferred are proteases derived from Bacillus stearothermophilus, Bacillus licheniformis, Bacillus amyloliquefaciens, and Geobacillus species thereof, and more preferred is a protease derived from Geobacillus stearothermophilus (including strains formerly known as Bacillus stearothermophilus).

[0025] The protease can be used in an embodiment in which the protease activity per 1 g of the vegetable protein is, for example, 5 to 50,000 U, 10 to 30,000 U, or 50 to 26,000 U. From the viewpoint of further improving the extensibility, or from the viewpoint of improving the hot melt property in addition to this viewpoint, the protease can be used in an embodiment in which the protease activity per 1 g of the vegetable protein is preferably 200 to 24,000 U, 240 to 22,000 U, 300 to 20,000 U, 350 to 15,000 U, or 400 to 13,000 U, more preferably 700 to 6,000 U, and even more preferably 1,100 to 3,600 U, 1,100 to 2,900 U, or 1,100 to 2,300 U.

[0026] When a protease derived from filamentous fungi is used as the protease, the protease derived from filamentous fungi can be used in a manner such that the protease activity per 1 g of vegetable protein reaches, for example, 20 to 30,000 U, 100 to 25,000 U, or 190 to 20,000 U. From the viewpoint of further improving the extensibility, or from the viewpoint of improving the thermal meltability in addition to this viewpoint, the protease derived from filamentous fungi can be used in a manner such that the protease activity per 1 g of vegetable protein reaches preferably 300 to 10,000 U or 400 to 7,500 U, more preferably 500 to 5,000 U, and even more preferably 900 to 3,000 U, 1,600 to 2,500 U, or 1,850 to 2,000 U.

[0027] When a protease derived from bacteria is used as the protease, the protease derived from bacteria can be used in a manner such that the protease activity per 1 g of the vegetable protein is, for example, 5 to 10,000 U, 10 to 8,000 U, or 50 to 6,000 U. From the viewpoint of further improving the extensibility, or from the viewpoint of improving the hot melt property in addition to this viewpoint, the protease derived from bacteria can be used in a manner such that the protease activity per 1 g of the vegetable protein is preferably 100 to 3,000 U, more preferably 200 to 1,000 U, further preferably 250 to 600 U, or 250 to 300 U.

[0028] When a protease derived from filamentous fungi and a protease derived from bacteria are used in combination as proteases, the ratio of the usage of the protease derived from filamentous fungi and the protease derived from bacteria is determined based on the usage of the above-mentioned proteases. However, from the viewpoint of further improving the extensibility, or from the viewpoint of improving the hot melt property in addition to this viewpoint, the usage of the protease derived from bacteria relative to 1U of the protease derived from filamentous fungi is preferably 0.05 to 5U or 0.1 to 3U, more preferably 0.15 to 2U, further preferably 0.2 to 1U, and further preferably 0.25 to 0.4U.

[0029] It should be noted that the protease activity is determined by the Folin method using casein as a substrate. That is, the activity of the protease is: using casein as a substrate, the enzyme reaction is carried out by a conventional method at a pH set according to the optimal pH of the protease to be measured, and the amount of enzyme that causes an increase in the color-developing substance of the Folin test solution equivalent to 1 μg of tyrosine within 1 minute is taken as 1 unit (1U) of enzyme activity.

[0030] 1-1-3. Peptidase In the present invention, in addition to the protease treatment step, a step of treating with a peptidase (hereinafter also referred to as a "peptidase treatment step") may be further included from the viewpoint of further improving the elongation and / or hot melt properties.

[0031] The peptidase treatment step may be performed simultaneously with the protease treatment step or after the protease treatment step. That is, the material containing vegetable protein may be treated by allowing both the above-mentioned protease and peptidase to act simultaneously, or the material containing vegetable protein may be treated by allowing the protease to act and then further treated by allowing the peptidase to act.

[0032] In the present invention, peptidase refers to exopeptidase. There is no particular limitation on the source of peptidase, for example, peptidase derived from fungi of the genus Rhizopus, Aspergillus, etc. can be used; peptidase derived from actinomycetes of the genus Streptomyces; peptidase derived from bacteria of the genus Bacillus, Geobacillus, Lactobacillus, Lactococcus, etc., more specifically, peptidase derived from fungi of the genus Rhizopus, Aspergillus, etc. can be used, and peptidase derived from Rhizopus oryzae and Aspergillus oryzae can be used more specifically. These peptidases can be used alone or in combination.

[0033] Among these peptidases, from the viewpoint of further improving the elongation property, or from the viewpoint of improving the hot melt property in addition to this viewpoint, a peptidase derived from the genus Rhizopus is preferred, and a peptidase derived from Rhizopus oryzae is more preferred.

[0034] The peptidase can be used so that the peptidase activity per 1 g of the plant protein is, for example, 0.001 to 1 U, preferably 0.005 to 0.6 U, more preferably 0.01 to 0.4 U, further preferably 0.02 to 0.2 U, and further preferably 0.03 to 0.1 U.

[0035] It should be noted that the peptidase activity is measured using L-leucyl-glycyl-glycine as a substrate by a method based on the 9th edition of the Food Additive Code. Specifically, an enzyme reaction is carried out using L-leucyl-glycyl-glycine as a substrate by a conventional method, and the amount of enzyme that causes an increase in the ninhydrin coloring substance equivalent to 1 μmol of leucine within 1 minute is taken as 1 unit (1U) of enzyme activity.

[0036] 1-1-4. Processing conditions, etc. The specific procedure of the protease treatment in this step is not particularly limited as long as the material containing the vegetable protein is brought into contact with the protease under an environment where the protease effectively acts.

[0037] The reaction temperature of the enzyme treatment in this step is not particularly limited, and can be appropriately determined by those skilled in the art based on the optimal temperature of the enzyme to be used, and is, for example, 40 to 60°C, preferably 45 to 55°C.

[0038] The enzyme treatment reaction time in this step is not particularly limited, and can be appropriately determined according to the feeding scale of the material containing the vegetable protein, and for example, more than 15 minutes can be cited, preferably more than 20 minutes. The upper limit of the range of the enzyme treatment reaction time is not particularly limited, and for example, less than 1 hour or less than 40 minutes can be cited.

[0039] 1-2. (b) Process In the step (b), the protease used in the step (a) is inactivated, or when a peptidase is further used in the step (a), the peptidase is also inactivated, thereby obtaining an enzyme-treated product after the enzyme is inactivated.

[0040] Regarding the inactivation method, the enzyme-treated product obtained in step (a) is subjected to conditions that inactivate the enzyme used. As the inactivation conditions, the conditions for denaturing the protease, or the protease and the peptidase used in step (a) can be appropriately selected, and typically they are heat-inactivated. As specific temperature conditions for heat inactivation, they can be set according to the thermal properties of the protease, or the protease and the peptidase actually used in step (a), for example, 70°C or more, preferably 80°C or more, and more preferably 85°C or more. There is no particular limitation on the time for heat inactivation, and for example, 10 to 20 minutes can be cited.

[0041] 1-3.(c) Process In the step (c), starch is mixed with the enzyme-treated product obtained in the step (b) after the enzyme is inactivated, thereby obtaining a vegetable cheese dough.

[0042] The starch is not particularly limited, and any starch that can impart extensibility to the vegetable cheese can be used without particular limitation. Specific examples of plants from which the starch is derived include cassava, potato, sweet potato, and kudzu. Starches derived from these plants may be used alone or in combination of two or more from different sources.

[0043] Among them, from the viewpoint of further improving the ductility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, cassava starch (tapioca starch) and potato starch are preferred, and cassava starch (tapioca starch) is more preferred.

[0044] The amount of starch mixed in the enzyme-treated product after enzyme inactivation is not particularly limited as long as the effects of the present invention can be obtained. For example, the amount of starch mixed in the vegetable cheese dough after mixing is 4% by weight or more. From the viewpoint of further improving the elongation, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the amount of starch mixed in the vegetable cheese dough is preferably 5% by weight or more, more preferably 6% by weight or more, and even more preferably 7% by weight or more.

[0045] The upper limit of the mixing amount of starch in the enzyme-treated product after enzyme inactivation is not particularly limited. From the viewpoint of appropriately mixing a prescribed amount of vegetable protein, for example, 20% by weight or less can be cited based on the content in the mixed vegetable cheese dough. In addition, the manufacturing method of the present invention has an excellent effect of improving the ductility, so even when the starch content is relatively small, the ductility can be effectively improved. From such a viewpoint, the upper limit of the mixing amount of starch in the enzyme-treated product after enzyme inactivation can be cited as preferably 17% by weight or less, more preferably 15% by weight or less, and further preferably 13% by weight or less.

[0046] In addition, the ratio of the vegetable protein used in the preparation of the enzyme-treated product after enzyme inactivation to the starch in this step is determined according to the content of the above-mentioned components. The content of starch per 1 part by weight of the vegetable protein used in the preparation of the enzyme-treated product after enzyme inactivation is preferably 0.2 to 1 part by weight, more preferably 0.3 to 0.8 part by weight, and even more preferably 0.4 to 0.6 part by weight.

[0047] In step (c), in addition to the above-mentioned starch, any other material components for producing vegetable cheese may be added. Examples of such other material components include vegetable oils and fats, thickening polysaccharides, salt, calcium salts, and organic acids.

[0048] As vegetable oil, there is no particular limitation, for example, canola oil (rapeseed oil), coconut oil, corn oil, olive oil, soybean oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, sunflower oil, safflower oil, linseed oil, palm oil, palm kernel oil, palm fruit oil, babassu oil, shea butter, mango fat, cocoa butter, wheat germ oil, rice bran oil, etc. can be mentioned. These vegetable oils can be used alone or in combination of two or more. Among these vegetable oils, from the viewpoint of further improving extensibility, or from the viewpoint of also improving hot meltability in addition to this viewpoint, preferably canola oil (rapeseed oil), coconut oil, sunflower oil can be mentioned, and more preferably canola oil (rapeseed oil) and coconut oil.

[0049] When vegetable oils and fats are mixed with the enzyme-treated product after enzyme inactivation, the mixing amount thereof is not particularly limited, but from the viewpoint of further improving the ductility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the content in the vegetable cheese dough after mixing is, for example, 4 to 30% by weight, preferably 6 to 25% by weight, more preferably 8 to 20% by weight, and even more preferably 9 to 15% by weight.

[0050] As thickening polysaccharides, there is no particular limitation, and for example, locust bean gum, guar gum, carrageenan, xanthan gum, tragacanth gum, tamarind gum, pectin, gum arabic, curdlan, tara gum, gellan gum, dawa gum, CMC (carboxymethyl cellulose), sodium alginate, pullulan, etc. can be cited, and carrageenan, etc. are preferably cited. These thickening polysaccharides can be used alone or in combination of two or more. Among these thickening polysaccharides, from the viewpoint of further improving extensibility, or from the viewpoint of also improving hot meltability in addition to this viewpoint, carrageenan is preferably cited.

[0051] When a thickening polysaccharide is mixed with the enzyme-treated product after enzyme inactivation, the mixing amount thereof is not particularly limited, but from the viewpoint of further improving the ductility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the content in the vegetable cheese dough after mixing is, for example, 0.1 to 2% by weight, more preferably 0.5 to 1.5% by weight, and even more preferably 0.8 to 1.2% by weight.

[0052] When salt is mixed with the enzyme-treated product after enzyme inactivation, the amount thereof is not particularly limited, but from the viewpoint of further improving ductility or from the viewpoint of improving hot meltability in addition to this viewpoint, the amount thereof in the vegetable cheese dough after mixing is, for example, 0.1 to 2% by weight, more preferably 0.5 to 0.7% by weight.

[0053] The calcium salt is not particularly limited, and examples thereof include calcium gluconate, calcium lactate, and calcium phosphate. One of these calcium salts may be used alone, or two or more of these calcium salts may be used in combination. Among these calcium salts, calcium phosphate is preferably used from the viewpoint of further improving ductility or from the viewpoint of also improving thermal solubility in addition to this viewpoint.

[0054] When a calcium salt is mixed with the enzyme-treated product after enzyme inactivation, the mixing amount thereof is not particularly limited, but from the viewpoint of further improving the ductility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the content in the vegetable cheese dough after mixing is, for example, 0.5 to 4% by weight, more preferably 1.5 to 2.0% by weight.

[0055] There are no particular limitations on the organic acid, and specific examples thereof include lactic acid, citric acid, acetic acid, succinic acid, malic acid, fumaric acid, propionic acid, pyruvic acid, orotic acid, etc., as described in the above-mentioned "1-1-1. Materials containing vegetable proteins". These organic acids may be used alone or in combination of multiple types. Of these organic acids, lactic acid is preferred.

[0056] When an organic acid is mixed with the enzyme-treated product after enzyme inactivation, the mixing amount thereof is not particularly limited, but from the viewpoint of further improving the ductility, or from the viewpoint of improving the hot meltability in addition to this viewpoint, the content in the vegetable cheese dough after mixing is, for example, 0.1 to 1% by weight, more preferably 0.3 to 0.5% by weight.

[0057] 1-4. Other processes The production method of the present invention may include any other steps for obtaining plant-based cheese in addition to the steps (a) to (c) described above.

[0058] As other steps, there may be mentioned a step of heating the vegetable cheese dough obtained in the step (c) to cook the vegetable cheese, and a step of cooling the obtained vegetable cheese.

[0059] The heating temperature in the step of heating the vegetable cheese dough can be selected without particular limitation and set to a temperature condition that allows the vegetable cheese dough to exhibit the extensibility due to the starch mixed in the step (c). Specific examples of the temperature condition include 70 to 110°C, preferably 80 to 100°C, and more preferably 85 to 95°C.

[0060] The heating time in the step of heating the vegetable cheese dough is not particularly limited, and is, for example, 5 to 30 minutes, preferably 10 to 20 minutes.

[0061] In the cooling step, the obtained vegetable cheese may be cooled in a state where it is filled in a suitable container of an appropriate size. The temperature in the cooling step is not particularly limited, and examples thereof include 2 to 5°C.

[0062] 2. Methods for improving the extensibility of plant-based cheese As described above, in the production of vegetable cheese, by sequentially performing the steps (a), (b), and (c), the extensibility of the obtained vegetable cheese can be improved. Therefore, the present invention also provides a method for improving the extensibility of vegetable cheese, wherein, in the production of vegetable cheese, the following steps are performed: (a) a step of allowing a protease to act on a material containing vegetable protein; (b) a step of inactivating the protease; and (c) a step of mixing starch.

[0063] In the method for improving the extensibility of the present invention, the types and amounts of the components used are as described in the above-mentioned section "1. Method for producing plant-based cheese".

[0064] 3. Plant-based cheese The vegetable cheese obtained by the production method described in the column "1. Production method of vegetable cheese" has improved extensibility. Therefore, the present invention also provides vegetable cheese obtained by a production method of vegetable cheese comprising (a) a step of allowing a protease to act on a material containing vegetable protein, (b) a step of inactivating the protease, and (c) a step of mixing starch.

[0065] The types and amounts of components contained in the vegetable cheese of the present invention are as described in the above-mentioned "1. Method for producing vegetable cheese". Example

[0066] Hereinafter, the present invention will be specifically described with reference to Examples, but the present invention is not construed as being limited to the following Examples.

[0067] [Enzyme used] The enzymes shown in the following table were used. All the enzymes used were manufactured by Amano Enzyme Products Co., Ltd. [Table 1]

[0068] [Protease activity assay] After heating 5 mL of 0.6% (v / w) casein solution (0.05 mol / L sodium hydrogen phosphate, pH 8.0 [in the case of bacterial protease], or 0.7% (v / w) lactic acid, pH 3.0 [in the case of filamentous bacterial protease]) at 37°C for 10 minutes, 1 mL of the sample solution containing protease was added and immediately shaken and mixed. After the liquid was placed at 37°C for 10 minutes, 5 mL of trichloroacetic acid test solution (containing 1.8% trichloroacetic acid, 1.8% sodium acetate and 0.33 mol / L acetic acid [in the case of bacterial protease], or containing 0.44 mol / L trichloroacetic acid [in the case of filamentous bacterial protease]) was added and shaken and mixed, and the mixture was placed at 37°C for 30 minutes again and filtered. The first 3 mL of filtrate was removed, the next 2 mL of filtrate was weighed, 5 mL of 0.55 mol / L sodium carbonate test solution and 1 mL of Folin test solution (1→3) were added, and the mixture was shaken and mixed thoroughly, and placed at 37°C for 30 minutes. For this liquid (enzyme reaction solution), absorbance AT at a wavelength of 660 nm was measured using water as a control.

[0069] Separately, 1 mL of a sample solution containing protease was weighed, 5 mL of a trichloroacetic acid test solution (containing 1.8% trichloroacetic acid, 1.8% sodium acetate and 0.33 mol / L acetic acid [in the case of bacterial protease], or containing 0.44 mol / L trichloroacetic acid [in the case of filamentous bacterial protease]) was added and shaken, and then 5 mL of a 0.6% (v / w) casein solution (0.05 mol / L sodium hydrogen phosphate, pH 8.0 [in the case of bacterial protease], or 0.7% (v / w) lactic acid, pH 3.0 [in the case of filamentous bacterial protease]) was added, immediately shaken and mixed, and the mixture was left at 37° C. for 30 minutes. The absorbance AB of the obtained liquid (blank) was measured in the same manner as the above enzyme reaction solution. The amount of enzyme that causes an increase in the color-developing substance of the Folin test solution equivalent to 1 μg of tyrosine in 1 minute was defined as 1 unit (1U).

[0070] Weigh 1mL, 2mL, 3mL and 4mL of 1mg / mL tyrosine standard stock solution (0.2mol / L hydrochloric acid), add 0.2mol / L hydrochloric acid test solution to make 100mL. Weigh 2mL of each liquid, add 5mL of 0.55mol / L sodium carbonate test solution and 1mL of Folin test solution (1→3), shake and mix immediately, and place at 37°C for 30 minutes. For these liquids, weigh 2mL of 0.2mol / L hydrochloric acid test solution and measure the absorbance A1, A2, A3 and A4 at a wavelength of 660nm. Take the absorbance A1, A2, A3 and A4 on the vertical axis and the amount of tyrosine (μg) in 2mL of each liquid on the horizontal axis, make a standard curve, and find the amount of tyrosine (μg) relative to the absorbance difference 1.

[0071] [Number 1] Protease activity (U / g, U / mL) = (AT-AB) × F × 11 / 2 × 1 / 10 × 1 / M AT: absorbance of enzyme reaction solution AB: absorbance of blank F: The amount of tyrosine (μg) when the absorbance difference is 1, obtained from the tyrosine standard curve 11 / 2: Conversion factor to the total liquid volume after the reaction stops 1 / 10: Conversion factor to 1 minute of reaction time M: The amount of sample in 1 mL of sample solution (g or mL)

[0072] [Peptidase activity assay] Weigh an appropriate amount of enzyme, add water, potassium phosphate buffer (0.005 mol / L) at pH 7.0, or potassium phosphate buffer (0.005 mol / L, pH 7.0, containing zinc sulfate), dissolve or evenly disperse it to make 50 mL of liquid, or further dilute it to 10 times, 100 times, or 1000 times with water or the same buffer and use it as a sample solution.

[0073] Weigh 30 mg of L-leucyl-glycyl-glycine, add potassium phosphate buffer (0.05 mol / L) at pH 7.0 and dissolve to make 50 mL. Dilute the liquid to 10 times with potassium phosphate buffer (0.05 mol / L) at pH 7.0 and use it as substrate solution. The substrate solution is prepared at the time of use.

[0074] 1 mL of substrate solution was weighed in a stoppered test tube, heated at 37°C for 5 minutes, 0.1 mL of sample solution was added and mixed, heated at 37°C for 60 minutes, heated in a boiling water bath for 5 minutes, and cooled to room temperature. 2 mL of ninhydrin·2-methoxyethanol·citric acid buffer solution and 0.1 mL of tin (II) chloride solution were added to the liquid, the stopper was covered and heated in a boiling water bath for 20 minutes. After cooling, 10 mL of 1-propanol (1→2) was added and mixed by shaking to prepare a test solution. Separately, 0.1 mL of sample solution was weighed in a stoppered test tube, heated in a boiling water bath for 5 minutes. After cooling, 1 mL of substrate solution was added and mixed, heated at 37°C for 5 minutes, and cooled to room temperature. 2 mL of ninhydrin·2-methoxyethanol·citric acid buffer solution and 0.1 mL of tin (II) chloride solution were added to the liquid, the stopper was covered and heated in a boiling water bath for 20 minutes. After cooling, add 10 mL of 1-propanol (1→2) and shake to mix to prepare a comparative solution. For the test solution and the comparative solution, when the absorbance at a wavelength of 570 nm is measured within 5 to 30 minutes after preparation, the absorbance of the test solution is greater than the absorbance of the comparative solution. It should be noted that when there is turbidity in the test solution and the comparative solution whose absorbance is measured, centrifugation is performed and the supernatant is measured. The amount of enzyme that causes an increase in the ninhydrin colorimetric substance equivalent to 1 μmol of leucine within 1 minute is set to 1 unit (1U).

[0075] [Number 2] Peptidase activity (U / g, U / mL) = (AT-AB) × F × (1 / 0.1) × (1 / 60) × n AT: absorbance of enzyme reaction solution AB: absorbance of blank F: The amount of leucine when the absorbance difference is 1 obtained from the standard curve (μnol) 0.1: Enzyme solution volume (mL) 60: Reaction time (minutes) n: dilution factor

[0076] [Materials used] Commercially available materials shown in the following table were used. [Table 2]

[0077] [Test Example 1] (1) Production of plant-based cheese (1-1) Production of plant-based cheese in Comparative Examples 1 and 2 Purified water (RO water) was added to a Thermomix mixer (product name: Thermomix TM6), and while stirring at 50°C and speed 3, pea protein material, tapioca starch (only in the case of Comparative Example 1), canola oil, coconut oil, salt, tricalcium phosphate, lactic acid (only in the case of Comparative Example 1), carrageenan, and the enzymes shown in Tables 3A to 3C were added in the indicated amounts. After stirring at 50°C and speed 3 for 15 minutes, the temperature was raised to 85°C and stirred at speed 3 for 7 minutes (treatment under enzyme inactivation conditions). Only in the case of Comparative Example 2, tapioca starch and lactic acid were then added and mixed.

[0078] The obtained mixture was filled in a plastic syringe (30 mm in diameter) in an appropriate amount, and filled in 100 g each in two aluminum containers (bottom inner diameter: 5 cm in diameter), covered, cooled to 4° C., and stored. Thus, vegetable cheese was obtained (n=2 for each comparative example).

[0079] (1-2) Production of plant-based cheese of Comparative Examples 3 and 4 and Examples 1 to 10 Purified water (RO water) was added to a Thermomix mixer (product name: Thermomix TM6), and while stirring at 50°C and speed 3, lactic acid (except for Example 1), pea protein material and tapioca starch (only for Comparative Example 4), and enzymes shown in Tables 3A to 3C were added in the amounts shown. After stirring at 50°C and speed 3 for 30 minutes (step (a)), the mixture was heated to 90°C and stirred at speed 3 for 15 minutes (treatment under enzyme inactivation conditions, step (b)), and tapioca starch (except for Comparative Example 4), canola oil, coconut oil, tricalcium phosphate, lactic acid (only for Example 1), salt, and carrageenan were added and mixed in the amounts shown in Tables 3A to 3C (step (c)). After stirring at 90°C at speed 3 for 15 minutes, a suitable amount was filled in a plastic syringe (30 mm in diameter), and 100 g was filled in two aluminum containers (bottom inner diameter: 5 cm in diameter), and the mixture was covered, cooled to 4°C, and stored. Thus, vegetable cheese (n=2 for each) was obtained.

[0080] (2) Extension evaluation The vegetable cheese filled in the aluminum container was used as a sample, and a steam oven set at 110°C (to eliminate the influence of water evaporation during heating) was used to heat for 30 minutes. Then, it was taken out of the steam oven, confirmed that the internal temperature of the sample reached 70°C, and stirred with a fork. After confirming that the fork was covered with the sample, the front end of the fork was lifted at 5 cm / second so that the sample was picked up with the fork, and the distance between the lifting start point of the front end of the fork and the point where the extension of the sample broke was measured (extension length (mm)). It should be noted that in each embodiment / comparative example, the extension length was derived as the average value obtained by testing the two samples prepared in the same way. Furthermore, the relative value of the extension length of the vegetable cheese of each comparative example and each embodiment was derived when the extension length of the vegetable cheese of Comparative Example 1 manufactured without the use of an enzyme was taken as 1, as an evaluation index for improving extensibility. If the evaluation index for improving extensibility exceeds 1, it is evaluated that improved extensibility is given. In addition, the larger the evaluation index for improving extensibility, the higher the effect of improving extensibility is evaluated. The results are shown in Tables 3A to 3C.

[0081] (3) Evaluation of thermal meltability The vegetable cheese filled in the plastic syringe was taken out and cut into a sample with a thickness of 5 mm. A steam oven set to 110°C was used to heat for 15 minutes. Then, the vegetable cheese was taken out from the steam oven and the diameter (mm) after heat melting was measured. The relative value of the diameter of the heated sample was derived as the diameter expansion rate after heat melting, taking the diameter before heating as 1. Furthermore, the relative value of the diameter expansion rate after heat melting of the vegetable cheese of each comparative example and each embodiment was derived as the evaluation index for improving heat meltability, taking the diameter expansion rate after heat melting of the vegetable cheese of Comparative Example 1 manufactured without using an enzyme as 1. The larger the evaluation index for improving heat meltability, the higher the effect of improving heat meltability is evaluated to be. The results are shown in Tables 3A to 3C.

[0082] [Table 3A] In the table, the numerical value indicating the blending amount of each component is % by weight. The numerical values ​​indicated by brackets ( ) indicating the amount of enzyme added are activity values ​​per 1 g of protein.

[0083] [Table 3B] In the table, the numerical value indicating the blending amount of each component is % by weight. The numerical values ​​indicated by brackets ( ) indicating the amount of enzyme added are activity values ​​per 1 g of protein.

[0084] [Table 3C] In the table, the numerical value indicating the blending amount of each component is % by weight. The numerical values ​​indicated by parentheses, which indicate the amount of enzyme added, are activity values ​​per 1 g of protein.

[0085] As shown in Tables 3A to 3C, the extensibility of the plant-based cheeses (Comparative Examples 2 and 3) produced by adding starch treated under enzyme inactivation conditions and the plant-based cheeses (Comparative Example 4 and Examples 1 to 10) produced by using protease is improved compared to the extensibility of the plant-based cheese (Comparative Example 1) produced without using protease and without adding starch treated under enzyme inactivation conditions. Among them, the extensibility improvement effect is particularly significant in the plant-based cheeses (Examples 1 to 10) produced by using protease and adding starch treated under enzyme inactivation conditions. It should be noted that the plant-based cheeses with excellent extensibility obtained in Examples 1 to 10 substantially do not show extensibility before heating, but show excellent extensibility by heating, so it can be confirmed that the thermal characteristics similar to those seen in animal-based cheeses are reproduced.

[0086] Furthermore, as shown in Tables 3A and 3B, in Examples 1 to 10, the effect of improving the hot melt property was also obtained in Examples 2 to 10 in which the timing of adding lactic acid (organic acid) was set before the treatment under the enzyme inactivation treatment conditions.

[0087] In detail, it can be seen from Table 3A that in the case where lactic acid (organic acid) is added before enzyme treatment and starch treated under enzyme inactivation conditions is not added (specifically, Comparative Examples 1 and Comparative Examples 4) and the case where starch treated under enzyme inactivation conditions is added (Comparative Example 3 and Example 2, respectively), the latter has improved extensibility and hot melt properties, and in particular, the effect of improving hot melt properties is more significant in the case of using protease than in the case of not using protease (i.e., Comparative Example 3 compared to Comparative Example 1, Example 2 compared to Comparative Example 4). That is, the effect of improving hot melt properties shown in Example 2 (and Examples 3 to 10) is considered to be a unique effect based on the two conditions of adding starch treated under enzyme inactivation conditions and using protease.

[0088] Furthermore, it can be seen from Table 3A that in the case of adding starch treated under enzyme inactivation conditions and adding lactic acid (organic acid) after enzyme treatment (specifically, Comparative Example 2 and Example 1) and the case of adding lactic acid (organic acid) before enzyme treatment (Comparative Example 3 and Example 2, respectively), the latter has improved extensibility and hot melt properties, and in particular, the effect of improving hot melt properties is more excellent in the case of using protease than in the case of not using protease (i.e., Example 2 compared to Example 1 compared to Comparative Example 3 compared to Comparative Example 2). That is, the effect of improving hot melt properties shown in Example 2 (and Examples 3 to 10) is considered to be a unique effect based on the two conditions of adding lactic acid (organic acid) and using protease before enzyme treatment.

Claims

1. A method for producing vegetable cheese, characterized in that: Including the following processes: (a) a step of allowing a protease to act on a material containing a vegetable protein; (b) a step of inactivating the protease; and (c) A step of mixing starch.

2. The manufacturing method according to claim 1, wherein: As the protease, at least a protease derived from filamentous fungi is used.

3. The manufacturing method according to claim 1, wherein: As the protease, a protease derived from filamentous fungi and / or a protease derived from bacteria is used.

4. The manufacturing method according to claim 2 or 3, wherein: The protease derived from filamentous fungi is a protease derived from the genus Aspergillus.

5. The manufacturing method according to claim 1, wherein: In the step (a), a peptidase is further used, and in the step (b), the peptidase is also inactivated.

6. The manufacturing method according to claim 1, wherein: In the step (a), the material containing vegetable protein contains an organic acid.

7. The manufacturing method according to claim 1, wherein: The amount of the starch used in the step (c) is 0.2 to 1 part by weight per 1 part by weight of the vegetable protein.

8. The manufacturing method according to claim 1, wherein: The protease activity of the protease is 50 to 26000 U per 1 g of the vegetable protein.

9. A method for improving the extensibility of plant-based cheese, characterized in that: In the production of plant-based cheese, the following steps are carried out: (a) a step of allowing a protease to act on a material containing a vegetable protein; (b) a step of inactivating the protease; and (c) A step of mixing starch.

10. A plant-based cheese, characterized in that: The method is obtained by the production method according to claim 1.

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