CN116940240A - Process for producing malleable cheese substitute - Google Patents

Process for producing malleable cheese substitute Download PDF

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Publication number
CN116940240A
CN116940240A CN202280017102.7A CN202280017102A CN116940240A CN 116940240 A CN116940240 A CN 116940240A CN 202280017102 A CN202280017102 A CN 202280017102A CN 116940240 A CN116940240 A CN 116940240A
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China
Prior art keywords
protease
weight
starch
vegetable protein
per
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CN202280017102.7A
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奥田启太
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Amano Enzyme Inc
Tianye Enzyme Preparation Usa Co ltd
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Amano Enzyme Inc
Tianye Enzyme Preparation Usa Co ltd
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Priority claimed from PCT/JP2022/008083 external-priority patent/WO2022181810A1/en
Publication of CN116940240A publication Critical patent/CN116940240A/en
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Abstract

The present invention aims to provide a technique for producing a cheese substitute, which can impart improved extensibility to a cheese substitute comprising a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein. An improvement in the extensibility of a cheese substitute obtained by a method of manufacturing an extensible cheese substitute, the method of manufacturing an extensible cheese substitute comprising: a step of treating a material composition containing a protease and optionally an amylase with an enzyme preparation, wherein the material composition contains a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein, and the enzyme preparation is used such that the starch gelatinization ability of the amylase per 1g of the starch is 8U or less, relative to 10 ten thousand U of protease activity of the protease per 1g of the vegetable protein.

Description

Process for producing malleable cheese substitute
Technical Field
The present invention relates to a method of making a malleable cheese alternative. More specifically, the present invention relates to a method for producing a malleable cheese alternative using a plant protein having heat ductility as a raw material.
Background
The popularity of vegetable protein foods has increased as substitutes for animal protein foods for various reasons such as recent health heat, response to allergic problems, religious reasons, and the like.
Since vegetable protein materials are far different from animal protein materials, various processing techniques have been studied to bring flavors, taste, and the like close to those of animal protein foods in the creation of vegetable protein foods.
Cheese-like foods using vegetable proteins as raw materials, so-called vegetable cheeses, have been studied as candidates for a substitute for cheeses using animal milk as raw materials. For example, patent document 1 describes a cream cheese-like food comprising an emulsified product of a soybean protein hydrolysate and an oil or fat, which is oxidized in a neutral or alkaline region to act a protease, which is not distinguished from cream cheese, and which has a smooth and good flavor.
Prior art literature
Patent literature
Patent document 1: international publication No. 2006/135089
Disclosure of Invention
Technical problem to be solved by the invention
Among the characteristics of cheese obtained from animal milk, characteristics that are particularly characteristic of cheese obtained from animal milk include those that are elongated by heating (hereinafter, this characteristic is also referred to as "extensibility". The characteristics are also responsible for casein contained in animal milk and are responsible for stimulating appetite of cheese.
To impart extensibility to the cheese alternative, the addition of starch is contemplated. The inventors tried to impart extensibility to cheese substitutes by adding starch, and as a result confirmed that: when starch is added in an amount of 0.6 parts by weight or more based on 1 part by weight of the vegetable protein, an excellent ductility improving effect can be obtained. However, the effect of imparting extensibility to cheese substitutes by the addition of starch alone is limited, and thus techniques capable of enhancing extensibility even further are desired.
Accordingly, an object of the present invention is to provide a technique for producing a cheese substitute comprising a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein, which can impart an improved extensibility to the cheese substitute.
Technical scheme for solving technical problems
The inventors found that: the malleability of the cheese substitute obtained by adding a protease to a material composition having a specific composition comprising a vegetable protein and 0.6 parts by weight or more of starch relative to 1 part by weight of the vegetable protein is improved. Further, it was found that: there are also cases where amylase is combined in use of protease, and when amylase is added to the material composition together with protease, the starch gelatinization ability of amylase acceptable for the material composition is limited to a predetermined condition (i.e., a condition satisfying a relationship that the starch gelatinization ability per 1g of starch is 8U or less for 10 ten thousand U protease activity per 1g of vegetable protein). Such limitations are not found in material compositions that do not have this particular composition (i.e., material compositions that comprise a vegetable protein and a composition of less than 0.6 parts by weight of starch relative to 1 part by weight of the vegetable protein), and thus material compositions having this particular composition are characteristic. The present invention has been completed by further repeated studies based on these findings.
That is, the present invention provides the following disclosed embodiments.
Item 1. A method of making a malleable cheese alternative, comprising: a step of treating a material composition containing a vegetable protein and starch in an amount of 0.6 parts by weight or more per 1 part by weight of the vegetable protein, with an enzyme preparation containing a protease, wherein the enzyme preparation is used such that the starch gelatinization ability of the amylase per 1g of the starch is 8U or less per 1g of the vegetable protein, with the protease activity of the protease being 10 ten thousand U.
The method according to item 2, wherein the enzyme preparation contains the amylase, and the starch paste refining ability per 1g of the starch is 0.5U or more per 1g of the protease activity of the vegetable protein of 10 ten thousand U.
The method according to item 1 or 2, wherein the protease is a protease derived from a bacterium.
The production method according to any one of items 1 to 3, wherein the protease is a protease derived from Bacillus and/or Geobacillus.
The method according to any one of items 1 to 4, wherein the protease is selected from the group consisting of proteases derived from Bacillus stearothermophilus (Bacillus stearothermophilus), bacillus licheniformis (Bacillus licheniformis) and Bacillus.
The method according to any one of items 1 to 5, wherein the enzyme preparation is used such that the protease activity per 1g of the vegetable protein is 10 to 500U.
The method according to any one of items 1 to 6, further comprising a step of treating with a peptidase.
The production method according to any one of items 1 to 7, wherein the vegetable protein is pea protein, fava bean protein, chickpea protein and/or lentil protein.
The production method according to any one of items 1 to 8, wherein the content of the vegetable protein in the material composition is 1% by weight or more and less than 15% by weight.
The production method according to any one of items 1 to 9, wherein the starch is tapioca starch.
The production method according to any one of items 1 to 10, wherein the starch content per 1 part by weight of the vegetable protein is 5 parts by weight or less.
A spread enhancer of a spread cheese alternative comprising an enzyme preparation comprising a protease and optionally an amylase, the spread cheese alternative comprising a vegetable protein and 0.6 parts by weight or more of starch relative to 1 part by weight of the vegetable protein, the spread enhancer being used in such a manner that the amylolytic ability of the amylase per 1g of the starch is 8U or less for a protease activity of the protease per 1g of the vegetable protein.
Item 13. The ductility enhancer of item 12, wherein the ductility enhancer further comprises a peptidase.
Effects of the invention
According to the present invention, there is provided a technique for producing a cheese substitute, which can impart improved extensibility to a cheese substitute comprising a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein.
Detailed Description
1. Process for producing malleable cheese substitute
The method for producing a malleable cheese alternative of the present invention is characterized by comprising a step of treating a material composition containing a protease and optionally an amylase with an enzyme preparation, wherein the material composition contains a vegetable protein and 0.6 parts by weight or more of starch per 1 part by weight of the vegetable protein (hereinafter, also referred to as "protease treatment step"), and the enzyme preparation is used such that the protease activity of the protease per 1g of the vegetable protein is 10 ten thousand U and the starch gelatinization ability of the amylase per 1g of the starch is 8U or less. The method for producing the malleable cheese alternative of the present invention will be described in detail below. According to the present invention, the extensibility of the cheese substitute obtained can be improved, or, in addition to the improvement of extensibility, a hot-melt property improving effect and/or a hydrophobic peptide reducing effect (hydrophobic peptide reducing effect means an effect of decomposing a hydrophobic peptide exhibiting a bitter taste and replacing it with a hydrophobic amino acid) can be further provided.
1-1 Material composition comprising vegetable protein and starch
The plant that is the origin of the plant protein is not particularly limited, and examples thereof include: beans such as peas, soybeans, fava beans, chickpeas, lentils, and the like; grains such as barley, wheat, oat, rice, buckwheat, barnyard grass, millet and the like; peach kernel, cashew, hazelnut, pecan, macadamia nut, pistachio, walnut, brazil nut, peanut, coconut and other nuts. As the plant protein derived from these plants, 1 species may be used alone, or 2 or more species different in use source may be used in combination.
Among them, from the viewpoint of further improving the ductility or the viewpoint of further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, proteins of beans are preferable, and proteins of peas, broad beans, chickpeas, lentils are more preferable.
The content of the vegetable protein in the material composition is not particularly limited, and examples thereof include 1 to 30 wt%, preferably 1 wt% or more and less than 15 wt%, more preferably 3 to 12 wt%, further preferably 4 to 11 wt%, further preferably 4 to 9 wt%, 4 to 8 wt%, 4 to 7 wt%, 4 to 6 wt%, 6 to 11 wt%, 7 to 11 wt%, 8 to 11 wt%, or 9 to 11 wt%.
The plant that is the origin of the starch is not particularly limited as long as it can impart extensibility to the cheese substitute, and examples thereof include cassava, potato, sweet potato, arrowroot, and the like. As the starch derived from these plants, 1 species may be used alone, or 2 or more species different in use source may be used in combination.
Among them, tapioca starch (tapioca starch) is preferable from the viewpoint of further improving the extensibility or the viewpoint of further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint.
The starch content of the plant protein is 0.6 parts by weight or more per 1 part by weight of the material composition. The method of the present invention is excellent in the effect of improving the extensibility, and therefore, in the case of using an enzyme preparation containing amylase, the extensibility can be effectively improved even under the adverse condition that the ratio of starch to vegetable protein is further susceptible to adverse effects caused by the starch gelatinization ability. From such a viewpoint, the starch content per 1 part by weight of the vegetable protein is preferably 0.7 part by weight or more, more preferably 0.8 part by weight or more, still more preferably 1 part by weight or more, still more preferably 1.5 parts by weight or more, still more preferably 2 parts by weight or more, and particularly preferably 2.5 parts by weight or more, based on 1 part by weight of the vegetable protein.
The upper limit of the content range of starch per 1 part by weight of vegetable protein in the material composition is not particularly limited, and from the viewpoint of properly blending a predetermined amount of vegetable protein, for example, 5 parts by weight or less is exemplified. Further, the method of the present invention has an excellent effect of improving the extensibility, and therefore, can effectively improve the extensibility even when the content ratio of starch to vegetable protein is relatively small. From such a viewpoint, the upper limit of the starch content range per 1 part by weight of the vegetable protein is preferably 3 parts by weight or less, more preferably 2 parts by weight or less, further preferably 1.2 parts by weight or less, and still more preferably 0.9 parts by weight or less. Further, from the viewpoint of being less susceptible to adverse effects due to the starch paste refining ability even when an enzyme preparation containing amylase is used, the upper limit of the starch content range per 1 part by weight of the vegetable protein is preferably 3 parts by weight or less, more preferably 2 parts by weight or less, still more preferably 1.2 parts by weight or less, and still more preferably 0.9 parts by weight or less.
The starch content in the material composition is not particularly limited as long as it can impart ductility, and may be, for example, 4% by weight or more. From the viewpoint of further improving the ductility, or from the viewpoint of further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect, the content of starch in the material composition may be preferably 5% by weight or more, more preferably 6% by weight or more, still more preferably 7% by weight or more, still more preferably 8% by weight or more, 9% by weight or more, 10% by weight or more, 11% by weight or more, 12% by weight or more, or 13% by weight or more.
The upper limit of the starch content range in the material composition is not particularly limited, and may be, for example, 20% by weight or less from the viewpoint of properly blending a predetermined amount of vegetable protein. In addition, the production method of the present invention has an excellent effect of improving the ductility, and therefore, even when the starch content is relatively small, the ductility can be effectively improved. From such a viewpoint, the upper limit of the content range of starch in the material composition is preferably 17% by weight or less, more preferably 15% by weight or less, further preferably 13% by weight or less, further preferably 11% by weight or less, further preferably 9% by weight or less.
The material composition may contain any material component used for cheese substitutes as a component other than vegetable protein and starch (hereinafter, also referred to as "other material component"). Examples of the other material components include vegetable oils and fats, thickening polysaccharides, water, and salt.
The vegetable fat is not particularly limited, and 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 oil, safflower oil, linseed oil, palm kernel oil, palm fruit (Palm fruil) oil, babassu oil (Babassu oil), shea butter, mango butter (mango butter), cocoa butter, wheat germ oil, rice bran oil, and the like. These vegetable oils and fats may be used alone or in combination of 1 or more than 2. From the viewpoint of further improving the ductility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, canola oil (rapeseed oil) and coconut oil are preferable.
When the material composition contains a vegetable oil or fat, the content of the vegetable oil or fat in the material composition is not particularly limited, and from the viewpoint of further improving the ductility or from the viewpoint of further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to the above, for example, 5 to 30% by weight, preferably 8 to 25% by weight, more preferably 10 to 20% by weight, still more preferably 10 to 17% by weight, 12 to 14% by weight, or 14 to 17% by weight may be exemplified. The content ratio of the vegetable protein to the vegetable oil is determined by the content of each component, and examples of the content of the vegetable oil per 1 part by weight of the vegetable protein include 0.3 to 5 parts by weight, preferably 0.5 to 4.5 parts by weight, more preferably 0.7 to 4 parts by weight, 0.7 to 3.5 parts by weight, still more preferably 0.9 to 3.5 parts by weight, still more preferably 1.1 to 3.3 parts by weight, 1.1 to 3.2 parts by weight, and 1.2 to 3 parts by weight.
The thickening polysaccharide is not particularly limited, and examples thereof include: locust bean gum, guar gum, carrageenan, xanthan gum, tragacanth gum, tamarind gum, pectin, acacia, curdlan (curdlan), tara gum, gellan gum, dawa gum (ghatti gum), CMC (carboxymethyl cellulose), sodium alginate, pullulan, etc., preferably carrageenan, etc. These thickening polysaccharides may be used alone or in combination of at least 2 kinds. From the viewpoint of further improving the ductility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, carrageenan is preferable.
When the material composition contains a thickening polysaccharide, the content of the thickening polysaccharide in the material composition is not particularly limited, and from the viewpoint of further improving the ductility or from the viewpoint of further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to the viewpoint, for example, 0.3 to 1.8% by weight, preferably 0.8 to 1.2% by weight is exemplified. The content ratio of the vegetable protein to the thickening polysaccharide is determined by the content of each component, and the content of the thickening polysaccharide per 1 part by weight of the vegetable protein is, for example, 0.03 to 0.3 parts by weight, preferably 0.08 to 0.12 parts by weight.
When the material composition contains water, the content of water is not particularly limited, and from the viewpoint of further improving ductility or from the viewpoint of further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to the viewpoint, for example, 50 to 72% by weight, preferably 55 to 70% by weight, and more preferably 62 to 68% by weight can be exemplified. The content ratio of the vegetable protein to water is determined by the content of each component, and examples of the content of water per 1 part by weight of the vegetable protein include 1 to 17 parts by weight, preferably 3 to 15 parts by weight, more preferably 6 to 13 parts by weight, 6 to 9 parts by weight, or 9 to 13 parts by weight.
When the material composition contains salt, the content of salt is not particularly limited, and from the viewpoint of further improving ductility or from the viewpoint of further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to the viewpoint, for example, 0.1 to 1% by weight, and more preferably 0.3 to 0.5% by weight is exemplified. The content ratio of the vegetable protein to the salt is determined by the content of each component, and examples of the content of the salt per 1 part by weight of the vegetable protein include 0.008 to 0.15 part by weight, preferably 0.01 to 0.12 part by weight, 0.02 to 0.1 part by weight, 0.02 to 0.09 part by weight, more preferably 0.03 to 0.09 part by weight, 0.03 to 0.06 part by weight, or 0.06 to 0.09 part by weight.
1-2 enzyme preparation
The enzyme preparation used for treating the above-mentioned material composition comprises at least a protease and may comprise an amylase. In the case where the enzyme preparation contains amylase, the amylase is not limited to amylase further added to the protease preparation, and amylase mixed in the protease preparation may be used together with protease in any other way.
In the present invention, protease means exopeptidase. The source of the protease is not particularly limited, and for example, a protease derived from a bacterium belonging to the genus Bacillus, geobacillus (Geobacillus) or the like; proteases derived from fungi of the genus Aspergillus, mucor, neurospora, penicillium, rhizomucor, rhizopus, sclerotinia; a protease derived from a yeast of the genus Saccharomyces; proteases derived from actinomycetes of the genus Streptomyces, and the like. These proteases may be used alone or in combination of 1 or more.
Among these proteases, from the viewpoint of further improving ductility or further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to this viewpoint, bacterial-derived proteases are preferable, proteases derived from Bacillus and/or Geobacillus are more preferable, proteases derived from Bacillus stearothermophilus (Bacillus stearothermophilus), bacillus licheniformis (Bacillus licheniformis) and these Geobacillus are more preferable, bacillus stearothermophilus and Geobacillus stearothermophilus are more preferable, and Geobacillus stearothermophilus is particularly preferable.
The enzyme preparation can be used such that the protease activity of the protease per 1g of the vegetable protein is, for example, 10 to 500U. From the viewpoint of further improving the extensibility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, the enzyme preparation can be used such that the protease activity of the protease is preferably 30 to 500U, more preferably 50 to 500U, and even more preferably 80 to 500U per 1g of the vegetable protein. The method of the present invention has an excellent ductility-improving effect, and therefore can effectively obtain a ductility-improving effect even with a relatively small amount of protease. From such a viewpoint, the enzyme preparation may be used such that the protease activity of the protease per 1g of the vegetable protein is, for example, 10 to 400U, 10 to 300U, 10 to 200U, 10 to 150U or 10 to 100U.
In the present invention, amylase refers to alpha-amylase. The source of amylase is not particularly limited, and examples thereof include: bacteria of the genus Bacillus (e.g., bacillus amyloliquefaciens (B. Amyloliquefaciens), bacillus subtilis (B. Subtilis), bacillus licheniformis (B. Lichenifermis), etc.), geobacillus (Geobacillus), etc.; fungi of Aspergillus (for example, aspergillus oryzae (A. Oryzae), aspergillus niger (A. Niger) and the like), mucor (Mucor) genus, neurospora (Neurospora) genus, penicillium (Penicillium) genus, rhizomucor (Rhizomucor) genus, rhizopus genus, sclerotinia (Sclerotinia) genus and the like; actinomycetes of the genus Streptomyces (Streptomyces), and the like. These amylases may be used alone or in combination of 1 or more.
The enzyme preparation is used in such a manner that the amylase per 1g of starch has a starch gelatinization ability of 8U or less per 1g of the protease activity of the protease of the vegetable protein of 10 ten thousand U. From the viewpoint of further improving the extensibility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, the starch paste refining ability per 1g of starch of 10 ten thousand U per 1g of the protease activity of the vegetable protein may be preferably 7U or less, more preferably 6.5U or less, further preferably 5.5U or less, further preferably 4.5U or less, further preferably 3.5U or less, or 2U or less.
The lower limit of the range of the starch gelatinization ability per 1g of starch, which is 10 ten thousand U per 1g of the protease activity of the vegetable protein, is 0U or more. For example, in the case where the enzyme preparation does not contain amylase, the starch gelatinization capacity per 1g of starch is 0U for a protease activity of 10 ten thousand U per 1g of vegetable protein. In the case where the enzyme preparation contains amylase, the starch paste refining ability per 1g of starch is more than 0U, preferably 0.5U or more, more preferably 1U or more, still more preferably 1.5U or more, 2U or more, or 3U or more, as 10 ten thousand U per 1g of protease activity of the vegetable protein.
The protease activity was measured by the furin method using casein as a substrate, specifically, the enzyme reaction was performed by a conventional method using casein as a substrate, and the enzyme activity of 1 unit (1U) was obtained by increasing the amount of the enzyme that caused the color-developing substance of the furin solution corresponding to 1. Mu.g of tyrosine in 1 minute. In addition, the starch gelatinization ability is an enzyme activity of reducing the iodine-based development of potato starch by 10% in 1 minute as 1 unit (1U).
In the present invention, from the viewpoint of further improving the ductility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect to the substrate in addition to the viewpoint, it is preferable that the substrate further comprises a step of treating the substrate with a peptidase (hereinafter, also referred to as "peptidase treating step") in addition to the protease treating step.
The peptidase treatment step may be performed simultaneously with the protease treatment step or after the protease treatment step. That is, the material composition containing the vegetable protein and the starch may be subjected to a treatment for allowing both the protease and the peptidase to act simultaneously, or the material composition containing the vegetable protein and the starch may be subjected to a treatment for allowing the protease to act further, and then subjected to a treatment for allowing the peptidase to act further.
In the present invention, peptidase refers to exopeptidase. The source of the peptidase is not particularly limited, and for example, a peptidase derived from a fungus such as a fungus belonging to the genus Yu Genmei (Rhizopus) or Aspergillus (Aspergillus) can be used; a peptidase derived from actinomycetes of the genus Streptomyces; the peptidase derived from bacteria of the genus Bacillus, geobacillus, lactobacillus, lactococcus, etc., more specifically, the peptidase derived from fungi of the genus Yu Genmei (Rhizopus), aspergillus, etc., and even more specifically, the peptidase derived from Rhizopus oryzae (Rhizopus oryzae), aspergillus oryzae (Aspergillus oryzae) can be used. These peptidases may be used alone in an amount of 1 or in combination.
Among these peptidases, from the viewpoint of further improving ductility or further imparting a hot-melt property improving effect and/or a hydrophobic peptide reducing effect in addition to this viewpoint, a peptidase derived from rhizopus is preferable, and a peptidase derived from rhizopus oryzae is more preferable.
The peptidase can be used in such a manner that the peptidase activity per 1g of the vegetable protein is, for example, 0.001 to 1U. From the viewpoint of further improving the ductility or further imparting the hot-melt property improving effect and/or the hydrophobic peptide reducing effect in addition to the viewpoint, the peptidase can be used such that the peptidase activity per 1g of the vegetable protein is, for example, 0.002 to 0.8U, preferably 0.0025 to 0.7U, more preferably 0.003 to 0.6U, still more preferably 0.0035 to 0.4U, still more preferably 0.0035 to 0.3U, still more preferably 0.004 to 0.25U, 0.004 to 0.02U, 0.004 to 0.01U, 0.004 to 0.008U, 0.004 to 0.006U, 0.01 to 0.25U, 0.02 to 0.25U, 0.03 to 0.25U, 0.04 to 0.25U, 0.05 to 0.25U, 0.1 to 0.25U, or 0.2 to 0.25U.
The peptidase activity was measured by a method based on the ninth edition of food additive, japanese (Japanese patent document: 9 th edition of food additive, public disclosure), using L-leucyl-glycyl-glycine as a substrate, and specifically, by performing an enzyme reaction using L-leucyl-glycyl-glycine as a substrate by a conventional method, and taking the enzyme amount which caused an increase in the ninhydrin chromogenic substance corresponding to 1. Mu. Mol of leucine within 1 minute as an enzyme activity of 1 unit (1U).
1-3 treatment conditions etc
The specific steps in the protease treatment step and the peptidase treatment step, which are optionally performed, are not particularly limited as long as the enzyme treatment object is brought into contact with the enzyme. For example, in the protease treatment step, the material composition may be prepared and then the protease (or protease and amylase) may be added, or the constituent materials of the material composition and the protease (or protease and amylase) may be mixed at the same time. In addition, in the combination of the protease treatment step and the peptidase treatment step, a material composition may be prepared, and then the protease (or protease and amylase) and the peptidase may be added simultaneously or sequentially, or the constituent materials of the material composition, the protease (or protease and amylase) and the peptidase may be mixed simultaneously.
The temperature in the protease treatment step and the peptidase treatment step to be performed as needed is not particularly limited, and may be appropriately determined by those skilled in the art depending on the optimum temperature of each enzyme to be used, and examples thereof include 45 to 90 ℃. In the present invention, the treatment temperature may be changed stepwise. For example, a temperature of 45 ℃ or higher and less than 70 ℃, preferably 45 to 60 ℃, more preferably 45 to 55 ℃ as heating condition 1, and a temperature of 70 to 90 ℃, preferably 80 to 90 ℃ as heating condition 2 may be combined. Preferably, these treatment steps can be performed under the heating condition 2 after the treatment under the heating condition 1 is performed.
The time taken for these treatment steps is not particularly limited and may be appropriately determined according to the ratio of the enzyme treatment target to be charged, and examples thereof include 10 minutes or more, preferably 15 minutes or more. The upper limit of the reaction time for the enzyme treatment is not particularly limited, and examples thereof include 6 hours or less, 3 hours or less, 1 hour or less, or 30 minutes or less. In these treatment steps, it is preferable that the treatment under the heating condition 1 is performed for 10 to 30 minutes, and then the treatment under the heating condition 2 is performed for 5 to 10 minutes.
After the necessary treatment process is completed, the material composition after the treatment can be filled into a container and cooled as necessary. Thus, a malleable cheese alternative is obtained.
2. Ductility improving agent for cheese substitute
As described above, in the production of a malleable cheese alternative comprising a vegetable protein and starch in an amount of 0.6 parts by weight or more per 1 part by weight of the vegetable protein, the enzyme preparation containing a protease and possibly an amylase can improve the malleability if it is used so that the starch paste ability per 1g of starch is 8U or less per 1g of protease activity of 10 ten thousand U per 1g of vegetable protein. Accordingly, the present invention also provides a extensibility enhancer of a extensibility cheese alternative comprising an enzyme preparation containing a protease and possibly an amylase, the extensibility cheese alternative comprising a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein, for use in such a manner that the protease activity of the protease per 1g of the vegetable protein is 10 ten thousand U, and the starch gelatinization capacity of the amylase per 1g of the starch is 8U or less. From the viewpoint of further improving the extensibility, the extensibility enhancer of the alternative to extensible cheese preferably further comprises a peptidase.
Among the above-mentioned extensibility improving agents, the types and amounts of the components used are as described in the column of "1. Method for producing a extensibility cheese alternative".
Examples
The present invention will be specifically described with reference to the following examples, but the present invention is not to be construed as being limited to the following examples.
[ use of enzyme ]
Commercially available enzymes shown in the following tables were used.
TABLE 1
[ method for measuring enzyme Activity ]
(1) Protease Activity assay
After heating 5mL of a 0.6% (w/v) casein solution (0.05 mol/L sodium hydrogen phosphate, pH 8.0) at 37℃for 10 minutes, 1mL of a sample solution containing a protease was added thereto, and immediately mixed with shaking. After the solution was left at 37℃for 10 minutes, 5mL of a trichloroacetic acid solution containing 1.8% trichloroacetic acid, 1.8% sodium acetate and 0.33mol/L acetic acid was added thereto, and the mixture was mixed with shaking, and the mixture was left at 37℃again for 30 minutes, and then filtered. The initial 3mL of the filtrate was removed, the next 2mL of the filtrate was weighed, and 5mL of 0.55mol/L sodium carbonate solution and 1mL of Fu Lin Shiye (1.fwdarw.3) were added thereto, followed by mixing with shaking, and the mixture was left at 37℃for 30 minutes. The absorbance AT AT 660nm was measured using water as a control for the liquid (enzyme reaction liquid).
Further, 1mL of a sample solution containing protease was weighed, 5mL of a trichloroacetic acid sample solution containing 1.8% trichloroacetic acid, 1.8% sodium acetate and 0.33mol/L acetic acid was added and mixed with shaking, 5mL of a 0.6% (w/v) casein solution was added and mixed with shaking immediately, and the mixture was left to stand at 37℃for 30 minutes, except that the absorbance AB was measured for a liquid (blank) obtained in the same manner as the above enzyme reaction solution.
The amount of enzyme that caused an increase in the amount of the chromogenic substance of the forskolin test solution corresponding to 1. Mu.g of tyrosine in 1 minute was taken as 1 unit (1U).
1mL/mL of a tyrosine standard stock solution (0.2 mol/L hydrochloric acid) 1mL,2mL,3mL and 4mL were weighed, and 0.2mol/L hydrochloric acid test solution was added to prepare 100mL. 2mL of each solution was weighed, 5mL of a sodium carbonate solution (0.55 mol/L) and 1mL of Fu Lin Shiye (1.fwdarw.3) were added thereto, and immediately mixed by shaking, and the mixture was left at 37℃for 30 minutes. For these liquids, 2mL of a 0.2mol/L hydrochloric acid sample was weighed, and absorbance A1, A2, A3 and A4 at 660nm was measured using a liquid obtained in the same manner as described above as a control. The absorbance A1, A2, A3 and A4 was measured on the vertical axis, the tyrosine amount (. Mu.g) in each liquid 2mL was measured on the horizontal axis, and a standard curve was prepared to determine the tyrosine amount (. Mu.g) with respect to the absorbance difference 1.
[ mathematics 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: tyrosine amount (. Mu.g) at 1 absorbance difference determined from tyrosine standard curve
11/2: conversion coefficient relative to total liquid amount after reaction is stopped
1/10: conversion coefficient relative to reaction time per 1 minute
M: sample amount (g or mL) in 1mL of sample solution
(2) Starch gelatinization ability assay
After 10mL of a 1% potato starch substrate solution (0.1 mol/L acetic acid (pH 5.0)) was heated at 37℃for 10 minutes, 1mL of a sample solution containing amylase was added thereto, and immediately mixed with shaking. After the liquid was left at 37℃for 10 minutes, 1mL of the liquid was added to 10mL of a 0.1mol/L hydrochloric acid solution, and immediately mixed with shaking. Next, 0.5mL of the solution was weighed, 10mL of an iodine solution (day office) of 0.0002mol/L was added thereto, and after mixing by shaking, the Absorbance (AT) AT 660nm was measured using water as a control. In addition, 1mL of water was added in place of the sample solution, and Absorbance (AB) was measured in the same manner. The amount of enzyme that reduced the iodine-based development of potato starch by 10% within 1 minute was taken as 1 unit (1U).
[ math figure 2]
Starch gelatinization ability (U/g) = (AB-AT)/AB×1/W
AT: absorbance of the reaction solution
AB: absorbance of blank
W: sample amount (g) of sample in 1mL of sample solution
(3) Peptidase Activity assay
An appropriate amount of enzyme was weighed, and water, potassium phosphate buffer (0.005 mol/L) at pH7.0 or potassium phosphate buffer (0.005 mol/L, pH7.0, containing zinc sulfate) was added thereto, dissolved or uniformly dispersed to prepare 50mL of a sample solution, or the sample solution was diluted 10-fold, 100-fold or 1000-fold with water or the same buffer.
30mg of L-leucyl-glycyl-glycine was weighed, and 50mL of potassium phosphate buffer (0.05 mol/L) was added to dissolve the L-leucyl-glycyl-glycine. The solution was diluted 10-fold with potassium phosphate buffer (0.05 mol/L) at pH7.0 to prepare a substrate solution. The substrate solution is prepared at the time of use.
1mL of the substrate solution was weighed into a stoppered test tube, heated at 37℃for 5 minutes, then 0.1mL of the sample solution was added and mixed, heated at 37℃for 60 minutes, then heated in a boiling water bath for 5 minutes, and cooled to room temperature. To this solution were added 2mL of ninhydrin 2-methoxyethanol citric acid buffer and 0.1mL of tin (II) chloride buffer, capped and heated in a boiling water bath for 20 minutes. After cooling, 10mL of 1-propanol (1.fwdarw.2) was added thereto and mixed with shaking to prepare a detection solution. In addition, 0.1mL of the sample solution was weighed into a stoppered test tube and heated in a boiling water bath for 5 minutes. After cooling, 1mL of the substrate solution was added and mixed, and after heating at 37℃for 5 minutes, it was cooled to room temperature. To this solution were added 2mL of ninhydrin 2-methoxyethanol citric acid buffer and 0.1mL of tin (II) chloride buffer, capped and heated in a boiling water bath for 20 minutes. After cooling, 10mL of 1-propanol (1.fwdarw.2) was added thereto and mixed with shaking to prepare a comparative liquid. After the detection solution and the comparison solution are prepared, when the absorbance at 570nm is measured within 5-30 minutes, the absorbance of the detection solution is larger than that of the comparison solution. When turbidity is present in the detection liquid and the comparison liquid for measuring absorbance, centrifugation is performed to measure the supernatant. The amount of enzyme that caused an increase in ninhydrin chromogenic material equivalent to 1. Mu. Mol leucine in 1 minute was taken as 1 unit (1U).
[ math 3]
Peptidase Activity (U/g, U/mL) = (AT-AB) ×F× (1/0.1) × (1/60) ×nAT: absorbance of enzyme reaction solution
AB: absorbance of blank
F: leucine amount (. Mu. nol) at an absorbance difference of 1 as determined by the standard curve
0.1: enzyme liquid amount (mL)
60: reaction time (minutes)
N: dilution factor
[ use of materials ]
The materials shown in the following table were used.
TABLE 2
Test example 1
(1) Manufacture of malleable cheese substitute
Pure water (RO water) was placed in a thermo mix mixer, and pea protein material, tapioca starch, canola oil, coconut oil, salt, and enzyme preparations shown in Table 3 were added in amounts shown in Table 3 while stirring at 50℃and speed 3. After stirring at 50℃for 15 minutes at a speed of 3, the temperature was raised to 85℃and stirring at a speed of 3 was carried out for 7 minutes, 100g of each 1 aluminum container (bottom inner diameter: 5 cm) was filled with 3 containers, and the containers were covered with a cap and cooled to 4℃for preservation. Thus, cheese substitutes (3 in each example/comparative example) were obtained.
(2) Ductility evaluation
A cheese substitute in a state of being filled in an aluminum container was used as a sample, and heated for 30 minutes using a steam oven set to 110 ℃ (to exclude the influence of evaporation of water during heating). Then, the sample was taken out of the steam oven, and the internal temperature of the sample was confirmed to be 70℃and stirred with a fork. The fork was confirmed to be covered with the sample, the front end of the fork was lifted up by 5 cm/sec so as to stir the sample with the fork, and the distance (tensile length (mm)) between the lifting start point of the front end of the fork and the tensile breaking point of the sample was measured. The tensile length was derived as an average value obtained by similarly testing 3 samples prepared in each example and comparative example. Further, the percentage value of the tensile length in each example was derived as the ductility improvement evaluation index when the tensile length of the comparative example in which the enzyme preparation was not used was 100%. If the ductility improvement evaluation index exceeds 100%, the ductility is evaluated as being imparted with an improved ductility. Further, the larger the ductility improvement evaluation index is, the higher the ductility improvement effect is evaluated. The results are shown in Table 3.
TABLE 3
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from table 3, the cheese substitutes (examples 1 and 2) produced with the protease have higher ductility than the cheese substitutes (comparative example 1) produced without the protease. Among them, in the cheese alternative (example 1) produced using the protease (Thermoase GL 30) derived from geobacillus stearothermophilus (Geobacillus stearothermophilus), a further excellent ductility-improving effect was confirmed.
Test example 2
Cheese substitutes were prepared and evaluated for extensibility in the same manner as in test example 1 except that pure water (RO water), pea protein material, tapioca starch, canola oil, coconut oil, salt, and enzyme preparations shown in tables 4 to 6 were added in the amounts shown in tables 4 to 6. The results are shown in tables 4 to 6. In table 4, the results of comparative example 1 and example 1 of test example 1 are recalled.
TABLE 4
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
TABLE 5
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
TABLE 6
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from tables 4 to 6, the cheese substitutes produced with protease (examples 1 and 6, reference example 1) had higher ductility than the cheese substitutes produced without protease (comparative examples 1, 4 and 6).
In addition, in the case where the amount of starch blended is 0.6 parts by weight or more based on 1 part by weight of vegetable protein in the cheese substitute (examples 3 to 5, comparative examples 2 and 3, examples 7 to 9, comparative example 5, and reference examples 2 to 5) produced by adding amylase to the enzyme preparation obtained by using protease (examples 3 to 5, comparative examples 2 and 3, examples 7 to 9, and comparative example 5), the extensibility of the enzyme preparation is improved only when the protease activity per 1g of vegetable protein (the [ A ] value in the table) is 10 ten thousand U and the starch gelatinization ability per 1g of starch (the [ B ] value in the table) is 8U or less. On the other hand, when the amount of starch blended is less than 0.6 parts by weight based on 1 part by weight of the vegetable protein (reference examples 2 to 5), no such limitation is observed in examples 3 to 5 and 7 to 9 regarding the [ B ] value of 10 ten thousand U relative to the [ A ] value, and the ductility is improved regardless of the [ B ] value of 10 ten thousand U relative to the [ A ] value.
Only when the material composition has a specific composition in which the amount of starch to be blended is 0.6 parts by weight or more based on 1 part by weight of the vegetable protein (examples 3 to 5, comparative examples 2 and 3, examples 7 to 9, comparative example 5), the mechanism of the specific limitation is not specified with respect to the value of [ B ] of 10 ten thousand U relative to the value of [ a ], but the following will be discussed. In general, proteins have a property of absorbing moisture, and in a material composition having no specific composition (such as a material composition having a starch content of less than 0.6 parts by weight based on 1 part by weight of vegetable protein, hereinafter referred to as "material composition (1)") the amount of vegetable protein relative to the amount of starch is large, and thus the amount of protein capable of absorbing water is large relative to the amount of starch, and in a material composition having a specific composition (examples 3 to 5, comparative examples 2 and 3, and examples 7 to 9, and comparative example 5, the amount of starch content of material composition used in relation to 1 part by weight of vegetable protein is 0.6 parts by weight or more, hereinafter referred to as "material composition (2)") the amount of vegetable protein relative to the amount of starch is small, and thus the amount of protein capable of absorbing water is small relative to the amount of starch. In the case of the material composition (1) having a large relative amount of protein, even if the starch is decomposed by the excessive starch gelatinization ability (the starch gelatinization ability exceeding 8U in [ B ] value of 10U in [ A ] value) and the viscosity is lowered, the protein can sufficiently absorb water to avoid a significant lowering of the viscosity, and the influence of the starch gelatinization ability is masked, so that the ductility-improving effect is not completely lost (reference examples 3 to 5). On the other hand, in the case of the material composition (2) having a relatively small amount of protein, if the starch is decomposed by the excessive starch gelatinization ability (the starch gelatinization ability exceeding 8U in [ B ] value of 10 ten thousand U in [ a ]) and the viscosity is lowered, the moisture cannot be sufficiently absorbed, and therefore, the influence of the starch gelatinization ability is exhibited, and the ductility improvement effect is completely lost (comparative examples 2, 3, and 5).
Test example 3
Cheese substitutes were produced in the same manner as in test example 1, except that pure water (RO water), pea protein material, tapioca starch, canola oil, coconut oil, nutritional yeast, kappa-carrageenan, salt, and enzyme preparations shown in table 7 were added in the amounts shown in table 7.
(1) Ductility evaluation
Ductility was evaluated in the same manner as in test example 1. The relative value of the tensile length in each example was derived as the ductility improvement assessment index when the tensile length of the comparative example in which the enzyme preparation was not used was 1. If the ductility improvement evaluation index exceeds 1, the ductility is evaluated as being imparted with an improved ductility. Further, the larger the ductility improvement evaluation index is, the higher the ductility improvement effect is evaluated. The results are shown in Table 7.
(2) Evaluation of Hot melt Property
The prepared cheese substitute was used for hot melt evaluation. The commercial frozen pizza dough (7 inches) was cut and coated with a commercial pizza sauce. The prepared cheese substitute was placed thereon, and heated and cooked in a steam oven at 110℃for 30 minutes. The hot melt properties of the cheese alternative after heat cooking were evaluated according to the following criteria. The results are shown in Table 7.
-: the melting of the cheese pieces could not be confirmed.
+: the shape of the cheese crumb remained clearly.
++: the shape of the cheese crumb was slightly residual.
+++: the shape of the cheese crumb was free of residue.
(3) Evaluation of bitter Peptides decrease (hydrophobic Peptidolysis, i.e., hydrophobic amino acid increase)
Using the cheese substitutes prepared, the increase in hydrophobic amino acids was investigated for the purpose of bitter peptide reduction evaluation. To 1g of cheese substitute was added 1ml of water and homogenized using a vortex mixer. The supernatant was recovered by centrifugation at 13000rpm for 5 minutes. The recovered supernatant was filtered using a syringe filter as a sample for HPLC analysis. Analysis by ninhydrin reaction using a post-column reactor was performed using HPLC, and the total amount of Gly, ala, val, met, ile, leu, phe, pro (derived as an amount converted to an amount (mg) of cheese substitute per 1 g) was measured as the amount of hydrophobic amino acid. Further, a relative value at which the amount of the hydrophobic amino acid in the corresponding comparative example (i.e., example prepared under the same conditions except that the treatment with the enzyme preparation was not performed) was 1 was derived as the increase rate of the amount of the hydrophobic amino acid. The higher the increase rate of the amount of hydrophobic amino acids, the more hydrophobic peptides exhibiting bitter taste are decomposed into amino acids, i.e., the bitter taste is further reduced. The results are shown in Table 7.
Analytical column: TSKgel Aminopak
Mobile phase: HITACHI AMINO ACID ANALYSIS Buffer pH1-4
TABLE 7
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from table 7, the cheese alternative (examples 10 and 11) produced with the protease was improved in the ductility as compared with the cheese alternative (comparative example 7) produced without using the protease, and the protease was used in combination with the peptidase to confirm the further excellent ductility improvement effect (example 11). Regarding the hot-melt property, in the cheese alternative (examples 10, 11) produced using protease, the hot-melt property was improved as compared with the cheese alternative (comparative example 7) produced without using protease, wherein the protease was used in combination with peptidase to exhibit further excellent hot-melt property (example 11). Regarding the amount of hydrophobic amino acid, in the cheese substitute produced with protease (examples 10, 11), the amount of hydrophobic amino acid was increased as compared with the amount of hydrophobic amino acid in the cheese substitute produced without protease (comparative example 7), and further excellent effect of increasing the amount of hydrophobic amino acid was confirmed by using peptidase in combination with protease (example 11). In fact, sensory tests were conducted on comparative example 7, example 10 and example 11, and as a result, it was confirmed that bitter taste was perceived in the cheese alternative of comparative example 7, while on the other hand, bitter taste was suppressed in the cheese alternative of example 10, and good taste with no bitter taste was obtained in the cheese alternative of example 11.
Test example 4
Cheese substitutes were produced in the same manner as in test example 1, except that pure water (RO water), a broad bean protein material, tapioca starch, coconut oil, kappa-carrageenan, salt, and an enzyme preparation shown in table 8 were added in the amounts shown in table 8.
(1) Ductility evaluation
Ductility was evaluated in the same manner as in test example 1. The relative value of the tensile length in each example was derived as the ductility improvement assessment index when the tensile length of the comparative example in which the enzyme preparation was not used was 1. If the ductility improvement evaluation index exceeds 1, the ductility is evaluated as being imparted with an improved ductility. Further, the larger the ductility improvement evaluation index is, the higher the ductility improvement effect is evaluated. The results are shown in Table 8.
(2) Evaluation of bitter Peptides decrease (hydrophobic Peptidolysis, i.e., hydrophobic amino acid increase)
In the same manner as in test example 3, the increase in hydrophobic amino acid was studied for the purpose of evaluation of reduction in bitter peptide. The results are shown in Table 8.
TABLE 8
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from table 8, the cheese substitute produced with protease (examples 12 and 13) had an improved extensibility compared to the cheese substitute produced without protease (comparative example 8), and the protease was used in combination with peptidase to confirm a further excellent extensibility-improving effect (example 13). Regarding the amount of hydrophobic amino acid, the amount of hydrophobic amino acid of the cheese substitute (examples 12, 13) produced with the protease was increased as compared with the amount of hydrophobic amino acid of the cheese substitute (comparative example 8) produced without the protease, and further excellent effect of increasing the amount of hydrophobic amino acid (example 13) was confirmed by the protease in combination with the peptidase, thus suggesting that the hydrophobic peptide which is the cause of bitterness was decreased.
Test example 5
Cheese substitutes were produced in the same manner as in test example 1 except that pure water (RO water), chickpea protein material, tapioca starch, coconut oil, kappa-carrageenan, salt, and enzyme preparations shown in Table 9 were added in the amounts shown in Table 9.
(1) Ductility evaluation
Ductility was evaluated in the same manner as in test example 1. The relative value of the tensile length in each example was derived as the ductility improvement assessment index when the tensile length of the comparative example in which the enzyme preparation was not used was 1. If the ductility improvement evaluation index exceeds 1, the ductility is evaluated as being imparted with an improved ductility. Further, the larger the ductility improvement evaluation index is, the higher the ductility improvement effect is evaluated. The results are shown in Table 9.
(2) Evaluation of bitter Peptides decrease (hydrophobic Peptidolysis, i.e., hydrophobic amino acid increase)
In the same manner as in test example 3, the increase in hydrophobic amino acid was studied for the purpose of evaluation of reduction in bitter peptide. The results are shown in Table 9.
TABLE 9
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from table 9, the cheese substitute produced with protease (examples 14 and 15) had an improved extensibility compared to the cheese substitute produced without protease (comparative example 9), and the protease was used in combination with peptidase to confirm a further excellent extensibility-improving effect (example 15). Regarding the amount of hydrophobic amino acid, in the cheese substitute (examples 14, 15) produced with protease, the amount of hydrophobic amino acid was increased as compared with the amount of hydrophobic amino acid in the cheese substitute (comparative example 9) produced without protease, and further excellent effect of increasing the amount of hydrophobic amino acid (example 15) was confirmed by the protease in combination with peptidase, thus suggesting that hydrophobic peptide, which is a cause of bitterness, was decreased.
Test example 6
Cheese substitutes were produced in the same manner as in test example 1 except that pure water (RO water), lentil protein material, tapioca starch, coconut oil, kappa-carrageenan, salt, and the enzyme preparation shown in table 10 were added in the amounts shown in table 10.
(1) Ductility evaluation
Ductility was evaluated in the same manner as in test example 1. The relative value of the tensile length in each example was derived as the ductility improvement assessment index when the tensile length of the comparative example in which the enzyme preparation was not used was 1. If the ductility improvement evaluation index exceeds 1, the ductility is evaluated as being imparted with an improved ductility. Further, the larger the ductility improvement evaluation index is, the higher the ductility improvement effect is evaluated. The results are shown in Table 10.
(2) Evaluation of Hot melt Property
The hot-melt property was evaluated in the same manner as in test example 3. The results are shown in Table 10.
(3) Evaluation of bitter Peptides decrease (hydrophobic Peptidolysis, i.e., hydrophobic amino acid increase)
In the same manner as in test example 3, the increase in hydrophobic amino acid was studied for the purpose of evaluation of reduction in bitter peptide. The results are shown in Table 10.
TABLE 10
In the table, the unit of the unbracked value among the values showing the amounts of the components is weight%.
As is clear from table 10, the cheese substitute produced with protease (examples 16 and 17) had an improved ductility compared with the cheese substitute produced without protease (comparative example 10), and the protease was used in combination with peptidase to confirm a further excellent ductility improving effect (example 17). Regarding the hot-melt property, the cheese alternative produced using protease (example 16) and the cheese alternative produced using protease in combination with peptidase (example 17) exhibited excellent hot-melt property as compared with the cheese alternative produced without protease (comparative example 10). Regarding the amount of hydrophobic amino acid, in the cheese substitute produced with protease (examples 16, 17), the amount of hydrophobic amino acid was increased as compared with the amount of hydrophobic amino acid in the cheese substitute produced without protease (comparative example 10), and further excellent effect of increasing the amount of hydrophobic amino acid (example 17) was confirmed by using peptidase in combination with protease, thus suggesting that hydrophobic peptide, which is a cause of bitterness, was decreased.

Claims (13)

1. A method of making a malleable cheese alternative, comprising:
a step of treating a material composition with an enzyme preparation, wherein the enzyme preparation contains a protease and contains or does not contain an amylase, and the material composition contains a vegetable protein and starch in an amount of 0.6 parts by weight or more relative to 1 part by weight of the vegetable protein;
the enzyme preparation is used in such a manner that the starch gelatinization ability of the amylase per 1g of the starch is 8U or less per 1 ten thousand U of protease activity of the protease per 1g of the vegetable protein.
2. The method according to claim 1, wherein the enzyme preparation comprises the amylase,
the starch paste refining ability per 1g of the starch is 0.5U or more per 1g of the protease activity of the vegetable protein of 10 ten thousand U.
3. The production method according to claim 1 or 2, wherein the protease is a protease derived from bacteria.
4. The method according to any one of claims 1 to 3, wherein the protease is a protease derived from Bacillus and/or Geobacillus.
5. The method according to any one of claims 1 to 4, wherein the protease is selected from the group consisting of proteases derived from Bacillus stearothermophilus (Bacillus stearothermophilus), bacillus licheniformis (Bacillus licheniformis) and Bacillus.
6. The method according to any one of claims 1 to 5, wherein the enzyme preparation is used such that the protease activity per 1g of the vegetable protein is 10 to 500U.
7. The manufacturing method according to any one of claims 1 to 6, wherein the manufacturing method further comprises:
and a step of treating with a peptidase.
8. The method according to any one of claims 1 to 7, wherein the vegetable protein is pea protein, broad bean protein, chickpea protein and/or lentil protein.
9. The production method according to any one of claims 1 to 8, wherein the content of the plant protein in the material composition is 1% by weight or more and less than 15% by weight.
10. The manufacturing method according to any one of claims 1 to 9, wherein the starch is tapioca starch.
11. The production method according to any one of claims 1 to 10, wherein the starch content per 1 part by weight of the vegetable protein is 5 parts by weight or less.
12. A extensibility improving agent for a extensibility cheese alternative, characterized by comprising an enzyme preparation containing a protease and optionally an amylase, said extensibility cheese alternative comprising a vegetable protein and 0.6 parts by weight or more of starch relative to 1 part by weight of said vegetable protein,
The extensibility-improving agent is used in such a manner that the starch-gelatinization ability of the amylase per 1g of the starch is 8U or less per 1 ten thousand U of protease activity of the protease per 1g of the vegetable protein.
13. The ductility enhancer of claim 12, wherein the ductility enhancer further comprises a peptidase.
CN202280017102.7A 2021-02-26 2022-02-25 Process for producing malleable cheese substitute Pending CN116940240A (en)

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JP2021-030292 2021-02-26
JP2021-197380 2021-12-03
JP2021197380 2021-12-03
PCT/JP2022/008083 WO2022181810A1 (en) 2021-02-26 2022-02-25 Method for producing stretching cheese substitute

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