CN116964214A - Process for producing protein decomposition product and enzyme preparation - Google Patents
Process for producing protein decomposition product and enzyme preparation Download PDFInfo
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- CN116964214A CN116964214A CN202280020198.2A CN202280020198A CN116964214A CN 116964214 A CN116964214 A CN 116964214A CN 202280020198 A CN202280020198 A CN 202280020198A CN 116964214 A CN116964214 A CN 116964214A
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- aspergillus
- glutamyl
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Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The present invention addresses the problem of providing a practical method for producing cysteine from a protein, which is also suitable for use in the food field (food use). According to the present invention, there is provided a method for producing a cysteine-containing protein degradation product, comprising the steps of: allowing gamma-glutamyl peptide hydrolase, a protease derived from a filamentous fungus, and a bacterial protease to act on the protein material.
Description
Technical Field
The present invention relates to a method for producing cysteine from a protein, an enzyme preparation for producing a cysteine-containing protein degradation product, and use thereof.
Background
Proteins in foods are very important as nutrients, and animal proteins such as livestock meat, fish and shellfish are mainly favored in terms of preference. In recent years, there has been an increasing demand for vegetable proteins as an alternative to animal proteins due to an improvement in environmental protection and health awareness, but there have been many problems in terms of preference, and various studies have been made with a view to improving physical properties and taste. For example, patent document 1 discloses a method for producing a soybean protein using a glutamine transaminase and a protease, wherein the protease is used to reduce the viscosity that increases due to the glutamine transaminase. On the other hand, amino acids and peptides are important factors not only as nutrients but also for the taste and flavor of foods. For example, glutamic acid, aspartic acid exhibits a delicious taste, sour taste, glycine, alanine, threonine, etc., and tryptophan, isoleucine, valine, etc., exhibit a bitter taste. Therefore, studies on the production of amino acids and peptides from proteins are underway. Patent document 2 discloses the following method: two or more enzymes having only endoprotease activity are allowed to act on soybean protein to produce a low molecular peptide. In addition, in order to impart taste, a method of producing an amino acid as a seasoning has been studied. For example, patent document 3 discloses the following method: an amino acid seasoning having a high glutamic acid content is obtained by hydrolyzing a protein material with a thermostable protease and a thermostable glutaminase.
However, cysteine is known to impart a meat flavor by forming maillard reactants. Cysteine is mainly extracted from animal-derived raw materials (hair, feathers) and is not preferably added to foods. Patent document 4 discloses a method of producing cysteine by allowing an acid protease and a glutaminase to act on glutathione, but there are limited cases where glutathione is used because the content varies depending on foods.
Patent document 5 discloses the following: free aspartic acid and free glutamic acid are increased by treating soy protein with a glutamate specific endo-protease. Further, patent document 6 discloses the following: when soybean protein is treated with a subtilisin (ALCALASE) derived from Bacillus licheniformis (Bacillus licheniformis) or a serine protease (SP 1) derived from Nocardia green (Nocardiopsis prasina), the SP1 hydrolysate has less bitter taste than the ALCALASE hydrolysate.
Prior art literature
Patent literature
Patent document 1: japanese patent laid-open No. 2006-141231
Patent document 2: japanese patent laid-open No. 5-252979
Patent document 3: japanese patent laid-open No. 48-82068
Patent document 4: WO2021/002195
Patent document 5: japanese patent publication No. 2008-526261
Patent document 6: japanese patent application publication No. 2011-530574
Disclosure of Invention
The present invention aims to provide a practical method capable of improving the intense taste or flavor of foods and the like.
Under the above-mentioned problems, the present inventors have conducted studies to improve the intense taste or flavor of foods by using enzymes. As a result, it has been found that foods having enhanced flavor or umami taste can be produced by using a combination of a glutaminase, which is one of γ -glutamyl peptide hydrolase, with a filamentous protease or a bacterial protease. Based on this finding, the present invention has been completed by further repeated studies. That is, the present invention provides the following embodiments.
[1] A method for producing a protein degradation product, comprising the steps of: allowing gamma-glutamyl peptide hydrolase, a protease derived from a filamentous fungus, and a bacterial protease to act on the protein material.
[2] The method according to [1], wherein the gamma-glutamyl peptide hydrolase is glutaminase, gamma-glutamyl transferase or gamma-glutamyl cyclase.
[3] The method according to [1] or [2], wherein the gamma-glutamylhydrolase is a glutaminase derived from a microorganism belonging to the genus Bacillus.
[4] The method according to any one of [1] to [3], wherein the gamma-glutamylpeptide hydrolase is a Bacillus amyloliquefaciens-derived glutaminase.
[5] The method according to any one of [1] to [4], wherein the filamentous protease is an acid protease derived from a microorganism belonging to the genus Aspergillus or a neutral protease derived from a microorganism belonging to the genus Aspergillus.
[6] The method according to any one of [1] to [5], wherein the filamentous fungus protease is an Aspergillus oryzae-derived acidic protease, an Aspergillus oryzae-derived neutral protease, or an Aspergillus melleus-derived neutral protease.
[7] The method according to any one of [1] to [6], wherein the bacterial protease is a protease derived from a microorganism belonging to the genus Bacillus or Geobacillus.
[8] The method according to any one of [1] to [7], wherein the bacterial protease is a protease derived from Geobacillus stearothermophilus (Geobacillus stearothermophilus).
[9] The method according to any one of [1] to [8], wherein the protein material is an animal protein material, a plant protein material or a microbial protein material.
[10] The method according to any one of [1] to [9], wherein the protein material is a vegetable protein material.
[11] The method according to any one of [1] to [9], wherein the protein material is a pea, soybean, broad bean, chickpea, barley, wheat, oat, rice, buckwheat, barnyard grass, millet, hemp, algae, almond, cashew, hazelnut, pecan, hawaii, pistachio, walnut, brazil nut, peanut, coconut-derived protein material.
[12] A food comprising a protein degradation product produced by the method of any one of [1] to [11 ].
[13] An enzyme preparation for producing protein decomposition product comprises gamma-glutamyl peptide hydrolase, protease derived from filamentous fungus and bacterial protease.
[14] The enzyme agent according to [13], wherein the gamma-glutamyl peptide hydrolase is glutaminase, gamma-glutamyl transferase or gamma-glutamyl cyclase.
[15] The enzyme preparation according to [13] or [14], wherein the gamma-glutamylhydrolase is a glutaminase derived from a microorganism belonging to the genus Bacillus.
[16] The enzyme preparation according to any one of [13] to [15], wherein the gamma-glutamylhydrolase is a Bacillus amyloliquefaciens-derived glutaminase.
[17] The enzyme preparation according to any one of [13] to [16], wherein the filamentous fungus protease is an acid protease derived from a microorganism belonging to the genus Aspergillus or a neutral protease derived from a microorganism belonging to the genus Aspergillus.
[18] The enzyme preparation according to any one of [13] to [17], wherein the filamentous fungus protease is an Aspergillus oryzae-derived acidic protease, an Aspergillus oryzae-derived neutral protease, or an Aspergillus melleus-derived neutral protease.
[19] The enzyme preparation according to any one of [13] to [18], wherein the bacterial protease is a protease derived from a microorganism belonging to the genus Bacillus or Geobacillus.
[20] The enzyme preparation according to any one of [13] to [19], wherein the bacterial protease is a Bacillus stearothermophilus-derived protease.
According to the present invention, it is possible to impart a strong taste or flavor to a food or the like, or to enhance the strong taste or flavor of a food.
Drawings
Fig. 1 shows the results of evaluation of hardness in example 2.
Figure 2 shows the results of the free amino acid analysis in example 2.
FIG. 3 shows the results of the free amino acid analysis in example 3.
Fig. 4 shows the results of the free amino acid analysis in example 3.
Fig. 5 shows the results of the free amino acid analysis in example 3.
Fig. 6 shows the results of the free amino acid analysis in example 3.
Detailed Description
According to the present invention, there is provided a method for producing a protein degradation product, comprising the steps of: allowing gamma-glutamyl peptide hydrolase, a protease derived from a filamentous fungus, and a bacterial protease to act on the protein material.
According to the present invention, there is further provided an enzyme preparation for producing a protein degradation product, which contains a gamma-glutamyl peptide hydrolase, a protease derived from a filamentous fungus, and a bacterial protease.
The step of allowing the gamma-glutamyl peptide hydrolase, the filamentous fungus-derived protease and the bacterial protease to act on the protein material may be performed in one step (i.e., a step of allowing the above 3 enzymes to act on the protein material simultaneously), or may be performed in two or three steps (i.e., a step of allowing 1 or 2 enzymes out of the above 3 to act on the protein material, and a step of allowing other enzymes out of the above 3 to act).
Examples of the gamma-glutamyl peptide hydrolase include glutaminase, gamma-glutamyl transferase and gamma-glutamyl cyclase.
As the gamma-glutamyl peptide hydrolase, a microbial-derived gamma-glutamyl peptide hydrolase may be used, and examples thereof include a microbial-derived glutaminase, a gamma-glutamyl transferase, and a gamma-glutamyl cyclase.
The γ -glutamylpeptide hydrolase is preferably a glutaminase derived from a microorganism belonging to the genus Bacillus, and more preferably a glutaminase derived from Bacillus amyloliquefaciens (Bacillus amyloliquefaciens) (e.g., glutaminase SD-C100S available from Tianye enzyme Co., ltd.).
The microorganism-derived γ -glutamyl peptide hydrolase may not be a purified product, and for example, a culture solution, a crushed solution/extract, a partially purified product thereof, or the like of the microorganism producing γ -glutamyl peptide hydrolase may be used. More than 2 microbial source gamma-glutamyl peptide hydrolase may also be used in combination. Some microbial gamma-glutamyl peptide hydrolase is commercially available (e.g., glutaminase SD-C100S described above) and can be readily obtained and utilized.
As the filamentous protease, there may be preferably mentioned an acid protease derived from an Aspergillus microorganism and a neutral protease derived from an Aspergillus microorganism.
Examples of acid proteases of Aspergillus origin are acid proteases of Aspergillus oryzae (Aspergillus oryzae) origin (e.g., protease M "AMANO" SD and protease HF "AMANO"150SD available from Tianye enzyme Co., ltd.).
Examples of Aspergillus microorganism-derived neutral proteases are Aspergillus oryzae (Aspergillus oryzae) and Aspergillus honey (Aspergillus melleus) derived neutral proteases, such as Aspergillus oryzae (Aspergillus oryzae) derived neutral protease (PR-AX, product name ProteaX), aspergillus oryzae (Aspergillus oryzae) derived neutral protease (PR-ASD, product name protease A "AMANO" SD), aspergillus honey (Aspergillus melleus) derived neutral protease (PR-P6 SD, product name protease P "AMANO"6 SD), and Aspergillus oryzae (Aspergillus oryzae) derived neutral protease (PR-AN 100 SD) supplied by Tianye enzyme Co.
The filamentous fungus-derived protease may not be purified, and for example, a culture solution, a disrupted solution/extract, a partially purified product thereof, or the like of a microorganism producing the filamentous fungus-derived protease may be used. More than 2 kinds of filamentous fungus-derived proteases may be used in combination. Some proteases derived from filamentous fungi are commercially available (e.g., protease M "AMANO" SD, protease HF "AMANO"150S, and protease AX, protease A "AMANO" SD, protease P "AMANO"6SD, PR-AN100 SD) and can be readily obtained and used.
As bacterial proteases, metalloproteases are preferred. As the source of the bacterial protease, there may be preferably mentioned a protease derived from a microorganism belonging to the genus Bacillus or Geobacillus, and there may be more preferably mentioned a protease derived from Geobacillus stearothermophilus. As an example of bacterial protease, samoase PC10F available from Tianye enzyme Co., ltd.
The bacterial protease may not be purified, and for example, a culture solution, a disrupted solution/extract, a partially purified product thereof, or the like of a microorganism producing the bacterial protease may be used. More than 2 bacterial proteases may be used in combination. Some bacterial proteases are commercially available (e.g., samoase PC10F described above) and can be readily obtained and utilized.
The enzyme preparation of the present invention containing gamma-glutamyl peptide hydrolase, protease derived from filamentous fungus and bacterial protease may contain, in addition to the active component (the above 3 enzymes), excipients, buffers, suspending agents, stabilizers, preserving agents, preservatives, physiological saline, etc. As the excipient, lactose, sorbitol, D-mannitol, maltodextrin, white sugar and the like can be used. As the buffer, phosphates, citrates, acetates, and the like can be used. As the stabilizer, propylene glycol, ascorbic acid, and the like can be used. As the preservative, phenol, benzalkonium chloride, benzyl alcohol, chlorobutanol, methylparaben, and the like can be used. As the preservative, benzalkonium chloride, parahydroxybenzoic acid, chlorobutanol, and the like can be used.
The content of the active ingredients (the above 3 enzymes) in the enzyme preparation is not particularly limited, and may be appropriately set.
The enzyme agent of the present invention is usually provided in a solid form (for example, an immobilized enzyme in which an enzyme is immobilized in a raw material, which can be immobilized on the surface or inside of particles, powder, silica, porous polymer, or the like) or in a liquid form.
The conditions under which the gamma-glutamyl peptide hydrolase, the protease derived from a filamentous fungus and the bacterial protease are allowed to act on the protein material are, for example, a reaction temperature of 15℃to 70℃and preferably 30℃to 65℃and more preferably 40℃to 60 ℃.
The reaction time and the amount of enzyme are not particularly limited as long as they exert the desired action. Examples of the reaction time include 5 minutes to 48 hours, preferably 10 minutes to 12 hours, and more preferably 15 minutes to 6 hours. The enzyme amount may be, for example, an amount of 0.001% (W/W) to 10% (W/W), preferably 0.01% (W/W) to 2% (W/W) of the concentration of each of the 3 enzymes in the reaction solution.
The protein material is preferably an animal protein material, a plant protein material or a microbial protein material, and more preferably a plant protein material. Specific examples of the protein material include protein materials derived from peas, soybeans, fava beans, chickpeas, barley, wheat, oats, rice, buckwheat, barnyard grass, millet, hemp, algae, almonds, cashews, hazelnuts, pecans, hawaii nuts, pistachios, walnuts, brazil nuts, peanuts, and coconuts.
According to the present invention, a protein degradation product containing a large amount of cysteine capable of forming a maillard reaction (protein degradation product containing cysteine) can be produced. The cysteine that can form the maillard reaction includes, in addition to the cysteine in the free amino acid state, a peptide having a cysteine residue in a state that can undergo the maillard reaction. Cysteine in the form of free amino acids may be preferably used.
According to the present invention, there is further provided a food containing a cysteine-containing protein hydrolysate produced by the method for producing a cysteine-containing protein hydrolysate of the present invention.
The present invention will be specifically described with reference to the following examples, but the present invention is not limited to the examples.
Examples
Example 1 >
The following experiments were conducted with the aim of establishing a method for efficiently producing cysteine from a protein.
1. Studies of cysteine formation
(1) Method of
A protein solution (15% (W/W), pH 5) was prepared by suspending 12g of each protein material in water. An enzyme solution was prepared by dissolving 1.4g of a filamentous protease (protease HF "AMANO"150SD, tianye enzyme Co., ltd.) and 0.7g of a glutaminase (glutaminase SD-C100S, tianye enzyme Co., ltd.) in 20mL of water, and 0.7g of a bacterial protease (Samoase PC10F, tianye enzyme Co., ltd.). After adding 1mL of the enzyme solution to 30mL of the protein solution at 50℃and mixing, the mixture was treated at 50℃for 2 hours. After the treatment solution was centrifuged, the supernatant was recovered. Thiol groups of cysteines contained in the supernatant were quantified using DTNB reagent. To 2.6mL of 0.1M Tris buffer (1 mM EDTA, pH 7.05), 0.2mL of 25mM DTNB solution (50 mM ammonium acetate, 1mM EDTA, pH 5.0) and 0.2mL of the supernatant diluted to an appropriate concentration were added and mixed, and the mixture was kept for 10 to 15 minutes until the reaction was completed. Immediately after the completion of the reaction, the absorbance at 412nm was measured. The amount of cysteine residues in the supernatant was calculated from a standard curve prepared by using 10. Mu.M to 50. Mu.M cysteine solution (1 mM EDTA) instead of the supernatant. In order to confirm the change in taste, 2mL of a solution obtained by neutralizing the supernatant with hydrochloric acid to pH7 was taken out, 1mL of 20% glucose was added, and the solution was boiled for 30 minutes to perform maillard reaction, whereby the intense taste of the sample after the reaction was confirmed. In particular, the change in taste was confirmed by sensory evaluation of the panelists.
(2) Results
By enzyme treatment, cysteine free was confirmed in all protein materials. In addition, it was confirmed that the meat flavor was improved by adding a fibrilia to the Maillard reaction product. Regarding the fibrilia protein, the flavor peculiar to fibrilia was too strong to confirm the change of the intense flavor.
TABLE 1
Example 2 >
To 70g of soybean vegetarian meat (TVP (Textured Vegetable Protein, structural vegetable protein) (DAIZU LABO soybean vegetarian meat foam type; markome Co.) were added 105g (1.5 times amount of water) and allowed to stand for 10 minutes, 8.7g of hypromellose (Metolose), 48.5g of sunflower seed oil and 26.7g of Sunlever 10 (soybean protein powder) were mixed uniformly in the above mixture, 1% of enzyme solution shown in Table 2 (relative to soybean TVP) was added to 25g of the above mixture, and reacted at 50℃for 1 hour, and after the reaction, 6mL of water was added to mold, baking (110℃in an oven, 10 minutes) was performed, and the obtained baked product was subjected to sensory evaluation (evaluation of 5 stages of delicacies and flavors). The sensory evaluation results are shown in Table 3. On the basis of no enzyme, the number was larger, indicating that 1 indicates no change, and 4 indicates a great improvement.
TABLE 2
Table 2: the enzyme agent comprises the following components: 50% of filamentous fungus protease (A) +25% of bacterial metalloprotease+25% of glutaminase (bacterial metalloprotease and glutaminase are the same as in example 1)
| (A) | |
| 1 | Aspergillus oryzae derived acid protease (PR-HF 150 SD) |
| 2 | Aspergillus oryzae origin neutral proteinase (PR-AX) |
| 3 | Aspergillus oryzae derived neutral protease (PR-ASD) |
| 4 | Aspergillus honey source neutral proteinase (PR-P6 SD) |
| 5 | Aspergillus oryzae origin neutral protease (PR-AN 100 SD) |
| 6 | Aspergillus oryzae derived acid protease (PR-MSD) |
TABLE 3 Table 3
Table 3: results of sensory evaluation
| Delicious taste | Fragrance of Chinese medicine | |
| Enzyme-free agent | 1 | 1 |
| 1 | 2.5 | 2 |
| 2 | 3 | 3 |
| 3 | 3 | 3 |
| 4 | 3 | 3 |
| 5 | 3 | 4 |
| 6 | 2.5 | 2 |
The hardness of the baked product obtained was evaluated under the following conditions.
The using device comprises: rheometer (COMPAC-100 II)
Press-in speed: 60mm/min
Distance of movement of the base: 7mm of
(measurement of hardness at a position 7mm from contact with meat)
The evaluation results of the hardness are shown in fig. 1. The vertical axis of FIG. 1 is in N (newtons).
The free amino acids in the resulting baked goods were analyzed as follows.
Distilled water (1 mL) was added to 1g of the baked product, and the mixture was mixed and centrifuged. The supernatant and ethanol were mixed (deproteinized) at supernatant: ethanol=1:1. The mixture was centrifuged, and the supernatant was recovered, diluted 12.5 times with water, filtered through a microfiltration Membrane (MF) and analyzed by HPLC. The conditions for HPLC analysis are as follows. The results of the analysis of free amino acids are shown in FIG. 2.
Agilent high performance liquid chromatograph (Agilent HPLC,1260 InfinityII)
Buffer a: 20mM Na 2 HPO 4 ·H 3 PO 4 pH8.2
Buffer B: methanol to acetonitrile to water=45:45:10
Chromatographic column: HPH-C18 2.7 μm 3.0X100 mm (Porosill)
Flow rate: 0.65mL/min
0－0.35min： A：96％， B：4％
0.35－13.4min： A：43％， B：57％
13.4－13.5min： A：0％， B：100％
13.5－15.7min： A：0％， B：100％
15.7－15.8min： A：96％， B：4％
15.8－18min： A：96％， B：4％
Example 3 >
To a 10% (w/v) vegetable protein solution (pea: pea protein (Usuki pharmaceutical), soybean: sun 10 (no two-step oil production)) was added 4% enzyme (2% filamentous protease+1% bacterial protease+1% glutaminase) relative to the weight of vegetable protein. The mixture was treated at 50℃for 2 hours at 400rpm to allow reaction. The reaction was boiled for 10 minutes, centrifuged, and the supernatant was recovered. The resulting sample supernatant was subjected to sensory evaluation and free amino acid analysis.
(sensory evaluation)
Sample supernatant 4mL was collected, and 2mL of 20% glucose was added. The resulting mixture was placed in boiling water, treated for 30 minutes, and subjected to sensory evaluation. The results are shown in Table 4. The larger the number, on an enzyme-free basis, the greater the improvement, 1 indicating no change and 5 indicating a substantial improvement.
TABLE 4 Table 4
(analysis of free amino acids)
Sample supernatant and ethanol were mixed (protein removed) at sample supernatant: ethanol=1:1. The mixture was centrifuged, and the supernatant was collected, diluted 12.5 times with water, filtered with a microfiltration Membrane (MF) and analyzed by HPLC (amino acid analysis) under the same conditions as in example 2. The results of the analysis of the free amino acids are shown in FIGS. 3 to 6.
Claims (16)
1. A method for producing a cysteine-containing protein degradation product, which comprises the steps of: allowing gamma-glutamyl peptide hydrolase, a protease derived from a filamentous fungus, and a bacterial protease to act on the protein material.
2. The method of claim 1, wherein the gamma-glutamyl peptide hydrolase is a glutaminase, a gamma-glutamyl transferase, or a gamma-glutamyl cyclase.
3. The method according to claim 1 or 2, wherein the gamma-glutamylpeptide hydrolase is a bacillus microorganism-derived glutaminase.
4. A method according to any one of claims 1 to 3, wherein the gamma-glutamylpeptide hydrolase is a bacillus amyloliquefaciens-derived glutaminase.
5. The method according to any one of claims 1 to 4, wherein the filamentous fungus protease is an acid protease derived from an Aspergillus microorganism or a neutral protease derived from an Aspergillus microorganism.
6. The method of any one of claims 1-5, wherein the filamentous fungal protease is an aspergillus oryzae-derived acidic protease, an aspergillus oryzae-derived neutral protease, or an aspergillus melleus-derived neutral protease.
7. The method of any one of claims 1-6, wherein the proteinaceous material is an animal proteinaceous material, a plant proteinaceous material, or a microbial proteinaceous material.
8. The method of any one of claims 1-7, wherein the proteinaceous material is a vegetable proteinaceous material.
9. The method of any one of claims 1-7, wherein the proteinaceous material is a pea, soybean, fava bean, chickpea, barley, wheat, oat, rice, buckwheat, barnyard grass, millet, hemp, algae, almond, cashew, hazelnut, pecan, hawaii, pistachio, walnut, brazil nut, peanut, coconut-derived proteinaceous material.
10. A food product comprising a cysteine-containing protein hydrolysate produced by the method of any one of claims 1 to 9.
11. An enzyme preparation for producing cysteine-containing protein decomposition product comprises gamma-glutamyl peptide hydrolase, protease derived from filamentous fungus and bacterial protease.
12. The enzymatic agent according to claim 11, wherein the gamma-glutamyl peptide hydrolase is a glutaminase, a gamma-glutamyl transferase, or a gamma-glutamyl cyclotransferase.
13. An enzymatic agent according to claim 11 or 12 wherein the γ -glutamyl peptide hydrolase is a bacillus microorganism-derived glutaminase.
14. The enzyme agent according to any one of claims 11 to 13, wherein the γ -glutamylpeptide hydrolase is a bacillus amyloliquefaciens-derived glutaminase.
15. The enzyme preparation according to any one of claims 11 to 14, wherein the filamentous fungus protease is an acid protease derived from an aspergillus microorganism or a neutral protease derived from an aspergillus microorganism.
16. The enzyme preparation according to any one of claims 11 to 15, wherein the filamentous fungus protease is an aspergillus oryzae-derived acidic protease, an aspergillus oryzae-derived neutral protease, or an aspergillus melleus-derived neutral protease.
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