WO2022168413A1 - デプレスタチン含有組成物の製造方法 - Google Patents

デプレスタチン含有組成物の製造方法 Download PDF

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Publication number
WO2022168413A1
WO2022168413A1 PCT/JP2021/043685 JP2021043685W WO2022168413A1 WO 2022168413 A1 WO2022168413 A1 WO 2022168413A1 JP 2021043685 W JP2021043685 W JP 2021043685W WO 2022168413 A1 WO2022168413 A1 WO 2022168413A1
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Prior art keywords
deprestatin
temperature
composition
raw material
enzyme
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English (en)
French (fr)
Japanese (ja)
Inventor
康浩 鹿島
泰治 松川
健二 長田
泰正 山田
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Uha Mikakuto Co Ltd
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Uha Mikakuto Co Ltd
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Priority to JP2022579356A priority Critical patent/JP7787424B2/ja
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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/185—Vegetable proteins
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products

Definitions

  • the present invention relates to a method for producing a composition containing deprestatin, which has an improving effect on depression and inflammatory neurodegenerative diseases, from a raw material solution containing soy protein.
  • Patent Document 1 discloses three novel peptides that have an effect of improving low motivation, depression, or depressive mood disorder.
  • the peptide of SEQ ID NO: 1 is known as "deprestatin", a partial sequence of beta-conglycinin ( ⁇ -CG) protein, which is the major storage protein of soybean.
  • Deprestatin is said to be obtainable from ⁇ -CG protein by hydrolysis of thermolysin.
  • soybean protein can be obtained.
  • the inventors have completed the present invention by finding that deprestatin concentration in enzymatic digests can be improved.
  • the gist of the present invention is [1] A method for producing a deprestatin-containing composition, comprising an enzymatic treatment step of hydrolyzing a raw material solution containing soy protein with a proteolytic enzyme while raising the temperature in the range of 5 to 70°C.
  • a composition containing a high amount of deprestatin can be produced from a raw material solution containing soy protein.
  • the resulting deprestatin-containing composition imparts neuropsychological function-improving effects such as an effect of improving motivation, depression, or depressive mood disorders derived from deprestatin by blending in various foods. It becomes possible to produce a nutrient-enriched food composition.
  • FIG. 1 is a graph showing the results of deprestatin content in the deprestatin-containing compositions obtained in Example 1 and Comparative Example 1.
  • FIG. 2 is a graph showing the results of the mouse tail suspension test performed in Example 3.
  • a raw material solution containing soy protein is hydrolyzed with a proteolytic enzyme while the temperature is raised in the range of 5 to 70°C. It has an enzymatic treatment process that In the method of the present invention, by including the enzyme treatment step, the enzymatic reaction at the enzymatic cleavage site contained in the amino acid sequence of deprestatin is suppressed, and a composition containing a higher amount of deprestatin than in the conventional method is produced. can do.
  • excessive hydrolysis of soybean protein is suppressed by increasing the temperature compared to the case where the temperature of the enzyme reaction is adjusted to be constant, and a peptide containing deprestatin can be efficiently obtained. It is conceivable that
  • the deprestatin is a 10 amino acid sequence: Leu-Ser-Ser-Thr-Gln-Ala-Gln-Gln-Ser-Tyr (SEQ ID NO: 1) is a peptide consisting of Deprestatin is known to have the effect of improving low motivation, depression or depressive mood disorders (Patent Document 1).
  • "decreased motivation” and “depressive mood disorder” include mental (mental) impulses such as lack of motivation and lack of interest in anything.
  • “Low motivation” and “depressive mood disorder” are not limited to diseases or conditions caused by depression, and states of persons not diagnosed with depression such as aging (aging), stress (e.g. adjustment disorder), etc. also includes
  • the raw material liquid containing soybean protein used in the present invention is not particularly limited as long as it contains soybean beta-conglycinin ( ⁇ -CG) protein.
  • the ⁇ -CG is a kind of protein constituting soybean protein.
  • Examples of the raw material liquid include a mixture with water containing pulverized soybeans, squeezed juice, or purified products thereof. It is sufficient that the raw material liquid contains sufficient water for the hydrolysis reaction by the protease to occur, and the content of water in the raw material liquid is not particularly limited.
  • the pulverized product may be obtained using a pulverizer known in the food field. Also, the state of pulverization is not particularly limited as long as it allows an enzymatic reaction with the protease. Examples include pomace (also referred to as meal or defatted soybean) obtained by extracting soybean oil from soybeans.
  • the squeezed juice may be obtained by using a juice squeezer, a presser, or the like known in the food field.
  • the pulverized product or squeezed juice may be purified by a method known in the food field, and examples thereof include commercial products containing soybean protein as a main component, purified ⁇ -CG protein, and the like.
  • the pulverized soybean, the squeezed juice, or the purified product thereof as described above can be mixed with water to form a mixed solution, so that the enzymatic treatment with the proteolytic enzyme can be performed efficiently.
  • the content of water in the mixed liquid is not particularly limited.
  • the raw material solution containing the soybean protein is mixed with a proteolytic enzyme.
  • a proteolytic enzyme used in the present invention, if a protease with a low optimum temperature is used, it becomes difficult to carry out the reaction at a low temperature.
  • Proteases derived from microorganisms of the genus Rhizopus, Bacillus and the like can be preferably used.
  • proteases derived from the genus Bacillus "Sumizym (registered trademark) ACP” (manufactured by Shin Nippon Chemical Industries, Ltd.), “Protease M (Amano) G” (manufactured by Amano Enzyme Co., Ltd.) (above, derived from Aspergillus oryzae) , "Orientase (registered trademark) 20A” (manufactured by HBI Co., Ltd.), “Denapsin (TM) 2P” (manufactured by Nagase ChemteX Co., Ltd.) (above, derived from Aspergillus niger), “Neurase ( R) F3G” (manufactured by Amano Enzyme Co., Ltd.), “Protin (TM) SD-NY10” derived from the genus Bacillus (manufactured by Amano Enzyme Co., Ltd.), "Orientase (registered trademark)
  • thermolysin is preferably used in the method of the present invention from the viewpoint of efficiently decomposing soybean protein.
  • Thermolysin is a proteolytic enzyme (protease) derived from a thermotolerant bacterium, Bacillus thermoproteolyticus (EC 3.4.24.4, EC 3.4.24.27).
  • Thermolysin can be used as a food additive in Japan.
  • Commercially available products such as food additive grade thermolysin can be used. Examples of the commercially available thermolysins include "Samoase PC10F” and “Samoase GL30" (both manufactured by Amano Enzyme Co., Ltd.).
  • a raw material solution containing soybean protein is hydrolyzed with a proteolytic enzyme while the temperature is raised within a temperature range of 5 to 70°C.
  • a method for increasing the temperature from the starting temperature any method may be used as long as the temperature is increased over time. For example, a method of gradually heating, a method of raising the temperature in stages, and the like can be mentioned.
  • the starting temperature for the temperature rise may be adjusted to be lower than the optimum temperature of the protease to be used, and can be appropriately selected from the temperature range of 5 to 40°C.
  • the starting temperature may be, for example, 10° C. or higher, or 15° C. or higher.
  • the upper limit of the initiation temperature may be set to 40° C. or lower.
  • the starting temperature may be, for example, 30° C. or lower.
  • the temperature in the second step is 45 to 70 ° C., 45 to 65 ° C., 45 to 55 ° C., 47 to 53 ° C., 49 to It can be appropriately selected from 51° C. and the like.
  • the temperature of the third stage or higher may be set, and in this case, it can be appropriately selected from 56 to 70°C, 58 to 65°C, 59 to 62°C, and the like.
  • the reaction time in the enzyme treatment step may be 48 hours or less, and from the viewpoint of efficient enzyme treatment, it may be appropriately selected from about 1 to 10 hours, about 2 to 5 hours, and the like.
  • the pH of the raw material solution containing the soybean protein that undergoes the enzymatic reaction can be appropriately selected from about pH 6.5 to 8.5 and about pH 7 to 8.
  • the pH adjustment may be performed using a pH adjuster or the like.
  • the protease is deactivated by a known method.
  • the deactivation method is not particularly limited, but may be, for example, heating the raw material solution undergoing the enzymatic reaction (eg, heating at a temperature exceeding 80° C. for about 5 to 60 minutes).
  • the end of the enzymatic treatment is determined by checking the pH of the enzymatic treatment solution over time and confirming that the pH has not decreased. do it.
  • the enzyme-treated solution obtained in the enzyme treatment step can be used as it is as a deprestatin-containing composition, but if necessary, insoluble components may be removed.
  • the insoluble components are unreacted proteins and macromolecular peptides derived from the raw material protein. Removal of these insoluble components not only increases the concentration of deprestatin in the composition, This has the advantage of increasing solubility, making it easier to incorporate deprestatin-containing compositions into a variety of food products (improved processing properties).
  • insoluble component removal step for example, a method of adjusting the pH of the enzyme-treated solution obtained in the enzyme treatment step to 4 to 6 to remove insoluble components can be used.
  • an acid that can be used according to the intended use may be used from inorganic acids such as hydrochloric acid, sulfuric acid, nitric acid and phosphoric acid, and organic acids such as citric acid, acetic acid and malic acid. .
  • decantation, filtration, centrifugation, etc. are mentioned as a method of removing an insoluble component.
  • a known protein purification method such as ultrafiltration or column chromatography may be used.
  • the resin used as the separation material for the ultrafiltration or column chromatography a resin capable of separating deprestatin may be used, and the type of resin is not particularly limited.
  • the deprestatin-containing composition obtained as described above is highly concentrated and pulverized by removing water by existing drying methods such as freeze-drying, spray-drying and drum-drying, and can be used stably. can do.
  • the deprestatin-containing composition obtained as described above can be incorporated into a food or drink to prepare a nutrient-enriched food composition. Since deprestatin is obtained from soybean protein, a nutrient-enriched food composition can be easily prepared by using a deprestatin-containing composition instead of a protein raw material.
  • the deprestatin-containing composition obtained by the present invention has a higher content of deprestatin than that obtained by the conventional method, and is a nutritious food containing deprestatin as an active ingredient compared to the conventional method. It becomes possible to manufacture the composition efficiently and at low cost.
  • the deprestatin-containing composition obtained in the present invention should have a deprestatin content of 1.2 mg/g or more from the viewpoint of easily exerting the desired effect derived from deprestatin. preferable.
  • the content of the deprestatin-containing composition should be such that the effects of deprestatin can be expected. Just do it.
  • the content of deprestatin in the nutrient-enriched food composition is adjusted to contain 40 ⁇ g or more, preferably 800 ⁇ g or more, more preferably 1 mg or more of deprestatin per dose for humans. do it.
  • the deprestatin-containing composition is added to the food or drink, it may be mixed with other raw materials, and the timing of addition is not particularly limited.
  • the form of the nutrient-enriched food composition is not particularly limited. , gum, candy, tablets, gummies, buns, sweet bean jelly, pudding, jelly, ice cream, sherbet, etc.), processed marine products (kamaboko, chikuwa, hanpen, etc.), processed livestock products (hamburgers, hams, sausages, wieners, cheese, Butter, yogurt, fresh cream, margarine, fermented milk, etc.), soup (powdered soup, liquid soup, etc.), staple foods (rice, noodles (dried noodles, raw noodles, pasta), bread, cereals, etc.), seasonings ( mayonnaise, shortening, dressing, sauce, sauce, soy sauce, etc.) and the like.
  • Example 1 10% suspension of isolated soy protein "GS5100” (manufactured by Gushen Biological Technology, protein content of 90% or more) or isolated soy protein "Supro 661” (manufactured by DuPont, protein content of 90% or more) mixed with water Liquids were prepared and used as raw material liquids containing soy protein.
  • Samoase PC10F was added to the raw material solution (room temperature: 25°C) at a concentration of 1 mg/ml, adjusted to pH 7.0 using a 10 mol/L sodium hydroxide aqueous solution, and stirred at room temperature for 1 hour while gently stirring. enzymatically reacted.
  • the enzymatic reaction was carried out for 1 hour while gently stirring at pH 7.0 and 50°C. Furthermore, after raising the liquid temperature to 60° C., the enzymatic reaction was carried out for 1 hour while gently stirring at pH 7.0. Next, the resulting enzyme-treated solution was freeze-dried, and the deprestatin content (mg/g) in the freeze-dried powder was measured by LCMS/MS.
  • Example 1 The results obtained are shown in FIG. In addition, in FIG. 1, the content of deprestatin is shown in “ ⁇ g/g”. From the results of FIG. 1, the deprestatin-containing composition obtained in Example 1 was superior to that of Comparative Example 1 in both "GS5100” and "Supro 661". Since the statin concentration is as high as 113 to 131%, it can be seen that the yield per unit raw material of deprestatin is higher in Example 1, and the concentration is higher.
  • Example 2 The enzyme-treated solution of soybean protein "GS5100" obtained in the same manner as in Example 1 was adjusted to pH 6.0 by dropping hydrochloric acid while stirring, and then centrifuged (8,000 rpm x 20 minutes, 25°C). Then, the supernatant (acidic treatment solution) was recovered. Then, part of the acidic treatment liquid was filtered through an ultrafiltration membrane (molecular weight cut off: MWCO 30000), and the filtrate (UF filtrate) was recovered. Two fractions of the acid-treated liquid and the UF filtrate were lyophilized respectively, and the content of deprestatin in each dry powder was determined by LCMS/MS. Table 1 shows the results obtained.
  • the amount of deprestatin was 1525 ⁇ g/g in the enzyme-treated solution, 3113 ⁇ g/g in the acid-treated solution, and 3978 ⁇ g/g in the UF filtrate. It was confirmed that the concentration was increased by a factor of two and about three times, respectively. It can be seen that the acidic treatment liquid has the insoluble components removed and is a deprestatin-containing composition with good solubility. In addition, since the concentration of deprestatin in the UF filtrate is higher than that in the acid-treated solution, the action and effect derived from deprestatin can be expected even if the amount added to the food is small, resulting in better processing characteristics. It can be seen that it is a deprestatin-containing composition.
  • Example 3 A mouse tail suspension test was performed as follows. Eight-week-old Slc:ddY mice (Japan SLC, Inc.) were given the composition containing deprestatin obtained in Example 1 (using "Supro 661") and the composition obtained in Comparative Example 1 ( “Supro 661”) were each administered with the gastric tube. The dosage of the deprestatin-containing composition obtained in Example 1 was adjusted to 5 mg/kg BW, and the dosage of the composition obtained in Comparative Example 1 was adjusted to 10 mg/kg BW. In addition, the solvent (water) was administered to the control group with a probe.
  • the ratio (%) of motionless time to the total measured time was calculated by the formula: motionless time (seconds)/360 (seconds) x 100. It should be noted that administration of a substance having an antidepressant effect reduces the immobility time. Therefore, when a decrease in immobility time is observed, it can be evaluated as having an antidepressant-like effect.
  • a state of immobility is considered to be a state of despair, and a decrease in the period of immobility is an index of improvement of the state of despair, that is, improvement of motivation.
  • Example 4 Production example of nutrient-enriched food composition
  • the freeze-dried powder obtained in Example 1 is 12.5%, and sorbitol is 86%. .3%, 1.0% calcium stearate, and 0.2% perfume were mixed, well mixed, and then tableted with a tableting machine to prepare a deprestatin-containing chewable.
  • the physical properties such as hardness of the resulting deprestatin-containing chewable product were the same as those of the conventional product. From the above, it was found that a nutrient-enriched food composition containing an effective amount of deprestatin can be easily prepared by blending the deprestatin-containing composition obtained by the present invention as a raw material component of a food or drink.

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PCT/JP2021/043685 2021-02-04 2021-11-29 デプレスタチン含有組成物の製造方法 Ceased WO2022168413A1 (ja)

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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023114846A1 (en) * 2021-12-15 2023-06-22 Digestome Therapeutics, Inc. Uses of therapeutic peptides
WO2024259556A1 (en) * 2023-06-19 2024-12-26 Viage Therapeutics, Inc. Uses of therapeutic peptides

Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH02240028A (ja) * 1989-03-14 1990-09-25 Agency Of Ind Science & Technol 血圧降下剤
JPH0687886A (ja) * 1990-02-27 1994-03-29 Agency Of Ind Science & Technol 新規オリゴペプチド、アンジオテンシン変換酵素阻害 剤及び血圧降下剤
JPH0769922A (ja) * 1993-08-27 1995-03-14 Nissin Food Prod Co Ltd アンジオテンシン変換酵素阻害蛋白分解物
JP2005053812A (ja) * 2003-08-01 2005-03-03 Maruzen Pharmaceut Co Ltd アンジオテンシンｉ変換酵素阻害剤及びその製造方法、並びに機能性食品
JP2006520809A (ja) * 2003-03-18 2006-09-14 サントリー株式会社 アンジオテンシン変換酵素阻害ペプチド
JP2012046450A (ja) * 2010-08-27 2012-03-08 Unitika Ltd アンジオテンシン変換酵素阻害ペプチド及びその製造方法。
JP6667781B2 (ja) * 2015-03-02 2020-03-18 国立大学法人京都大学 ペプチド
WO2021100614A1 (ja) * 2019-11-19 2021-05-27 国立大学法人京都大学 大豆ペプチド及び／又はコラーゲンペプチド含有神経心理学的機能改善剤

Patent Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH02240028A (ja) * 1989-03-14 1990-09-25 Agency Of Ind Science & Technol 血圧降下剤
JPH0687886A (ja) * 1990-02-27 1994-03-29 Agency Of Ind Science & Technol 新規オリゴペプチド、アンジオテンシン変換酵素阻害 剤及び血圧降下剤
JPH0769922A (ja) * 1993-08-27 1995-03-14 Nissin Food Prod Co Ltd アンジオテンシン変換酵素阻害蛋白分解物
JP2006520809A (ja) * 2003-03-18 2006-09-14 サントリー株式会社 アンジオテンシン変換酵素阻害ペプチド
JP2005053812A (ja) * 2003-08-01 2005-03-03 Maruzen Pharmaceut Co Ltd アンジオテンシンｉ変換酵素阻害剤及びその製造方法、並びに機能性食品
JP2012046450A (ja) * 2010-08-27 2012-03-08 Unitika Ltd アンジオテンシン変換酵素阻害ペプチド及びその製造方法。
JP6667781B2 (ja) * 2015-03-02 2020-03-18 国立大学法人京都大学 ペプチド
WO2021100614A1 (ja) * 2019-11-19 2021-05-27 国立大学法人京都大学 大豆ペプチド及び／又はコラーゲンペプチド含有神経心理学的機能改善剤

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023114846A1 (en) * 2021-12-15 2023-06-22 Digestome Therapeutics, Inc. Uses of therapeutic peptides
WO2024259556A1 (en) * 2023-06-19 2024-12-26 Viage Therapeutics, Inc. Uses of therapeutic peptides

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