WO2011152330A1 - Anti-oxydant contenant un hydrolysat de protéine de soja, et son utilisation - Google Patents
Anti-oxydant contenant un hydrolysat de protéine de soja, et son utilisation Download PDFInfo
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- WO2011152330A1 WO2011152330A1 PCT/JP2011/062321 JP2011062321W WO2011152330A1 WO 2011152330 A1 WO2011152330 A1 WO 2011152330A1 JP 2011062321 W JP2011062321 W JP 2011062321W WO 2011152330 A1 WO2011152330 A1 WO 2011152330A1
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K36/00—Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
- A61K36/18—Magnoliophyta (angiosperms)
- A61K36/185—Magnoliopsida (dicotyledons)
- A61K36/48—Fabaceae or Leguminosae (Pea or Legume family); Caesalpiniaceae; Mimosaceae; Papilionaceae
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
- A61K38/011—Hydrolysed proteins; Derivatives thereof from plants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/168—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/06—Free radical scavengers or antioxidants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2200/00—Function of food ingredients
- A23V2200/02—Antioxidant
Definitions
- the present invention relates to an antioxidant containing soybean protein white hydrolyzate, and a method of using soybean protein hydrolyzate as an antioxidant.
- Aerobic organisms including humans take oxygen by respiration for survival, but some of the oxygen taken into the body at this time is reactive oxygen species such as superoxide radicals, hydrogen peroxide, and hydroxy radicals during energy metabolism. Changes to. Such reactive oxygen species originally played an important role in maintaining health, such as being involved in biological defense including the pathogen removal mechanism of macrophages during bacterial or viral infection. However, due to environmental factors such as air pollution and ultraviolet rays, lifestyle habits such as smoking, mental stress, etc., the balance in the body is lost, and once the active oxygen species becomes excessive, it reacts with proteins, lipids, DNA, etc. in the body.
- soybean isoflavone has been confirmed to have high antioxidant activity like other flavonoids.
- peptide sequences exhibiting antioxidant activity have been identified. However, it is difficult in production to isolate a large amount of a specific peptide from soybean protein hydrolyzate and use it as an antioxidant. Therefore, it is useful if soybean protein hydrolyzate itself, which is a mixture of various peptides, can be used as an antioxidant.
- Patent Document 1 describes a hydrolyzate of soybean protein having an increased antioxidant power, and describes that the average molecular weight of the peptide is 3 kDa to 30 kDa (3000 to 30000). This document obtains relatively high molecular weight peptides in order to avoid expression of bitterness due to excessive hydrolysis.
- Patent Documents 2 and 3 also describe a hydrolyzate of soy protein exhibiting antioxidative activity, but the average molecular weight of the peptide described in Patent Document 2 is 500 to 5000. The average amino acid chain length is 10 to 100, and the molecular weight is approximately 1200 or more.
- Patent Document 4 describes hydrolysates by various prostheses derived from Bacillus subtilis, Aspergillus oryzae, etc., as soybean protein hydrolysates having antioxidant activity, and the hydrolysates have a molecular weight. It is described that 2,000 or less are collected by filtration, and the content of free amino acids in the hydrolyzate is 20 to 30% by weight. Although these soy protein hydrolysates are recognized to have a certain antioxidant activity, the activities are not necessarily at a level that can be put to practical use as an antioxidant, and soy protein hydrolysates that exhibit higher antioxidant activity are required. ing.
- JP 2005-80668 A Japanese Patent Laid-Open No. 10-203994 Japanese Unexamined Patent Publication No. 2000-4896 Japanese Patent Laid-Open No. 2003-210138
- This invention made it the subject to provide the antioxidant which shows the high antioxidant activity which can be utilized for food-drinks or a pharmaceutical.
- the present inventor obtained a soybean protein hydrolyzate in which the content of peptides having a molecular weight of less than 500 in the protein hydrolyzate is 50% by weight or more based on the total amount of peptides and free amino acids.
- the present inventors have found that an antioxidant having higher antioxidant activity than before can be obtained, and have completed the present invention.
- the present invention provides the following (1) to (13).
- Antioxidant for use as an active ingredient in a method for preventing or treating diseases caused by oxidation in a living body wherein the content of peptides having a molecular weight of less than 500 in protein hydrolyzate is the sum of peptides and free amino acids
- An antioxidant comprising 50% by weight or more of a soy protein hydrolyzate
- the antioxidant substance according to (1), wherein the disease caused by oxidation of the living body is arteriosclerosis, myocardial infarction, cancer, diabetes, Alzheimer, or hay fever.
- the content of peptides having a molecular weight of less than 500 in the protein hydrolyzate as antioxidants as active ingredients is peptides and Adding the soy protein hydrolyzate which is 50% by weight or more based on the total amount of free amino acids, (6)
- An antioxidant substance containing soybean protein hydrolyzate in which the content of peptides having a molecular weight of less than 500 in the protein hydrolyzate is
- a method for preventing or treating diseases caused by oxidation of a living body (8) an antioxidant comprising a soy protein hydrolyzate in which the content of a peptide having a molecular weight of less than 500 in the protein hydrolyzate is 50% by weight or more based on the total amount of the peptide and free amino acids; (9) The antioxidant according to (8), wherein the soy protein hydrolyzate is a soy protein hydrolyzate from which insolubles after hydrolysis have been removed, (10) The antioxidant according to (8), further comprising one or more antioxidants selected from vitamins, polyphenols, carotenoids, saponins, and allicin, (11) A food or drink to which the antioxidant according to (8) is added, (12) A pharmaceutical comprising the antioxidant according to (8) as an active ingredient, (13) A method for using soy protein hydrolysis in which the content of a peptide having a molecular weight of less than 500 in the protein hydrolyzate is 50% by weight or more based on the total amount of the peptide
- a peptide having a specific antioxidant activity is not isolated from a soy protein hydrolyzate, but a practical, high antioxidant activity using a soy protein hydrolyzate (peptide mixture) itself.
- An oxidizing agent can be provided, which can be used for prevention or treatment of diseases such as arteriosclerosis caused by oxidation of a living body.
- the antioxidant of the present invention the antioxidant for use as an active ingredient in the method of preventing or treating the disease caused by oxidation of the living body of the present invention, and the prevention or treatment of the disease caused by oxidation of the living body of the present invention
- the content of a peptide having a molecular weight of less than 500 in the protein hydrolyzate is the total amount of the peptide and free amino acid. It contains 50% by weight or more of soy protein hydrolyzate or is used as an active ingredient.
- the soy protein hydrolyzate according to the present invention is a soy protein raw material hydrolyzed with a protease.
- the soy protein raw material there are full-fat soy milk and defatted soy milk from which protein components are extracted with water from whole soybeans, defatted soybeans, etc., and the okara components are removed.
- isolated soy protein obtained by concentrating the protein from these soymilks by treatment with an ultrafiltration membrane or isoelectric point precipitation using an acid can be mentioned.
- soy protein raw material concentrated soy protein obtained by removing whey components from soybean by acid washing or ethanol washing to concentrate the protein, and soybean powder obtained by pulverizing soybean. These soy protein raw materials may be sterilized and dried. In addition, it is preferable that the soybean protein raw material finally obtained contains 80 weight% or more of protein by dry weight, for example, isolation
- Isolated soy protein is generally prepared as follows. That is, water is added to defatted soybean, extraction is performed near neutrality, soy milk is separated to obtain soy milk. Next, the soy milk is adjusted to around pH 4.5, and the isoelectric point precipitate is collected.
- the isolated soybean protein thus obtained may be used as it is in the following steps, or may be used after dissolving an unsterilized product or a sterilized product after drying. It is also possible to make reducing sugar an aqueous solution in advance and dissolve the soy protein raw material in this solution.
- the separated soybean protein is not limited to the above-described production method, and it goes without saying that the production method may be variously modified.
- the soybean protein hydrolyzate according to the present invention is a peptide mixture obtained by subjecting the soybean protein raw material to protease treatment.
- the protein hydrolyzate preferably has a higher degree of degradation, and in particular, the ratio of peptides having a molecular weight of less than 500 to the total amount of peptides and free amino acids in the hydrolyzate is preferably high.
- it is important that the content of peptides having a molecular weight of less than 500 in the protein hydrolyzate is 50% by weight or more with respect to the total amount of peptides and free amino acids, and more preferably 60% by weight or more. preferable.
- the peptide having a molecular weight of less than 500 is substantially composed of a dipeptide and a tripeptide in which 2 to 3 amino acids are bonded.
- the content of the peptide having a molecular weight of less than 500 is determined by measuring the ratio of the peptide having a molecular weight of less than 500 and a free amino acid fraction in the protein hydrolyzate by gel filtration chromatography for peptides, and then calculating the release in the protein hydrolyzate calculated by amino acid analysis. It shall be calculated by subtracting the amino acid content.
- the soy protein hydrolyzate identified as described above preferably has a reduced ratio of peptides and free amino acids other than peptides having a molecular weight of less than 500 as much as possible.
- the free amino acid content in the protein hydrolyzate is preferably 12% by weight or less, more preferably 5% by weight or less, and still more preferably 3% by weight or less based on the total amount of the peptide and free amino acid. . Furthermore, since it is desirable that the peptide in the protein hydrolyzate has a lower molecular weight, the fraction ratio of the molecular weight of 500 or more in the protein hydrolyzate is 40% by weight with respect to the total amount of peptide and free amino acid. It is preferably at most 38% by weight, more preferably at most 35% by weight.
- protease used to obtain the soy protein hydrolyzate according to the present invention regardless of animal origin, plant origin or microbial origin, is classified into “metal protease”, “acidic protease”, “thiol protease”, " It can be appropriately selected from proteases classified as “serine protease”, preferably proteases classified as “metal protease”, “thiol protease” and “serine protease”.
- a degradation method in which enzymes belonging to two or more, or three or more different classifications are acted on sequentially or simultaneously can increase the proportion of peptides having a molecular weight of less than 500.
- protease is a classification method based on the type of amino acid at the active center, which is usually performed in the field of enzyme science.
- metal protease includes Bacillus-derived neutral protease, Streptomyces-derived neutral protease, Aspergillus-derived neutral protease, “Samoase”, etc.
- acidic protease includes pepsin, Aspergillus-derived acidic protease, “ “Sumiteam FP” and the like
- thiol protease includes bromelain, papain and the like
- seerine protease includes trypsin, chymotrypsin, subtilisin, Streptomyces-derived alkaline protease, “alkalase”, “bioprese” and the like .
- the classification can be confirmed by the action pH and the reactivity with inhibitors. Since the site of action on the substrate is greatly different between enzymes having different active centers, it is possible to reduce “uncut residue” and efficiently obtain an enzyme degradation product. In addition, enzymatic degradation products can be produced more efficiently by using enzymes of different origins (origin organisms) together. Even in the same classification, if the origins are different, the site of action on the protein as a substrate is also different, and as a result, the proportion of peptides having a molecular weight of less than 500 can be increased. These proteases preferably have low exoprotease activity.
- the reaction pH and reaction temperature of the protease treatment may be set in accordance with the characteristics of the protease to be used. Usually, the reaction pH is carried out near the optimum pH, and the reaction temperature may be carried out around the optimum temperature. In general, the reaction temperature is 20 to 80 ° C., preferably 40 to 60 ° C. After the reaction, the enzyme is heated to a temperature sufficient to inactivate the enzyme (about 60 to 170 ° C.) to inactivate the residual enzyme activity.
- the reaction solution after the protease treatment can be used as it is or after being concentrated, but is usually sterilized, spray-dried, freeze-dried, etc. and used in the form of a dry powder.
- Sterilization is preferably heat sterilization, and the heating temperature is preferably 110 to 170 ° C, more preferably 130 to 170 ° C.
- the heating time is preferably 3 to 20 seconds.
- the value (unit: micromol TE / g) of "ORAC" (Oxygen Radical Absorbance Capacity: active oxygen absorption capacity) measured by the method of a nonpatent literature 1 is used. It can be an indicator.
- the unit “TE” is an abbreviation of “Trolox equivalent”, and “Trolox” is a registered trademark of “6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid” which is a standard substance. .
- Antioxidant activity can be synergistically enhanced by using one or more extracts containing sucrose.
- the form in which other antioxidants are used in combination is not particularly limited, and can be used by previously mixing with the soy protein hydrolyzate according to the present invention to prepare a mixed preparation. In the present invention, the soy protein hydrolyzate can be used. When using the decomposition product, it is also possible to add other antioxidants separately.
- antioxidants examples include vitamins, polyphenols, carotenoids, saponins, and allicin.
- Vitamins include vitamin C, vitamin A, vitamin E, and the like.
- Polyphenols include flavonoids such as isoflavone, quercetin, myricetin, kaempferol, hesperidin, naringin, anthocyanin, catechin, chrysin, apigenin, luteolin, and lignans such as sesamin, sesaminol, sesaminol, episesamin, sesamol, sesamoline.
- carotenoids include carotenes ( ⁇ -, ⁇ -, ⁇ -, ⁇ -) and lycopene, or xanthophylls such as lutein, astaxanthin, zeaxanthin, canthaxanthin, fucoxanthin, anthaxanthin, violaxanthin, capsaicin and the like. And the like.
- saponins examples include saponins derived from herbal medicines such as Kiraya saponin, soybean saponins, tea saponins and the like.
- plant extracts containing them can be used instead.
- anthocyanins blueberry extract, cassis extract, acai extract, elderberry extract and the like can be used.
- vitamin C, pycnogenol, acai extract, curcumin or sesamin in combination with a strong synergistic effect.
- Soy protein hydrolyzate having a content of peptides with a molecular weight of less than 500 in the protein hydrolyzate according to the present invention of 50% by weight or more based on the total amount of peptides and free amino acids is used as an antioxidant. It can be used for various foods and drinks. For example, it can add to food-drinks for the purpose of antioxidant of food-drinks itself.
- the protein hydrolyzate according to the present invention has a physiological content for a person who has taken it by adding soy protein hydrolyzate having a content of a peptide having a molecular weight of less than 500 to 50% by weight or more based on the total amount of peptides and free amino acids.
- beverages tablets, food bars, salad dressings, meat products, snack confectionery, desserts, confectionery, nutritional supplements, etc. that can exert the antioxidant power as a function and prevent the following diseases caused by oxidation of the living body Can do.
- the soy protein hydrolyzate in which the content of peptides having a molecular weight of less than 500 in the protein hydrolyzate according to the present invention is 50% by weight or more based on the total amount of peptides and free amino acids can also be used as a pharmaceutical product.
- Diseases caused by oxidation of the living body include arteriosclerosis, myocardial infarction, cancer, diabetes, Alzheimer, hay fever and the like, and can be used as pharmaceuticals for preventing and treating these diseases.
- When used as a pharmaceutical form it can be used in various forms such as liquid, powder, tablet, capsule and the like.
- the molecular weight distribution of the soy protein hydrolyzate was measured by the HPLC method using the following gel filtration column.
- An HPLC system using a gel filtration column for peptides was assembled, a known peptide serving as a molecular weight marker was charged, and a calibration curve was obtained in relation to the molecular weight and the retention time.
- the molecular weight markers are [ ⁇ -Asp] -Angiotensin II ⁇ -Asp-Arg-Val-Tyr-Ile-His-Pro-Phe (molecular weight 1046) as octapeptide and Angiotensin IV Val-Tyr- as hexapeptide.
- the ratio (%) of the free amino acid in the protein hydrolyzate and the peptide fraction having a molecular weight of less than 500 was determined by the ratio of the area of the molecular weight less than 500 (time range) to the total absorbance chart area (column used). : Superdex Peptide 7.5 / 300GL (manufactured by GE Healthcare Japan Ltd.), solvent: 1% SDS / 10 mM phosphate buffer, pH 8.0, column temperature 25 ° C., flow rate 0.25 ml / min, detection wavelength: 220 nm) .
- the ratio (%) of the peptide fraction having a molecular weight of 500 or more in the protein hydrolyzate was determined by the ratio of the area having a molecular weight of 500 or more to the total absorbance chart area as described above.
- the free amino acid content in the protein hydrolyzate was measured by amino acid analysis. Protein hydrolyzate (4 mg / ml) was added to an equal volume of 3% sulfosalicylic acid and shaken at room temperature for 15 minutes. Centrifugation was performed at 10,000 rpm for 10 minutes, and the obtained supernatant was filtered with a 0.45 ⁇ m filter, and free amino acids were measured with an amino acid analyzer “JLC500V” (manufactured by JEOL Ltd.).
- the free amino acid content in the protein hydrolyzate was calculated as a ratio to the protein content obtained by the Kjeldahl method.
- the value obtained by subtracting the “free amino acid content” from the “ratio of free amino acids and peptide fractions having a molecular weight of less than 500” obtained above was defined as “content of peptides having a molecular weight of less than 500” in the proteolysate.
- separation soybean protein was prepared from the low modified
- Production Example 4 Preparation of soy protein hydrolyzate (soy protein hydrolyzate E, F, G) A 3% solution of the separated soybean protein obtained in Production Example 1 was prepared, and 1%, 1.5% or 2% of the same “samoyase” as in Production Example 3 was added per protein, and pH 9.0, 58 ° C. for 60 minutes. Enzymatic reaction was performed. Next, 0.5%, 0.75%, or 1% of the same “bioplase” as in Production Example 3 was added, and the enzyme reaction was performed at pH 7.5, 58 ° C. for 60 minutes.
- a solution in which 100 mg of each sample was made up to 100 ml and a solution in which 100 mg of soybean protein hydrolyzate G was made up to 100 ml were mixed at a ratio of 1: 1, and the measurement was performed at a specified dilution ratio.
- the soy protein hydrolyzate G alone has an ORAC value of 551 ⁇ mol TE / g, but when used in combination with various antioxidant components, each component has its own antioxidant properties (no addition) (See (-) data) was confirmed to be synergistically enhanced (see added (+) data). Furthermore, since the synergistic effect of antioxidant properties is the value of a mixture of soybean protein hydrolyzate G and food ingredients in a ratio of 1: 1, even if the amount of food ingredients added is reduced by half, the antioxidant effect is the food ingredient alone It shows a higher value. In particular, when used in combination with vitamin C, pycnogenol, acai extract, curcumin, and sesamin, it was confirmed that the single antioxidant activity was enhanced more than twice, and a high synergistic effect was exhibited.
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Abstract
Priority Applications (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN2011800268113A CN102917723A (zh) | 2010-05-31 | 2011-05-30 | 含有大豆蛋白水解物的抗氧化剂及其用途 |
| KR1020127032395A KR20130081231A (ko) | 2010-05-31 | 2011-05-30 | 대두 단백질 가수 분해물 함유 항산화제 및 그 이용 |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
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| JP2010124430A JP2011246425A (ja) | 2010-05-31 | 2010-05-31 | 大豆蛋白質加水分解物含有抗酸化剤 |
| JP2010-124430 | 2010-05-31 |
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| Publication Number | Publication Date |
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| WO2011152330A1 true WO2011152330A1 (fr) | 2011-12-08 |
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| PCT/JP2011/062321 Ceased WO2011152330A1 (fr) | 2010-05-31 | 2011-05-30 | Anti-oxydant contenant un hydrolysat de protéine de soja, et son utilisation |
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| JP (1) | JP2011246425A (fr) |
| KR (1) | KR20130081231A (fr) |
| CN (1) | CN102917723A (fr) |
| TW (1) | TW201204266A (fr) |
| WO (1) | WO2011152330A1 (fr) |
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| KR101638551B1 (ko) * | 2014-07-10 | 2016-07-12 | (주)제니트리 | 피부미백 및 피부주름 개선용 조성물, 이를 이용한 피부미백 및 피부주름 개선제의 제조방법 및 이를 포함하는 피부 외용제 |
| JP6709016B2 (ja) * | 2014-12-25 | 2020-06-10 | 太陽化学株式会社 | ラウリン酸系油脂含有食品の劣化臭抑制剤 |
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| CN107296283A (zh) * | 2017-06-07 | 2017-10-27 | 东北农业大学 | 一种大豆蛋白—花青素复合物的制备方法 |
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| CN109797183B (zh) * | 2019-02-28 | 2020-12-29 | 江南大学 | 一种具有抗油脂氧化功能的活性肽及其制备方法和应用 |
| CN110547355A (zh) * | 2019-06-06 | 2019-12-10 | 东北农业大学 | 一种利用水酶法大豆水解液制备功能性蛋白复合物的方法 |
| CN111248327B (zh) * | 2020-01-19 | 2022-09-20 | 北京工商大学 | 一种利用大豆提取物提高咖啡豆品质的加工方法及咖啡豆 |
| CN114847478B (zh) * | 2022-04-28 | 2023-08-22 | 江苏大学 | 一种提高大蒜素稳定性的方法 |
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| JP2009051746A (ja) * | 2007-08-24 | 2009-03-12 | Fuji Oil Co Ltd | クレアチンホスホキナーゼ分泌抑制組成物 |
| JP2009084197A (ja) * | 2007-09-28 | 2009-04-23 | Fuji Oil Co Ltd | 内因性オピオイドペプチドの血中分泌促進用組成物 |
| JP2009209080A (ja) * | 2008-03-04 | 2009-09-17 | Fuji Oil Co Ltd | アディポネクチン分泌促進組成物 |
| JP2010248134A (ja) * | 2009-04-16 | 2010-11-04 | Rheology Kino Shokuhin Kenkyusho:Kk | ペプチド組成物 |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPWO2006134752A1 (ja) * | 2005-06-15 | 2009-01-08 | 不二製油株式会社 | 大豆ペプチド組成物 |
| JP2006347946A (ja) * | 2005-06-15 | 2006-12-28 | Fuji Oil Co Ltd | 成長ホルモン分泌促進組成物 |
| JPWO2007139128A1 (ja) * | 2006-05-31 | 2009-10-08 | 不二製油株式会社 | クレアチンホスホキナーゼ分泌抑制組成物 |
-
2010
- 2010-05-31 JP JP2010124430A patent/JP2011246425A/ja active Pending
-
2011
- 2011-05-30 WO PCT/JP2011/062321 patent/WO2011152330A1/fr not_active Ceased
- 2011-05-30 KR KR1020127032395A patent/KR20130081231A/ko not_active Withdrawn
- 2011-05-30 TW TW100118861A patent/TW201204266A/zh unknown
- 2011-05-30 CN CN2011800268113A patent/CN102917723A/zh active Pending
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| JP2009051746A (ja) * | 2007-08-24 | 2009-03-12 | Fuji Oil Co Ltd | クレアチンホスホキナーゼ分泌抑制組成物 |
| JP2009084197A (ja) * | 2007-09-28 | 2009-04-23 | Fuji Oil Co Ltd | 内因性オピオイドペプチドの血中分泌促進用組成物 |
| JP2009209080A (ja) * | 2008-03-04 | 2009-09-17 | Fuji Oil Co Ltd | アディポネクチン分泌促進組成物 |
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| NAOHIKO YAMAGUCHI ET AL.: "Yushi no Anteisei ni Oyobosu Amino Kagobutsu no Eikyo III Daizu Tanpakushitsu no Kasui Bunkaibutsu no Kosankaryou to Tocopherol tono Sojosei", NIHON SHOKUHIN KOGYO GAKKAISHI, vol. 22, no. 9, 1975, pages 431 - 435 * |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN116875648A (zh) * | 2023-04-18 | 2023-10-13 | 天津科技大学 | 一种具有抗氧化和拮抗铅损伤作用的大豆多肽制备方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| KR20130081231A (ko) | 2013-07-16 |
| CN102917723A (zh) | 2013-02-06 |
| JP2011246425A (ja) | 2011-12-08 |
| TW201204266A (en) | 2012-02-01 |
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