WO2009140833A1 - 霞水母来源有免疫增强活性的胶原蛋白肽及制备和应用 - Google Patents
霞水母来源有免疫增强活性的胶原蛋白肽及制备和应用 Download PDFInfo
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- WO2009140833A1 WO2009140833A1 PCT/CN2008/072397 CN2008072397W WO2009140833A1 WO 2009140833 A1 WO2009140833 A1 WO 2009140833A1 CN 2008072397 W CN2008072397 W CN 2008072397W WO 2009140833 A1 WO2009140833 A1 WO 2009140833A1
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- WIPO (PCT)
- Prior art keywords
- collagen peptide
- acid
- jellyfish
- peptide according
- preparing
- Prior art date
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43595—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from coelenteratae, e.g. medusae
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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 COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
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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 COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
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- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/39—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
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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
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
Definitions
- Collagen peptide with immunopotentiating activity derived from Xia jellyfish, preparation and application thereof
- the invention relates to a collagen peptide with immune enhancement activity derived from Xia jellyfish and a preparation process thereof, and belongs to the field of natural biological active substances.
- Cyanea nozaki i is a large marine plankton, belonging to the Phylum Cnidaria, Class Scyphomedusae, Order Phylum cnidaria, and Xia jellyfish.
- Family Cyanea There are four species of Cyanea nozaki Kishinouye, Cyanea capillata, Cyanea ferruginea Eschscholtz, and CyEmea purpurea Kishinouye.
- White Xia jellyfish has the largest number and the widest distribution range. Xia jellyfish is usually bait with small zooplankton. Its gonads are developed, its reproductive ability is strong, and its growth rate is extremely fast. At present, the annual output of Xia jellyfish in China has reached 10 million tons, which constitutes a new natural marine biological resource.
- Marine-derived polysaccharides, proteoglycans and collagen peptides are important natural marine food resources, and often have significant biological activities, such as sea cucumber polysaccharides, seaweed polysaccharides, etc., which have been reported to have significant biological activity.
- Research reports on the separation and extraction of collagen peptides from Xia jellyfish are rare at home and abroad. So far, there have been no reports on the isolation and extraction of collagen peptides with immunopotentiating activity. Summary of the invention
- the invention discloses a collagen peptide derived from Xia jellyfish and having immunopotentiating activity, and a preparation process and application thereof. More uniquely, it uses a new type of natural marine biological resource, Xia Shuimu (Cyim ⁇ 'O- as a raw material for the preparation of collagen peptides, to achieve the purpose of development and utilization of Xia jellyfish.
- the invention operates to obtain a high-purity collagen peptide product in an extremely high yield, which is essential for the comprehensive utilization of the natural jellyfish, a natural marine living resource.
- a collagen peptide derived from Xia jellyfish derived from an immunopotentiating activity characterized in that it has a white or yellowish appearance, an odorless, slightly bitter powder, and a seawater jellyfish (C) w ⁇ / ⁇ ⁇ H ⁇ ⁇ ⁇ ), Cyweflilla (Cy wefl capillata), Cywefl ferruginea Escfec/iote or Purple Jellyfish (Cyanea purpurea S ⁇ w ⁇ ) freshly caught or isolated from the marinated pickled products, non-toxic, with significant immune-enhancing activity, containing 80-90% protein, 10 ⁇ 20% of sugar, the average molecular weight is between 1,000 and 3,000.
- the monosaccharide contains glucose as the main component.
- the glycine in the amino acid accounts for more than 16%, and the combination of proline and hydroxyproline accounts for more than 18%.
- the solubilization treatment refers to the use of a melting agent to melt the Xia Shui mother into water to form a liquid.
- the type of the hydrolyzing agent and the temperature used in the hydrolysis are the most important for the hydrolysis yield.
- the effective solvent is a common alkali (such as sodium, potassium, calcium, barium hydroxide or carbonate, ammonia, etc.)
- the concentration is 0.1 ⁇ 10molL - common acid (such as hydrochloric acid, phosphoric acid, sulfuric acid, etc.
- Acid or acid acetic acid, malic acid, lactic acid, citric acid and other organic acids, concentration of 0.1 ⁇ 10mol L - ⁇ or various proteases (such as pepsin, trypsin, trypsin, acid protease, alkaline protease, neutral protease
- proteases such as pepsin, trypsin, trypsin, acid protease, alkaline protease, neutral protease
- papain, bromelain, collagenase, elastase, etc. melted at a pH of 0.5 to 14.0, at a temperature of 10 to 120 ° C, and at an operating pressure of 0.0001 to 0.5 MPa.
- sodium is a solvent
- the pH should be in the range of 7.0 - 14.0.
- the pH should be in the range of 0.5-6.8.
- the pH should be The optimum pH range of the enzyme is selected; when the acid-base is used as the solvent, the melting temperature should be in the range of 10 - 120 ° C, preferably in the range of 0 - 60 ° C.
- hydrolysis should be carried out at an optimum temperature of the protease.
- the soaking should be carried out at a certain value within the range of pH adjustment of 2-12, preferably in water of 6.5 ⁇ 6.8, and the soaking temperature is in the range of 0 ⁇ 98 °C, preferably 0 ⁇ 15°. Within the range of C, the soaking operation is carried out until the conductivity of the soaking water is lower than 3 ( ⁇ Scm- 1 stops. Centrifugal separation is carried out at 0 ⁇ 120 °C, preferably at 0 ⁇ 10 °C, the speed of the centrifuge Between 4000 and 12000 rpm, preferably between 6000 and 8000 rpm, the centrifugation time is 10 to 60 minutes.
- the drying method of the liquid may be freeze drying or spray drying.
- the Xia jellyfish active collagen peptide of the invention has been confirmed by preliminary research, has significant immunopotentiating activity, and can be widely used as a novel bioactive material and health food raw material for food, health care products, skin care and beauty products, medical supplies, etc. In the field, it is used for preparing medicines, health products, skin care and beauty products with immune enhancement functions.
- the above melt treatment can also be carried out under the operating pressure of 0.001 MPa.
- a clear and transparent liquid which is a collagen peptide solution
- the collagen peptide solution is concentrated at 40 ° C, O.OOlMPa to After 1/2 of the original volume, it was freeze-dried to obtain 1000 g of a collagen peptide powder solid having a purity-enhancing activity of 95% or more.
- Example three The above melt treatment can also be carried out under the operating pressure of 0.1 MPa.
- Example three The above melt treatment can also be carried out under the operating pressure of 0.1 MPa.
- a sample of collagen peptide powder (e.g., prepared according to the method of Example 2) was used to determine the protein content, the determination of the total sugar content, the determination of the amino acid composition, and the determination of the monosaccharide composition. The results showed that the sample contained 88% protein, 10.5% sugar, and the average molecular weight was 1274.
- the monosaccharide contained is mainly glucose, and the composition of the amino acids contained in Table 1 is shown in Table 1.
- mice Administration dose One-week weight gain Growth rate Number of deaths Blank control 10 0.5ml/only 3.374g 14.79% 0
- the experimental group 10 7500mg/kg 3.299g 14.55% 0
- the activity of the mice decreased within 1 hour after administration, and gradually resumed normal activities after 4 hours.
- the food intake increased gradually within 7 days, and the appetite, spirit and hair color of the mice were normal.
- the neck was sacrificed and the main organ lesions and poisoning were not observed in the eyes, liver, spleen, lung and kidney.
- the observation period was weighed every day for 7 days, and the weight of the mice in the test group increased continuously.
- the results of the study showed that in the case of large doses of the test sample, no mice died and no significant toxicity was observed. It indicates that it is non-toxic or has little toxicity, and its maximum safe dose is above 7500mg/Kg.
- Test group 25 0.26 soil 0.04
- Hemolysin is a method that reflects the status of humoral immune function. If the hemolysin production increases after administration, the absorbance value of red blood cell hemolysis increases, indicating that the humoral immunity of the body is enhanced after administration. From the results in Table 4, the difference between the high-dose group and the blank control group was significant (P ⁇ 0.05). There was no difference between the low-dose group and the middle-dose group and the control group (P>0.05), indicating that the high dose was high. The test sample has a significant effect on the production of serum hemolysin (IgM), showing a better humoral immune enhancement.
- Delayed hypersensitivity reaction is a method to reflect the status of cellular immune function. It can be seen from Table 5 that the difference in weight between the left and right auricles of the experimental group is increased compared with the control group, and the difference between the middle dose group and the blank control group. There was a significant difference (P ⁇ 0.01), and there was no significant difference between the low-dose group and the high-dose group (P > 0.05). It indicates that the sample can significantly improve the cellular immune function of mice in a certain concentration range.
- Test group 25 32.58 soil 1.16 2.25 soil 1.00
- the phagocytic function of phagocytic cells is a method to reflect the status of non-specific immune function. It can be seen from Table 6 that the percentage of phagocytosis is significantly different between the middle dose group and the high dose group compared with the control group (P ⁇ 0.05), the middle dose group and the high dose group. The phagocytic index was significantly different from the control group (P ⁇ 0.01). There was no difference between the low dose group and the control group (P>0.05), indicating that a certain dose of the test sample can activate phagocytic activity and increase mononuclear phagocytic cells. System phagocytosis.
- the results of the cellular immune function, the humoral immune function, the mononuclear-macrophage function, and the NK cell activity are positive in two aspects, and the test sample can be judged to have an enhanced immunity function.
- This experiment is positive in the three aspects of cellular immune function, humoral immune function and monocyte-macrophage function in experimental mice, so it can be determined that the test sample has immunopotentiating effect.
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US12/993,819 US8450100B2 (en) | 2008-05-20 | 2008-09-17 | Collagen peptide having immune-enhancing activity from Cyanea nozakii and preparation method and uses thereof |
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CNA2008100249146A CN101353380A (zh) | 2008-05-20 | 2008-05-20 | 霞水母来源有免疫增强活性的胶原蛋白肽及制备和应用 |
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US8450100B2 (en) | 2008-05-20 | 2013-05-28 | Lili Zhang | Collagen peptide having immune-enhancing activity from Cyanea nozakii and preparation method and uses thereof |
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CN102178636B (zh) * | 2011-04-27 | 2012-10-10 | 中国科学院南海海洋研究所 | 一种用于细致毛孔的海洋生物功能化妆品 |
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CA2937613C (en) | 2013-01-23 | 2021-03-02 | Bottled Science Limited | Skin enhancing beverage composition |
CN103255113B (zh) * | 2013-05-21 | 2015-01-14 | 中国人民解放军第二军医大学 | 一种发形霞水母过氧化物还原酶及其编码基因与应用 |
WO2014209101A2 (en) * | 2013-06-28 | 2014-12-31 | Universiti Putra Malaysia | Method of obtaining gelatin from aquatic animals |
CN104212864A (zh) * | 2014-08-22 | 2014-12-17 | 青岛龙宫海洋牧场生态修复工程有限公司 | 一种水母活性胶原蛋白水解产物的提取工艺 |
CN107073076A (zh) * | 2014-11-11 | 2017-08-18 | 株式会社日皮 | 免疫活化剂、细胞性免疫活化剂及t细胞增殖剂 |
US11060122B2 (en) * | 2017-05-10 | 2021-07-13 | Robert den Hoed | Method of producing jellyfish collagen extract |
CN109770275A (zh) * | 2019-02-22 | 2019-05-21 | 水母娘娘海洋生物科技有限公司 | 一种海月水母水及其制备方法和应用 |
CN111995671B (zh) * | 2020-09-07 | 2023-06-20 | 青海瑞肽生物科技有限公司 | 一种胶原蛋白肽及其应用 |
CN112568441A (zh) * | 2020-12-23 | 2021-03-30 | 北京可利可徕科技有限公司 | 一种增强免疫力的组合物及其制备方法 |
CN113318003A (zh) * | 2021-04-08 | 2021-08-31 | 海臻(上海)生物科技有限公司 | 一种水母多肽及其应用 |
CN116082492A (zh) * | 2022-06-14 | 2023-05-09 | 浙江海洋大学 | 一种来源于龙头鱼骨胶原蛋白的Nrf2激动肽 |
CN115005352B (zh) * | 2022-06-17 | 2023-04-11 | 日照壳美乐海洋生物科技有限公司 | 一种壳寡糖复合阿胶蛋白肽的组合物及其制备方法 |
CN118169997B (zh) * | 2024-03-25 | 2024-08-23 | 山东谦和云科技有限公司 | 一种gnss授时同步控制器的控制方法、装置及介质 |
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