NL2031244A - System for preparing collagen tripeptide (gly-x-y) microparticles - Google Patents
System for preparing collagen tripeptide (gly-x-y) microparticles Download PDFInfo
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- NL2031244A NL2031244A NL2031244A NL2031244A NL2031244A NL 2031244 A NL2031244 A NL 2031244A NL 2031244 A NL2031244 A NL 2031244A NL 2031244 A NL2031244 A NL 2031244A NL 2031244 A NL2031244 A NL 2031244A
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- Prior art keywords
- gly
- unit
- collagen
- collagen tripeptide
- tripeptide
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
- A23J3/06—Gelatine
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/10—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from hair, feathers, horn, skins, leather, bones, or the like
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
- A23J3/342—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of collagen; of gelatin
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- 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]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/0806—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Rheumatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Mycology (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Abstract
The present application discloses a system for preparing collagen tripeptide (Gly-X-Y) microparticles, which comprises a pretreatment part for extracting fish skin gelatin from fresh fish skin, a reaction part for hydrolyzing the fish skin gelatin with enzymes to obtain a collagen tripeptide (Gly-X-Y), and a refining part for refining the collagen tripeptide (Gly-X-Y) to form the collagen tripeptide (Gly-X-Y) microparticles haVing an embedded particle structure.
Description
Specification SYSTEM FOR PREPARING COLLAGEN TRIPEPTIDE (GLY-X-Y)
[0001] The present application relates to a food manufacturing system, in particular to a system for preparing collagen tripeptide (Gly-X-Y) microparticles.
[0002] Collagen is an important protein in the human body, usually one of the constituents of skin, bones, cartilages, ligaments, blood vessels, tendons and connective tissues. However, as the human body ages, the amount of collagen production decreases and externally manifests as, for example, wrinkles on the skin.
[0003] In order to improve the above-mentioned problem, related collagen products are sold or circulated in the market, and are usually in a powder form, a lozenge form or a liquid form. Among them, collagen products in a lozenge form are taken orally to supplement collagens for uptake, and the liquid collagen products can be used as wound dressings for medical purposes, and can also be taken orally to supplement desired collagens for uptake.
[0004] However, if collagen products are stored in undesired environmental conditions, such as being exposed to direct sunlight for a long time or in a high-temperature environment, deterioration is likely to occur, which means that the structure of collagen may be disrupted, which in turn reduces activity.
[0005] In addition, conventional preparation methods for producing collagen mainly comprise procedures such as obtaining raw materials (such as fish skin or fish scale), chopping, and hydrolysis. Various types and quantities of devices are required in the preparation process, and each device operates independently. If the devices are manually controlled, errors will often occur, resulting in quality fluctuations between batches of collagen products.
[0006] Based on the above description, it can be seen that conventional collagen products have the disadvantages of being difficult to store and unstable in quality, which are the problems that the related practitioners urgently want to improve.
1
[0007] Therefore, the primary object of the present application is to provide a system for preparing collagen tripeptide (Gly-X-Y) microparticles, which is able to provide automated operations to ensure the quality of the finished product.
[0008] Accordingly, the present application provides a system for preparing collagen tripeptide (Gly-X-Y) microparticles, which comprises a pretreatment part, a reaction part and a refining part, wherein the pretreatment part is used for receiving a fresh fish skin and pretreating the fresh fish skin to form an intermediate product; the reaction part is disposed behind the pretreatment part for receiving the intermediate product and adding an enzyme to react with the intermediate product, thereby producing a collagen tripeptide (Gly-X-Y); and the refining part is disposed behind the reaction part for receiving and refining the collagen tripeptide (Gly-X-Y) to form the collagen tripeptide (Gly-X-Y) microparticles. The collagen tripeptide (Gly-X-Y) microparticles produced by the system have high content of active peptide ingredients, and can maintain their functional activity to a certain extent, as well as prolong the shelf life of the product therefrom.
[0009] In one embodiment, the intermediate product is fish skin gelatin.
[0010] Figure 1 is a schematic diagram of the system for preparing collagen tripeptide (Gly-X-Y) microparticles disclosed in a preferred embodiment of the present application. Figure 2 is a block diagram of the system for preparing collagen tripeptide (Gly-X-Y) microparticles disclosed in a preferred embodiment of the present application. Figure 3 is a flow chart of the system for preparing collagen tripeptide (Gly-X-Y) microparticles disclosed in a preferred embodiment of the present application. Figure 4 is a partial cross-sectional view of the collagen tripeptide (Gly-X-Y) microparticles in a preferred embodiment of the present application. Figure 5 shows the results of absorption capacity experiments in the digestive tract of rats in each group. Figure 6 shows the results of collagen production experiments of human dermal fibroblasts in each group in the absence of vitamin C. FIG. 7 shows the results of collagen production experiments of human dermal fibroblasts in each 2 group in the presence of vitamin C.
Figure 8 shows the results of hyaluronic acid production experiments of human dermal fibroblasts in each group.
Figure 9 shows the results of collagen synthesis experiments of rats in each group.
Figure 10 shows the results of collagen production experiments of human osteoblasts in each group. Figure 11 shows the results of calcium synthesis experiments of human osteoblasts in each group, as measured by the absorbance value at 562 nm.
Figure 12 shows the results of bone strength assessing experiments performed on rats in each group. Figure 13 and Figure 14 show the results of healing experiments of injured tendon performed on rats in each group. Figure 15 shows the results of healing experiments of injured cartilage tissue performed on rabbits in each group. Figure 16 shows the results of experiments performed on patients with knee degenerative joint disease in each group.
[0011] Firstly, referring to Figures 1-3, a system for preparing collagen tripeptide (Gly-X-Y) microparticles provided in a preferred embodiment of the present application mainly comprises a unidirectional processing path that is provided with a pretreatment part 10, a reaction part 20 and a refining part 30 in sequence for mass production. Wherein, the pretreatment part 10, the reaction part 20 and the refining part 30 are connected with each other by pipelines, so as to achieve the purpose of automatic operation.
[0012] The pretreatment unit 10 compirses a crushing unit 11, a screening unit 12, a reaction treatment unit 13 and an extraction unit 14 which are connected in sequence. Among them, the crushing unit 11 is used for receiving and chopping a fresh fish skin to form a crushed product. The screening unit 12 is disposed behind the crushing unit 11 for receiving and screening the crushed product. The reaction treatment unit 13 is disposed behind the screening unit 12 for receiving the screened and crushed product and adding an acid and/or a base for reaction to obtain a decomposed mixture. The extraction unit 14 is disposed behind the reaction treatment unit 13 for receiving and extracting the decomposed mixture to obtain an intermediate product. In this embodiment, the intermediate product is fish skin gelatin. In addition, the pretreatment unit 10 is further provided 3 with a crushing unit 11A between the crushing unit 11 and the screening unit 12, which can crush solid particles of the crushed product from the crushing unit 11 into smaller size.
[0013] The reaction part 20 is disposed behind the pretreatment part 10 for receiving the intermediate product and adding an enzyme to react with the intermediate product, thereby producing a collagen tripeptide (Gly-X-Y). In this embodiment, the reaction part 20 has a stirring unit 21, the stirring unit comprising a tank for accommodating the enzyme, the intermediate product and a liquid, and a stirring part disposed in the tank for uniformly mixing the enzyme and the intermediate product in the tank and distributing them in the liquid.
[0014] The refining part 30 comprises a concentration and sterilization unit 31, a drying unit 32 and an embedding unit 33. Among them, the concentration and sterilization unit 31 is used for receiving the collagen tripeptide (Gly-X-Y) and performing a concentration and sterilization procedure thereon. The drying unit 32 is disposed behind the concentration and sterilization unit 31 for heating and drying the concentrated and sterilized collagen tripeptide (Gly-X-Y) to produce a collagen tripeptide (Gly-X-Y) powder. The embedding unit 33 is disposed behind the drying unit 32 for receiving the collagen tripeptide (Gly-X-Y) powder, and mixing and processing the collagen tripeptide (Gly-X-Y) powder with a base material to form the collagen tripeptide (Gly-X-Y) microparticles.
[0015] In addition, the collagen tripeptide (Gly-X-Y) microparticles 40 have a diameter between 60 um and 1000 um, and further comprise a core layer 41 and a coating layer 42, as shown in Figure 4.
[0016] Further, the core layer 41 comprises the collagen tripeptide, which is composed of a Gly-Xaa-Yaa sequence, wherein Gly is glycine, and Xaa and Yaa are one of the following amino acids: glycine, asparagine, glutamate, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, tyrosine, aspartate, histidine, methionine, arginine, serine, threonine, lysine, glutamine, cysteine, proline, hydroxyproline and the like.
[0017] The collagen tripeptide of the present application is prepared from fish skin. However, in other embodiments, the collagen tripeptide can also be extracted from other animal tissues, such as pig skin. Since the molecular mass of the collagen tripeptide is 300 Dalton (Da), which is one thousandth of that of conventional collagen, it is easier to be absorbed by the human intestine and can achieve an absorption rate and utilization rate optimal for the human body. In other words, the collagen tripeptide (Gly-X-Y) microparticles prepared by the system of the present application can 4 improve the absorption rate and utilization rate of collagen in the human body, and thus can effectively improve the consumer's favorability and repurchase rate.
[0018] By above-mentioned structural design, the specific implementation steps of the present application are as follows:
[0019] Step A: subjecting fresh fish skin to crushing, screening, reaction treatment and extraction in sequence, to obtain fish skin gelatin;
[0020] Step B: decomposing the fish skin gelatin with enzymes to producing a collagen tripeptide (Gly-X-Y); and
[0021] Step C: subjecting the collagen tripeptide (Gly-X-Y) to concentration, sterilization, drying and embedding, to obtain collagen tripeptide (Gly-X-Y) microparticles.
[0022] The following are real world experimental data according to the present application.
[0023] Example 1: Absorption in the digestive tract
[0024] Figure 5 shows the results of rat experiments. Rats were divided into an experimental group A and a control A according to restriction conditions. The experimental group A comprises rats fed with the collagen tripeptide of the present application, and the control A comprises rats fed with conventional amino acids.
[0025] As shown in Figure 5, the amount of collagen tripeptide absorbed was greater than that of amino acids within a predetermined period of time.
[0026] Example 2: Collagen production
[0027] Firstly, experiments were performed in the absence of vitamin C with human dermal fibroblasts and different amount of the collagen tripeptide. As shown in Figure 6, the addition of the collagen tripeptide helped to increase collagen production.
[0028] Secondly, experiments were performed in the presence of vitamin C with human dermal fibroblasts and different amount of the collagen tripeptide. As shown in Figure 7, the addition of the collagen tripeptide and vitamin C significantly increased collagen production.
[0029] Example 3: Hyaluronic acid production
[0030] Figure 8 shows the results of experiments with human dermal fibroblasts. The experimental group C was added with the collagen tripeptide and the experimental group C' was added with glucosamine. The control C was added with only water. As shown in Figure 8, the amount of hyaluronic acid produced in the experimental group C was greater than that in the experimental group C', and the amount of hyaluronic acid produced in the experimental group C' 5 was greater than that in the control C.
[0031] Example 4: Collagen synthesis
[0032] Figure 9 shows the results of rat experiments. The experimental group D was added with the collagen tripeptide, the experimental group D' was added with an amino acid mixture, the experimental group D" was added with undecomposed collagen, and the experimental group D" was added with a conventional collagen peptide. The control D was without any of these components. As shown in Figure 9, the hydroxyproline content in the experimental group D was greater than those in other experimental groups. Thus, the collagen tripeptide of the present application can promote collagen synthesis.
[0033] Example 5: Collagen production
[0034] Figure 10 shows the results of experiments with human osteoblasts. The experimental group E was added with 10ug/ml of the collagen tripeptide, and the control E was without the collagen tripeptide. As shown in Figure 10, the collagen content in the experimental group E was greater than that in the control E. Thus, the collagen tripeptide of the present application can promote collagen production in bones.
[0035] Example 6: Calcium synthesis
[0036] Figure 11 shows the results of experiments with human osteoblasts under different amount of the collagen tripeptide. As can be seen, the higher the amount of collagen tripeptide added, the greater the calcium synthesis.
[0037] Example 7: Bone strength assessment
[0038] Figure 12 shows the experimental results of rats fed with different amount of the collagen tripeptide. As can be seen, the higher the amount of collagen tripeptide fed, the greater the applied weight ratio.
[0039] Example 8: Healing promotion of tendon injury
[0040] Figures 13 and 14 show the results of experiments utilizing rats with the Achilles tendon severed and fed with different amount of the collagen tripeptide.
[0041] As can be seen from Figures 13 and 14, the higher the amount of collagen tripeptide fed, the higher the ratio of collagen content and the higher the ratio of tendon tension.
[0042] Example 9: Healing of injured cartilage tissue
[0043] Figure 15 shows the results of rabbit experiments obtained from observing changes of the cartilage tissue surface of an injured knee joint after four weeks. The experimental group F was fed 6 with the collagen tripeptide, the experimental group F' was fed with the conventional collagen, and the control F was not fed with the collagen tripeptide or the conventional collagen.
[0044] As can be seen from Figure 15, compared with other groups, the experimental group F showed more reduction in the injured site.
[0045] Example 10: Improvement of knee degenerative joint disease
[0046] Figure 16 shows the changes in human clinical trials performed on patients with knee the knee degenerative joint disease over 10 weeks. The experimental group G was given 4g of the collagen tripeptide and the control G was not given the collagen tripeptide.
[0047] As can be seen from Figure 16, the experimental group G had more improvement in knee pain than the control G. 5
Claims (5)
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN202958670U (en) * | 2012-12-27 | 2013-06-05 | 烟台新大洋水产食品有限公司 | Production line for preparing collagen by using sleeve-fish skin |
| KR20140015876A (en) * | 2012-07-26 | 2014-02-07 | 영산홍어(주) | Production method of collagen peptide derived from fishskin and roduction method of oil soluble collagen peptide |
| CN203429169U (en) * | 2013-09-09 | 2014-02-12 | 青州隆贝生物科技有限公司 | Automatic collagen production line |
| CN203498380U (en) * | 2013-07-23 | 2014-03-26 | 吴长海 | Production line for preparing collagen peptide from yak bone |
| CN108485961A (en) * | 2018-06-29 | 2018-09-04 | 邱芳萍 | The production line of collagen peptide is extracted from wood frog's fallopian tube skin |
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- 2021-04-04 TW TW110203645U patent/TWM616785U/en unknown
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- 2022-03-04 DE DE202022101209.1U patent/DE202022101209U1/en active Active
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20140015876A (en) * | 2012-07-26 | 2014-02-07 | 영산홍어(주) | Production method of collagen peptide derived from fishskin and roduction method of oil soluble collagen peptide |
| CN202958670U (en) * | 2012-12-27 | 2013-06-05 | 烟台新大洋水产食品有限公司 | Production line for preparing collagen by using sleeve-fish skin |
| CN203498380U (en) * | 2013-07-23 | 2014-03-26 | 吴长海 | Production line for preparing collagen peptide from yak bone |
| CN203429169U (en) * | 2013-09-09 | 2014-02-12 | 青州隆贝生物科技有限公司 | Automatic collagen production line |
| CN108485961A (en) * | 2018-06-29 | 2018-09-04 | 邱芳萍 | The production line of collagen peptide is extracted from wood frog's fallopian tube skin |
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| NL2031244B1 (en) | 2023-01-06 |
| DE202022101209U1 (en) | 2022-03-28 |
| TWM616785U (en) | 2021-09-11 |
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