CN112521489A - Moisturizing collagen active peptide and preparation process thereof - Google Patents
Moisturizing collagen active peptide and preparation process thereof Download PDFInfo
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 88
- 102000008186 Collagen Human genes 0.000 title claims abstract description 67
- 108010035532 Collagen Proteins 0.000 title claims abstract description 67
- 229920001436 collagen Polymers 0.000 title claims abstract description 67
- 230000003020 moisturizing effect Effects 0.000 title claims abstract description 62
- 238000002360 preparation method Methods 0.000 title claims abstract description 27
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 24
- 238000001035 drying Methods 0.000 claims abstract description 19
- 238000000926 separation method Methods 0.000 claims abstract description 15
- 241000251468 Actinopterygii Species 0.000 claims description 45
- 239000000843 powder Substances 0.000 claims description 33
- 102000004190 Enzymes Human genes 0.000 claims description 29
- 108090000790 Enzymes Proteins 0.000 claims description 29
- 229940088598 enzyme Drugs 0.000 claims description 29
- 239000000463 material Substances 0.000 claims description 29
- 238000009777 vacuum freeze-drying Methods 0.000 claims description 24
- 238000003756 stirring Methods 0.000 claims description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 20
- 108090000145 Bacillolysin Proteins 0.000 claims description 16
- 102000035092 Neutral proteases Human genes 0.000 claims description 16
- 108091005507 Neutral proteases Proteins 0.000 claims description 16
- 108090000526 Papain Proteins 0.000 claims description 16
- 239000004365 Protease Substances 0.000 claims description 16
- 239000000706 filtrate Substances 0.000 claims description 16
- 238000010438 heat treatment Methods 0.000 claims description 16
- 235000019834 papain Nutrition 0.000 claims description 16
- 229940055729 papain Drugs 0.000 claims description 16
- 239000006228 supernatant Substances 0.000 claims description 14
- 239000007788 liquid Substances 0.000 claims description 13
- 229940054190 hydroxypropyl chitosan Drugs 0.000 claims description 12
- 102000004169 proteins and genes Human genes 0.000 claims description 12
- 108090000623 proteins and genes Proteins 0.000 claims description 12
- 241000209140 Triticum Species 0.000 claims description 11
- 235000021307 Triticum Nutrition 0.000 claims description 11
- 108010007119 flavourzyme Proteins 0.000 claims description 11
- 239000012528 membrane Substances 0.000 claims description 10
- 235000010489 acacia gum Nutrition 0.000 claims description 9
- 238000004140 cleaning Methods 0.000 claims description 8
- 239000011248 coating agent Substances 0.000 claims description 8
- 238000000576 coating method Methods 0.000 claims description 8
- 230000002255 enzymatic effect Effects 0.000 claims description 8
- 238000007710 freezing Methods 0.000 claims description 8
- 230000008014 freezing Effects 0.000 claims description 8
- 239000000413 hydrolysate Substances 0.000 claims description 8
- 238000002156 mixing Methods 0.000 claims description 8
- 238000007873 sieving Methods 0.000 claims description 8
- 239000007787 solid Substances 0.000 claims description 8
- 239000002352 surface water Substances 0.000 claims description 8
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 claims description 5
- 239000005913 Maltodextrin Substances 0.000 claims description 5
- 229920002774 Maltodextrin Polymers 0.000 claims description 5
- 239000001785 acacia senegal l. willd gum Substances 0.000 claims description 5
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 claims description 5
- 239000001768 carboxy methyl cellulose Substances 0.000 claims description 5
- 229940035034 maltodextrin Drugs 0.000 claims description 5
- 235000010413 sodium alginate Nutrition 0.000 claims description 5
- 239000000661 sodium alginate Substances 0.000 claims description 5
- 229940005550 sodium alginate Drugs 0.000 claims description 5
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 claims description 5
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 claims description 5
- 235000010493 xanthan gum Nutrition 0.000 claims description 5
- 239000000230 xanthan gum Substances 0.000 claims description 5
- 229920001285 xanthan gum Polymers 0.000 claims description 5
- 229940082509 xanthan gum Drugs 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims 6
- 230000003078 antioxidant effect Effects 0.000 abstract description 4
- 235000019658 bitter taste Nutrition 0.000 abstract description 4
- 239000000243 solution Substances 0.000 description 21
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 12
- 238000012360 testing method Methods 0.000 description 11
- 150000001875 compounds Chemical class 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 239000007864 aqueous solution Substances 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 6
- 235000017557 sodium bicarbonate Nutrition 0.000 description 6
- 238000003860 storage Methods 0.000 description 6
- HHEAADYXPMHMCT-UHFFFAOYSA-N dpph Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1[N]N(C=1C=CC=CC=1)C1=CC=CC=C1 HHEAADYXPMHMCT-UHFFFAOYSA-N 0.000 description 5
- 229920000084 Gum arabic Polymers 0.000 description 4
- 239000000205 acacia gum Substances 0.000 description 4
- MGJZITXUQXWAKY-UHFFFAOYSA-N diphenyl-(2,4,6-trinitrophenyl)iminoazanium Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1N=[N+](C=1C=CC=CC=1)C1=CC=CC=C1 MGJZITXUQXWAKY-UHFFFAOYSA-N 0.000 description 4
- 230000001376 precipitating effect Effects 0.000 description 4
- -1 DPPH free radical Chemical class 0.000 description 3
- 230000002292 Radical scavenging effect Effects 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 150000003254 radicals Chemical class 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000005187 foaming Methods 0.000 description 2
- 235000013373 food additive Nutrition 0.000 description 2
- 239000002778 food additive Substances 0.000 description 2
- 230000007760 free radical scavenging Effects 0.000 description 2
- 238000000034 method Methods 0.000 description 2
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- HUQKUJNSVHEHIH-UHFFFAOYSA-N 5,7-dihydroxy-4-phenylchromen-2-one Chemical compound C=1C(=O)OC2=CC(O)=CC(O)=C2C=1C1=CC=CC=C1 HUQKUJNSVHEHIH-UHFFFAOYSA-N 0.000 description 1
- 244000215068 Acacia senegal Species 0.000 description 1
- 101800000068 Antioxidant peptide Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- AFCARXCZXQIEQB-UHFFFAOYSA-N N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(CCNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 AFCARXCZXQIEQB-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004695 Polyether sulfone Substances 0.000 description 1
- SWDKDXWGADMDSP-UHFFFAOYSA-N Serratin Natural products C1C(=O)C23CCCN2CCCC23C1CC(C)(O)CC2O SWDKDXWGADMDSP-UHFFFAOYSA-N 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 230000003796 beauty Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 230000001804 emulsifying effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 210000004209 hair Anatomy 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 1
- 150000002576 ketones Chemical class 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 229930014626 natural product Natural products 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 229920006393 polyether sulfone Polymers 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 235000019640 taste Nutrition 0.000 description 1
Classifications
-
- 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]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- 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
-
- 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
-
- 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
- A61Q19/08—Anti-ageing preparations
-
- 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
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Dermatology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Toxicology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a moisturizing collagen active peptide and a preparation process thereof, wherein the preparation process of the moisturizing collagen active peptide comprises the following steps of (1) enzymolysis; (2) carrying out centrifugal separation; (3) ultrafiltration; (4) concentrating and drying. The moisturizing collagen active peptide and the preparation process have the advantages that the preparation process is simple, the obtained moisturizing collagen active peptide has good stability, good antioxidant activity and no bitter taste, is easy to absorb by a human body, and has high bioavailability and a good moisturizing effect on skin.
Description
Technical Field
The invention relates to a collagen active peptide with a moisturizing effect and a preparation process thereof, belonging to the technical field of biochemistry.
Background
Today, the national economic level is continuously improved, people pay more attention to the quality of life and personal body quality. The collagen peptide product is increasingly applied to various skin care, medicines and foods due to good functions of water replenishing, water locking, oxidation resistance, tumor resistance, foaming property and the like.
Collagen is a fibrous protein widely present in bones, skin, hair and blood vessels of animals, and mainly plays a role in supporting, maintaining and repairing the body. The main constituent substances of collagen are amino acids, which are hydrolyzed to produce collagen peptides and amino acids as byproducts. Collagen peptides are more soluble than collagen due to their smaller molecular weight. At a concentration of 50%, the collagen peptide still has no turbidity and has very low viscosity. In addition, at ordinary pH, its solubility is enhanced.
The collagen peptide is prepared by hydrolyzing collagen, a large number of hydrophilic groups are exposed outside, and the water absorption performance and the water locking performance of the collagen peptide are much stronger than those of the collagen. Therefore, the collagen peptide is widely applied to skin care products, and mainly has the effects of locking the moisture of the skin and replenishing water. Collagen peptides are also often used extensively in food cooking as food additives, primarily due to their emulsifying and foaming properties. The product prepared in this way not only has good taste, but also has higher nutritional value.
With the increase of economic level, people will spend more money for beauty care, skin care, aging delay and healthy body. Collagen peptide is widely used in today's foods, skin care products and medicines with its unique efficacy.
However, the existing collagen peptide is mostly prepared by an enzyme extraction method, and during the enzymolysis process, fishy smell substances such as bitter peptide, volatile aldehyde and ketone are easily generated, so that the product is accompanied with strong fishy smell and bitter taste and has poor stability, and the use of the collagen peptide is limited.
Disclosure of Invention
The invention aims to solve the problem of providing the moisturizing collagen active peptide and the preparation process thereof, the preparation process is simple, the obtained moisturizing collagen active peptide has good stability, good antioxidant activity, no bitter taste, high bioavailability and good moisturizing effect on skin, and is beneficial to human body absorption.
A preparation process of collagen active peptide with moisturizing effect comprises the following steps:
(1) carrying out enzymolysis;
(2) carrying out centrifugal separation;
(3) ultrafiltration;
(4) concentrating and drying.
Preferably, the preparation process of the collagen active peptide with moisturizing effect comprises the following steps:
(1) carrying out enzymolysis;
(2) high-pressure micro-jet treatment;
(3) carrying out centrifugal separation;
(4) ultrafiltration;
(5) concentrating and drying.
Preferably, the preparation process of the collagen active peptide with moisturizing effect comprises the following steps:
(1) carrying out enzymolysis;
(2) high-pressure micro-jet treatment;
(3) carrying out centrifugal separation;
(4) ultrafiltration;
(5) concentrating and drying;
(6) and (4) coating.
Preferably, the preparation process of the collagen active peptide with moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 40-80 mesh sieve to obtain fish skin coarse powder, adding water which is 1-3 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 50-55 ℃, adjusting the pH to 7.0-7.5, adding complex enzyme which is 0.1-1% of the weight of the fish skin coarse powder, stirring for 3-6 hours at 50-55 ℃ at 200 revolutions per minute of 100 and one second, and keeping the temperature for 5-10 minutes at 95-100 ℃ to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure micro-jet treatment on the enzymolysis liquid, wherein the circulation frequency is 1-3 times, the circulation pressure is 100-;
(3) centrifugal separation: centrifuging the treatment solution at 3000-;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.1-0.2MPa and temperature of 35-45 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 45-55 deg.C under vacuum degree of 0.05-0.1MPa to obtain concentrated solution with solid content of 45-55%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 5-10g of inner wall material into 100mL of water, stirring for 10-20 minutes at the temperature of 35-45 ℃ at 200-.
The inner wall material is one or a mixture of more of maltodextrin, sodium carboxymethylcellulose, wheat protein and hydroxypropyl chitosan.
The outer wall material is one of xanthan gum, Arabic gum and sodium alginate.
Preferably, the inner wall material is wheat protein and/or hydroxypropyl chitosan.
More preferably, the inner wall material is a mixture of wheat protein and hydroxypropyl chitosan, and the mass ratio of the wheat protein to the hydroxypropyl chitosan is 1: (8-10).
Preferably, the outer wall material is gum arabic.
The vacuum freeze drying conditions in the step (5) are as follows: placing the concentrated solution in a culture dish with a thickness of 5-10 mm, freezing in a refrigerator at-68 deg.C for 3-6 hr, vacuum freeze-drying under 60-100Pa for 15-20 hr, and heating at 40 deg.C to obtain active peptide.
Preferably, the compound enzyme is papain, neutral protease and flavourzyme in a mass ratio of (1-3): (1-3): (1-3).
Preferably, the fish skin is Wuchang fish skin.
A collagen active peptide with moisturizing effect is prepared by any one of the preparation processes.
The moisturizing collagen active peptide and the preparation process have the advantages that the preparation process is simple, the obtained moisturizing collagen active peptide has good stability, good antioxidant activity and no bitter taste, is easy to absorb by a human body, and has high bioavailability and a good moisturizing effect on skin.
Detailed Description
The invention is further illustrated below with reference to specific examples. It is to be understood, however, that these examples are illustrative only and are not to be construed as limiting the scope of the present invention. Test methods in which specific conditions are not specified in the following examples are generally carried out under conventional conditions or under conditions recommended by the manufacturer.
And (3) measuring the yield of the nano active peptide: the moisturizing effect collagen active peptides and the fish skin meal in examples 1-2 were weighed, and the yield was calculated as follows:
in the formula, m1Mass m of the moisturizing collagen active peptide obtained in the examples0Is the quality of the fishskin coarse powder. Each set of tests was repeated 3 times and averaged.
DPPH free radical clearance rate test of moisturizing effect collagen active peptide: weighing 2 parts of the moisturizing effect collagen active peptide in example 2, wherein each part is 1.0g, measuring one part of the moisturizing effect collagen active peptide to remove DPPH free radicals, weighing 1.0g of the moisturizing effect collagen active peptide in example 3-9 and comparative example 1, packaging the other part of the moisturizing effect collagen active peptide in example 2 by using a transparent plastic self-sealing bag, storing the packaged product at 25 ℃ for 30 days, grinding and breaking the walls, and measuring the removal of DPPH free radicals according to 'super-biological pre-treatment rice protein preparation antioxidant peptide' of Jiajunqiang, Mahalane and the like; each set of tests was repeated 3 times and averaged.
And the ultrafiltration membrane adopts a polyether sulfone membrane with the molecular weight cutoff of 3000 Da.
The fish skin, in the embodiment, fresh Wuchang fish skin is adopted, cleaned and purified for standby.
The maltodextrin is pharmaceutical grade maltodextrin produced by Xuzhou city high-voyage food additive company Limited.
The sodium carboxymethylcellulose is pharmaceutical grade sodium carboxymethylcellulose produced by Changzhou ocean Sen Biotechnology limited.
The wheat protein is food-grade wheat protein produced by Shaanxi Senfu natural products Co.
Hydroxypropyl chitosan is pharmaceutical grade hydroxypropyl chitosan produced by Sienna Ricini Biotechnology limited.
Xanthan gum, medicinal xanthan gum produced by Beijing Jinluhong biotechnology limited.
Acacia gum, pharmaceutical grade acacia gum produced by Tongyu chemical Co., Ltd, Dongguang county.
The sodium alginate is food-grade sodium alginate produced by Wuhan Baixing Biotech limited company.
The papain is food-grade papain produced by Biotech Limited of Henghuadao, Nanjing, with enzyme activity of 30000U/g.
The neutral protease is also named as Serratin peptidase, and is food-grade neutral protease produced by Biotech Limited in Henghua, Nanjing, and has enzyme activity of 30000U/g.
The flavourzyme adopts food-grade flavourzyme produced by Biotech Limited company of Henghuadao of Nanjing, and the enzyme activity is 30000U/g.
Example 1
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) centrifugal separation: centrifuging the enzymolysis solution at 4000 rpm for 15 min, and collecting supernatant;
(3) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(4) concentrating and drying: and (3) concentrating the filtrate under reduced pressure at 50 ℃ and under the vacuum degree of 0.06MPa to obtain a concentrated solution with the solid content of 50%, and then carrying out vacuum freeze drying to obtain the collagen active peptide with the moisturizing effect.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the collagen active peptide with the moisturizing effect.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
Example 2
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure microjet treatment on the enzymolysis liquid, wherein the circulation frequency is 2 times, the circulation pressure is 120MPa, and the feeding temperature is 50 ℃ to obtain a treatment liquid;
(3) centrifugal separation: centrifuging the treated solution at 4000 rpm for 15 minutes, and collecting the supernatant;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(5) concentrating and drying: and (3) concentrating the filtrate under reduced pressure at 50 ℃ and under the vacuum degree of 0.06MPa to obtain a concentrated solution with the solid content of 50%, and then carrying out vacuum freeze drying to obtain the collagen active peptide with the moisturizing effect.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the collagen active peptide with the moisturizing effect.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
Test example 1
The yield of the collagen-active peptide having moisturizing effect obtained in example 1-2 was measured, and the results are shown in table 1.
TABLE 1 test results of yield table
Example 2 the yield of the collagen active peptide with the moisturizing effect is obviously improved by treating the enzymolysis liquid with high-pressure micro-jet. This is because the high pressure microjet treatment can cause cleavage of the collagen peptide chain, thereby increasing product yield.
Example 3
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure microjet treatment on the enzymolysis liquid, wherein the circulation frequency is 2 times, the circulation pressure is 120MPa, and the feeding temperature is 50 ℃ to obtain a treatment liquid;
(3) centrifugal separation: centrifuging the treated solution at 4000 rpm for 15 minutes, and collecting the supernatant;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 50 deg.C under vacuum degree of 0.06MPa to obtain concentrated solution with solid content of 50%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 8g of inner wall material into 100mL of water, stirring for 15 minutes at 40 ℃ at 300 rpm, adding 2g of active peptide, stirring for 35 minutes at 40 ℃ at 150 rpm, adding 0.6g of outer wall material, stirring for 100 minutes at 40 ℃ at 150 rpm, standing for 18 hours at 4 ℃, centrifuging for 15 minutes at 4000 rpm, and precipitating and drying for 25 hours at 50 ℃ to obtain the collagen active peptide with moisturizing effect.
The inner wall material is maltodextrin.
The outer wall material is xanthan gum.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the active peptide.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
Example 4
Essentially the same as example 3, except that: the outer wall material is Arabic gum.
Example 5
Essentially the same as example 3, except that: the outer wall material is sodium alginate.
Test example 2
The results of the test on the DPPH radical scavenging effect of the moisturizing collagen active peptides obtained in examples 2 to 5 are as follows:
TABLE 2 table of results of DPPH radical scavenging test
| DPPH radical clearance% | |
| Example 2 (storage 0 days) | 86.67 |
| Example 2 (storage for 30 days) | 44.16 |
| Example 3 (storage for 30 days) | 75.62 |
| Example 4 (storage for 30 days) | 77.96 |
| Example 5 (storage for 30 days) | 76.29 |
Examples 3-5, in which the active peptide was coated, showed significantly better antioxidant activity after 30 days storage than example 2 (uncoated), and example 4, in which acacia gum was used as the outer wall material, showed the least decrease in DPPH radical scavenging rate.
Example 6
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure microjet treatment on the enzymolysis liquid, wherein the circulation frequency is 2 times, the circulation pressure is 120MPa, and the feeding temperature is 50 ℃ to obtain a treatment liquid;
(3) centrifugal separation: centrifuging the treated solution at 4000 rpm for 15 minutes, and collecting the supernatant;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 50 deg.C under vacuum degree of 0.06MPa to obtain concentrated solution with solid content of 50%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 8g of inner wall material into 100mL of water, stirring for 15 minutes at 40 ℃ at 300 rpm, adding 2g of active peptide, stirring for 35 minutes at 40 ℃ at 150 rpm, adding 0.6g of outer wall material, stirring for 100 minutes at 40 ℃ at 150 rpm, standing for 18 hours at 4 ℃, centrifuging for 15 minutes at 4000 rpm, and precipitating and drying for 25 hours at 50 ℃ to obtain the collagen active peptide with moisturizing effect.
The inner wall material is sodium carboxymethyl cellulose.
The outer wall material is Arabic gum.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the active peptide.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
The DPPH free radical clearance rate of the obtained collagen active peptide with the moisturizing effect after being stored for 30 days is 78.33%.
Example 7
Essentially the same as example 6, except that: the inner wall material is wheat protein.
The obtained collagen active peptide with moisturizing effect has DPPH free radical scavenging rate of 80.37% after being stored for 30 days
Example 8
Essentially the same as example 6, except that: the inner wall material is hydroxypropyl chitosan.
The obtained collagen active peptide with moisturizing effect has DPPH free radical scavenging rate of 80.81% after being stored for 30 days
Comparative example 1
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure microjet treatment on the enzymolysis liquid, wherein the circulation frequency is 2 times, the circulation pressure is 120MPa, and the feeding temperature is 50 ℃ to obtain a treatment liquid;
(3) centrifugal separation: centrifuging the treated solution at 4000 rpm for 15 minutes, and collecting the supernatant;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 50 deg.C under vacuum degree of 0.06MPa to obtain concentrated solution with solid content of 50%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 8g of inner wall material into 100mL of water, stirring for 15 minutes at 40 ℃ at 300 rpm, adding 2g of active peptide, stirring for 135 minutes at 40 ℃ at 150 rpm, standing for 18 hours at 4 ℃, centrifuging for 15 minutes at 4000 rpm, and precipitating at 50 ℃ for drying for 25 hours to obtain the collagen active peptide with the moisturizing effect.
The inner wall material is hydroxypropyl chitosan.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the active peptide.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
The clearance rate of DPPH free radicals after the collagen active peptide with the moisturizing effect is stored for 30 days is 66.74%.
Example 9
The preparation process of the collagen active peptide with the moisturizing effect comprises the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 60-mesh sieve to obtain fish skin coarse powder, adding water 2 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 52 ℃, adjusting the pH to 7.2 by using a sodium bicarbonate aqueous solution with the mass fraction of 5%, adding a complex enzyme 0.5% of the weight of the fish skin coarse powder, stirring at the temperature of 52 ℃ at 150 revolutions per minute for 4 hours, and keeping the temperature at 98 ℃ for 8 minutes to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure microjet treatment on the enzymolysis liquid, wherein the circulation frequency is 2 times, the circulation pressure is 120MPa, and the feeding temperature is 50 ℃ to obtain a treatment liquid;
(3) centrifugal separation: centrifuging the treated solution at 4000 rpm for 15 minutes, and collecting the supernatant;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.15MPa and temperature of 40 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 50 deg.C under vacuum degree of 0.06MPa to obtain concentrated solution with solid content of 50%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 8g of inner wall material into 100mL of water, stirring for 15 minutes at 40 ℃ at 300 rpm, adding 2g of active peptide, stirring for 35 minutes at 40 ℃ at 150 rpm, adding 0.6g of outer wall material, stirring for 100 minutes at 40 ℃ at 150 rpm, standing for 18 hours at 4 ℃, centrifuging for 15 minutes at 4000 rpm, and precipitating and drying for 25 hours at 50 ℃ to obtain the collagen active peptide with moisturizing effect.
The inner wall material is a mixture of wheat protein and hydroxypropyl chitosan, and the mass ratio of the wheat protein to the hydroxypropyl chitosan is 1: 9.
the outer wall material is Arabic gum.
The vacuum freeze-drying conditions are as follows: placing the concentrated solution in a culture dish, wherein the thickness is 8 mm, freezing in a refrigerator at-68 ℃ for 4 hours, then carrying out vacuum freeze drying under the vacuum condition of 80Pa for 18 hours, and heating the plate at the temperature of 40 ℃ to obtain the active peptide.
The compound enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the papain to the neutral protease is 1: 1: 1.
The obtained collagen active peptide with moisturizing effect has a DPPH free radical clearance rate of 83.72%.
Test example 3
The moisturizing effects of the moisturizing efficacy collagen-active peptides obtained in examples 3 to 9 were tested.
The test method comprises the following steps: 210 healthy women 25-35 years old, whose skins are dry and randomly divided into 7 groups, 30 persons in each group were administered with the collagen active peptide having moisturizing effect of examples 3-9 once a day, 5g each time, dissolved in warm water at 80 ℃ and administered for 90 days.
And (4) testing standard:
the effect is shown: the skin is obviously improved, fine wrinkles are obviously reduced, and the skin is kept moist.
The method has the following advantages: the skin is improved, fine wrinkles are reduced, and the skin is kept relatively moist.
And (4) invalidation: the skin condition did not improve at all.
Table 3 moisturizing effect test results table
| Show effect | Is effective | Invalidation | |
| Example 3 | 19 | 11 | 0 |
| Example 4 | 21 | 9 | 0 |
| Example 5 | 20 | 10 | 0 |
| Example 6 | 22 | 8 | 0 |
| Example 7 | 24 | 6 | 0 |
| Example 8 | 24 | 6 | 0 |
| Example 9 | 27 | 3 | 0 |
Claims (10)
1. A preparation process of collagen active peptide with moisturizing effect is characterized by comprising the following steps:
(1) carrying out enzymolysis;
(2) carrying out centrifugal separation;
(3) ultrafiltration;
(4) concentrating and drying.
2. The process for preparing collagen-active peptide with moisturizing effect according to claim 1, comprising the following steps:
(1) carrying out enzymolysis;
(2) high-pressure micro-jet treatment;
(3) carrying out centrifugal separation;
(4) ultrafiltration;
(5) concentrating and drying.
3. The process for preparing collagen-active peptide with moisturizing effect according to claim 2, comprising the following steps:
(1) carrying out enzymolysis;
(2) high-pressure micro-jet treatment;
(3) carrying out centrifugal separation;
(4) ultrafiltration;
(5) concentrating and drying;
(6) and (4) coating.
4. The process for preparing collagen-active peptide with moisturizing effect according to claim 3, comprising the following steps:
(1) enzymolysis: cleaning fish skin, draining surface water, crushing, sieving with a 40-80 mesh sieve to obtain fish skin coarse powder, adding water which is 1-3 times of the weight of the fish skin coarse powder into the fish skin coarse powder, uniformly mixing, heating to 50-55 ℃, adjusting the pH to 7.0-7.5, adding complex enzyme which is 0.1-1% of the weight of the fish skin coarse powder, stirring for 3-6 hours at 50-55 ℃ at 200 revolutions per minute of 100 and one second, and keeping the temperature for 5-10 minutes at 95-100 ℃ to inactivate the enzyme to obtain an enzymatic hydrolysate;
(2) high-pressure micro-jet treatment: carrying out high-pressure micro-jet treatment on the enzymolysis liquid, wherein the circulation frequency is 1-3 times, the circulation pressure is 100-;
(3) centrifugal separation: centrifuging the treatment solution at 3000-;
(4) and (3) ultrafiltration: ultrafiltering the supernatant with membrane with molecular weight cutoff of 3000Da at ultrafiltration pressure of 0.1-0.2MPa and temperature of 35-45 deg.C to obtain filtrate;
(5) concentrating and drying: concentrating the filtrate at 45-55 deg.C under vacuum degree of 0.05-0.1MPa to obtain concentrated solution with solid content of 45-55%, and vacuum freeze drying to obtain active peptide;
(6) coating: adding 5-10g of inner wall material into 100mL of water, stirring for 10-20 minutes at the temperature of 35-45 ℃ at 200-.
5. The preparation process of the collagen active peptide with moisturizing effect as claimed in claim 4, wherein the inner wall material is one or more of maltodextrin, sodium carboxymethylcellulose, wheat protein and hydroxypropyl chitosan.
6. The process for preparing collagen-active peptide with moisturizing effect according to claim 5, wherein the inner wall material is wheat protein and/or hydroxypropyl chitosan.
7. The process for preparing collagen-active peptide with moisturizing effect according to claim 4, wherein the outer wall material is one of xanthan gum, arabic gum and sodium alginate.
8. The process for preparing collagen active peptide with moisturizing effect according to claim 4, wherein the vacuum freeze-drying conditions in step (5) are as follows: placing the concentrated solution in a culture dish with a thickness of 5-10 mm, freezing in a refrigerator at-68 deg.C for 3-6 hr, vacuum freeze-drying under 60-100Pa for 15-20 hr, and heating at 40 deg.C to obtain active peptide.
9. The preparation process of the collagen active peptide with moisturizing effect according to claim 4, wherein the complex enzyme is papain, neutral protease and flavourzyme, and the mass ratio of the complex enzyme to the flavourzyme is (1-3): (1-3): (1-3).
10. A collagen active peptide with moisturizing effect, which is prepared by the preparation process of any one of claims 1 to 9.
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115211569A (en) * | 2022-08-01 | 2022-10-21 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide food with antioxidant function |
| CN115820779A (en) * | 2023-02-17 | 2023-03-21 | 瑞吉明(山东)生物科技有限公司 | Fish skin collagen and preparation method thereof |
Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101323850A (en) * | 2008-07-28 | 2008-12-17 | 天津科技大学 | Lactobacillus helveticus microcapsule, preparation and use thereof |
| CN102511854A (en) * | 2011-12-26 | 2012-06-27 | 山东好当家海洋发展股份有限公司 | Collagen polypeptide drink and its preparation method |
| CN103981170A (en) * | 2014-05-09 | 2014-08-13 | 陕西科技大学 | Method for preparing lactobacillus acidophilus microcapsules by using xanthan gum / chitosan / xanthan gum and application thereof |
| CN106191189A (en) * | 2016-09-20 | 2016-12-07 | 武汉百思凯瑞纳米科技有限公司 | A kind of preparation method and applications of tuna skin height moisturizing bioactive peptide |
| CN109457005A (en) * | 2018-11-23 | 2019-03-12 | 胜田(福清)食品有限公司 | A kind of substep efficiently prepares the preparation method of sea cucumber internal organ anti-oxidation peptide |
| CN110144376A (en) * | 2019-06-05 | 2019-08-20 | 杭州柏淼生物科技有限公司 | Nanoscale collagen peptide and preparation method thereof |
| CN111574618A (en) * | 2020-06-26 | 2020-08-25 | 润科生物工程（福建）有限公司 | Preparation method of whitening compound protein peptidase hydrolysate, whitening compound protein peptide beverage and preparation method thereof |
| CN111643389A (en) * | 2020-06-04 | 2020-09-11 | 张雯雯 | Anti-wrinkle whitening repair mask containing marine bioactive peptide and preparation method thereof |
-
2020
- 2020-12-07 CN CN202011416724.6A patent/CN112521489B8/en active Active
Patent Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101323850A (en) * | 2008-07-28 | 2008-12-17 | 天津科技大学 | Lactobacillus helveticus microcapsule, preparation and use thereof |
| CN102511854A (en) * | 2011-12-26 | 2012-06-27 | 山东好当家海洋发展股份有限公司 | Collagen polypeptide drink and its preparation method |
| CN103981170A (en) * | 2014-05-09 | 2014-08-13 | 陕西科技大学 | Method for preparing lactobacillus acidophilus microcapsules by using xanthan gum / chitosan / xanthan gum and application thereof |
| CN106191189A (en) * | 2016-09-20 | 2016-12-07 | 武汉百思凯瑞纳米科技有限公司 | A kind of preparation method and applications of tuna skin height moisturizing bioactive peptide |
| CN109457005A (en) * | 2018-11-23 | 2019-03-12 | 胜田(福清)食品有限公司 | A kind of substep efficiently prepares the preparation method of sea cucumber internal organ anti-oxidation peptide |
| CN110144376A (en) * | 2019-06-05 | 2019-08-20 | 杭州柏淼生物科技有限公司 | Nanoscale collagen peptide and preparation method thereof |
| CN111643389A (en) * | 2020-06-04 | 2020-09-11 | 张雯雯 | Anti-wrinkle whitening repair mask containing marine bioactive peptide and preparation method thereof |
| CN111574618A (en) * | 2020-06-26 | 2020-08-25 | 润科生物工程（福建）有限公司 | Preparation method of whitening compound protein peptidase hydrolysate, whitening compound protein peptide beverage and preparation method thereof |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115211569A (en) * | 2022-08-01 | 2022-10-21 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide food with antioxidant function |
| CN115820779A (en) * | 2023-02-17 | 2023-03-21 | 瑞吉明(山东)生物科技有限公司 | Fish skin collagen and preparation method thereof |
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Correction item: Patentee|Address|Patent agency|Patent Agent Correct: Harbin Hayi Jizheng Pharmaceutical Technology Development Co.,Ltd.|150000 the second and third floors of Building 1, No.8, Tongjiang Road, concentrated area, haping Road, economic development zone, Harbin City, Heilongjiang Province|Beijing Huijie Intellectual Property Agency (General Partnership) 11531|Ge Baocai False: Wuhan Textile University |430073 No. 1 Textile Road, Hongshan District, Wuhan City, Hubei Province|Wuhan Taishan Beidou Patent Agency Office (special general partnership) 42250|Dong Jiajia Number: 48-01 Page: The title page Volume: 38 Correction item: Patentee|Address|Patent agency|Patent Agent Correct: Harbin Hayi Jizheng Pharmaceutical Technology Development Co.,Ltd.|150000 the second and third floors of Building 1, No.8, Tongjiang Road, concentrated area, haping Road, economic development zone, Harbin City, Heilongjiang Province|Beijing Huijie Intellectual Property Agency (General Partnership) 11531|Ge Baocai False: Wuhan Textile University |430073 No. 1 Textile Road, Hongshan District, Wuhan City, Hubei Province|Wuhan Taishan Beidou Patent Agency Office (special general partnership) 42250|Dong Jiajia Volume: 38 |
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