CN114106151A - Preparation method of antioxidant active collagen peptide - Google Patents
Preparation method of antioxidant active collagen peptide Download PDFInfo
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- CN114106151A CN114106151A CN202111510111.3A CN202111510111A CN114106151A CN 114106151 A CN114106151 A CN 114106151A CN 202111510111 A CN202111510111 A CN 202111510111A CN 114106151 A CN114106151 A CN 114106151A
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- 102000008186 Collagen Human genes 0.000 title claims abstract description 50
- 108010035532 Collagen Proteins 0.000 title claims abstract description 50
- 229920001436 collagen Polymers 0.000 title claims abstract description 50
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 39
- 230000003078 antioxidant effect Effects 0.000 title claims abstract description 21
- 239000003963 antioxidant agent Substances 0.000 title claims abstract description 11
- 238000002360 preparation method Methods 0.000 title claims abstract description 9
- 241001465754 Metazoa Species 0.000 claims abstract description 32
- 238000000034 method Methods 0.000 claims abstract description 24
- 239000003480 eluent Substances 0.000 claims abstract description 22
- 238000004140 cleaning Methods 0.000 claims abstract description 21
- 210000000988 bone and bone Anatomy 0.000 claims abstract description 18
- 238000002791 soaking Methods 0.000 claims abstract description 17
- 238000005406 washing Methods 0.000 claims abstract description 16
- 108090000790 Enzymes Proteins 0.000 claims abstract description 11
- 102000004190 Enzymes Human genes 0.000 claims abstract description 11
- 239000006228 supernatant Substances 0.000 claims abstract description 10
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 7
- 238000004537 pulping Methods 0.000 claims abstract description 7
- 239000003513 alkali Substances 0.000 claims abstract description 5
- 238000005520 cutting process Methods 0.000 claims abstract description 5
- 238000005238 degreasing Methods 0.000 claims abstract description 5
- 238000010828 elution Methods 0.000 claims abstract description 5
- 238000000605 extraction Methods 0.000 claims abstract description 5
- 238000000926 separation method Methods 0.000 claims abstract description 5
- 230000008569 process Effects 0.000 claims abstract description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 28
- 238000001035 drying Methods 0.000 claims description 16
- 230000007935 neutral effect Effects 0.000 claims description 16
- 239000004365 Protease Substances 0.000 claims description 13
- 229940088598 enzyme Drugs 0.000 claims description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 8
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 8
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 8
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 8
- 108010004032 Bromelains Proteins 0.000 claims description 6
- 108090000526 Papain Proteins 0.000 claims description 6
- 102000004142 Trypsin Human genes 0.000 claims description 6
- 108090000631 Trypsin Proteins 0.000 claims description 6
- 235000019835 bromelain Nutrition 0.000 claims description 6
- 238000010438 heat treatment Methods 0.000 claims description 6
- 235000019834 papain Nutrition 0.000 claims description 6
- 229940055729 papain Drugs 0.000 claims description 6
- 239000012588 trypsin Substances 0.000 claims description 6
- 208000007536 Thrombosis Diseases 0.000 claims description 4
- 239000007853 buffer solution Substances 0.000 claims description 4
- 239000000843 powder Substances 0.000 claims description 3
- 230000003064 anti-oxidating effect Effects 0.000 claims 1
- 150000001875 compounds Chemical class 0.000 claims 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 abstract description 4
- 235000013305 food Nutrition 0.000 abstract description 4
- 235000013373 food additive Nutrition 0.000 abstract description 3
- 239000002778 food additive Substances 0.000 abstract description 3
- -1 hydroxyl free radical Chemical class 0.000 abstract description 3
- 210000003491 skin Anatomy 0.000 description 14
- 101800000068 Antioxidant peptide Proteins 0.000 description 6
- 239000010985 leather Substances 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- TUJKJAMUKRIRHC-UHFFFAOYSA-N hydroxyl Chemical compound [OH] TUJKJAMUKRIRHC-UHFFFAOYSA-N 0.000 description 2
- 235000013372 meat Nutrition 0.000 description 2
- 239000012567 medical material Substances 0.000 description 2
- 229940127554 medical product Drugs 0.000 description 2
- 230000003020 moisturizing effect Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 150000003254 radicals Chemical class 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 230000008439 repair process Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 235000017060 Arachis glabrata Nutrition 0.000 description 1
- 244000105624 Arachis hypogaea Species 0.000 description 1
- 235000010777 Arachis hypogaea Nutrition 0.000 description 1
- 235000018262 Arachis monticola Nutrition 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 210000004087 cornea Anatomy 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 235000011194 food seasoning agent Nutrition 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 235000020232 peanut Nutrition 0.000 description 1
- 238000005502 peroxidation Methods 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
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
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- 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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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
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Abstract
The invention discloses a preparation method of antioxidant active collagen peptide, which comprises the following steps: the method comprises the following steps: pre-extraction: cleaning animal skin or bone, cutting into pieces, soaking in alkali liquor for degreasing, cleaning, pulping, centrifuging, and collecting supernatant; step two: performing enzymolysis on a column: introducing the supernatant obtained in the step one into a hydrophobic chromatographic column, adsorbing, washing the chromatographic column by using eluent containing complex enzyme, and performing enzymolysis on collagen; step three: elution and separation: eluting the collagen peptide on the chromatographic column in the second step by using an eluent, and collecting the eluent; the antioxidant activity is high, the clearance rate of the prepared collagen peptide hydroxyl free radical is higher than 90%, and the clearance rate of superoxide anion is higher than 86%; the used enzymes belong to food additives allowed by the nation, and can be used in the food industry without treatment; stable process, simple operation, standardized equipment, low cost and convenient popularization and application.
Description
Technical Field
The invention belongs to the technical field of food processing, and particularly relates to a preparation method of an antioxidant active collagen peptide.
Background
The collagen is mainly present in the connective tissues of animals, the collagen content in mammals accounts for about 25-30% of the total protein, and the collagen content in some marine animals is higher and can reach more than 80%, so that the collagen is the functional protein which is most widely distributed and has the most content.
Collagen has wide application in food additive, seasoning, food packing material, etc. and the direct addition of collagen powder into meat can change the tenderness of meat. The collagen has low antigenicity, biocompatibility, repairability and biodegradability, and is an ideal natural macromolecular medical material. According to the characteristics of the collagen and the medical materials, medical products with biological characteristics are developed, such as the medical products which can be used for wound healing and burn repair, cornea repair and the like. Collagen, as a structural protein, is usually added to cosmetics to enhance the moisturizing and moisturizing properties of skin care products. The collagen and a small amount of elastin form a network fiber to convey moisture to the epidermis, so that the skin has certain elasticity and moisture.
The antioxidant peptide is a peptide with the functions of inhibiting the peroxidation of biological macromolecules and removing free radicals in vivo. Researches show that some animal and plant raw materials can generate antioxidant peptides after being hydrolyzed by protease, such as soybean peptide, peanut peptide, corn peptide, yak skin collagen antioxidant peptide, tuna antioxidant peptide, sheep bone antioxidant peptide and the like.
Disclosure of Invention
The present invention aims at providing the preparation method of the collagen peptide with antioxidant activity to solve the problems in the background technology.
In order to achieve the purpose, the invention provides the following technical scheme: a preparation method of an antioxidant active collagen peptide specifically comprises the following steps:
the method comprises the following steps: pre-extraction: cleaning animal skin or bone, cutting into pieces, soaking in alkali liquor for degreasing, cleaning, pulping, centrifuging, and collecting supernatant;
step two: performing enzymolysis on a column: introducing the supernatant obtained in the step one into a hydrophobic chromatographic column, adsorbing, washing the chromatographic column by using eluent containing complex enzyme, and performing enzymolysis on collagen;
step three: elution and separation: eluting the collagen peptide on the chromatographic column in the second step by using an eluent, and collecting the eluent;
step four: concentrating and drying: concentrating and drying the eluent in the third step to obtain dried powder, namely the antioxidant active collagen peptide.
As a preferable technical scheme of the invention, in the first step, the water adding amount is 10-15 times of the weight of the animal skin or bone in the pulping process, and the pH value is 11-14.
As a preferred technical scheme of the invention, the complex enzyme used in the second step is trypsin, papain and bromelain, the enzyme adding amount is 1-3% of the weight of the animal skin or bone, and the weight ratio of trypsin: papain: the bromelain is 5-8: 4-8: 3 to 5.
In a preferred embodiment of the present invention, the eluent used in the second step is an ammonium sulfate buffer solution with a pH of 7-9 and a concentration of 0.5-2 mol/L, and the flow rate is 0.1-5 ml/min.
In a preferred embodiment of the present invention, the eluent used in the third step is a buffer solution containing 0.1-0.2M ammonium sulfate at a pH of 7-9, and the flow rate is 0.1-5 ml/min.
In a preferred embodiment of the present invention, the step of washing the skin or bone of the animal in the step one is as follows:
the cleaning method of the animal skin comprises the following steps:
s1: removing damage and spots on the surface of the animal skin, and soaking the animal skin in high-temperature water for 5-20 min at the water temperature of 90-100 ℃;
s2: unhairing animal skins through unhairing equipment;
s3: soaking the unhaired animal skin in pH 6.5-7.5, and adding edible alcohol at a ratio of 9-13 KG/g for 20-25 min;
s4: fishing out, and soaking again in a pH of 6.5-7.5 for 15-20 min;
s5: taking out and drying.
The cleaning method of the animal bone comprises the following steps:
a1: removing blood clots on the surface of the animal bone, and washing with neutral water with the pH of 6.5-7.5 for 1.5-3 min;
a2: putting the animal bones into neutral water with the pH value of 6.5-7.5, and heating the neutral water to 60-75 ℃ at the heating rate of 10-15 ℃/min;
a3: fishing out the animal bones treated in the step A2, and washing with neutral water with the pH value of 6.5-7.5 for 1.5-2 min;
a4: taking out and drying.
As a preferable technical solution of the present invention, in S2, the unhairing device comprises tweezers, a spatula; in S3, the degree of the edible alcohol is 45-50 degrees.
Compared with the prior art, the invention has the beneficial effects that:
1. the antioxidant activity is high, the clearance rate of the prepared collagen peptide hydroxyl free radical is higher than 90%, and the clearance rate of superoxide anion is higher than 86%;
2. the used enzymes belong to food additives allowed by the nation, and can be used in the food industry without treatment;
3. the process is stable, the operation is simple and convenient, the equipment is standardized, the cost is low, and the popularization and the application are convenient;
4. through a special cleaning mode, stains can not exist on the surface and inside of the raw materials, and the quality of finished products at the later stage is not influenced.
Detailed Description
The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the embodiments of the present invention, and it is obvious that the described embodiments are only a part of the embodiments of the present invention, and not all of the embodiments. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
Example 1
The invention provides a technical scheme that: a preparation method of an antioxidant active collagen peptide specifically comprises the following steps:
the method comprises the following steps: pre-extraction: cleaning 10kg of cow leather, cutting into pieces, soaking in alkali liquor for degreasing, cleaning, adding 100kg of water with the pH value of 12, pulping, centrifuging, and taking supernatant;
step two: performing enzymolysis on a column: introducing the supernatant obtained in the first step into a butyl hydrophobic chromatographic column, adsorbing, washing the chromatographic column with eluent containing 100g of complex enzyme (trypsin: papain: bromelain 5: 4: 3) and 0.5M ammonium sulfate in pH7 at a flow rate of 1ml/min, and performing enzymolysis on collagen;
step three: elution and separation: eluting the collagen peptide on the chromatographic column in the second step by using eluent with pH7 and 0.1M ammonium sulfate, wherein the flow rate is 2ml/min, and collecting the eluent;
step four: concentrating and drying: concentrating and drying the eluent in the third step to obtain the antioxidant active collagen peptide, wherein the hydroxyl radical clearance rate of the prepared collagen peptide is 96.3 percent and the superoxide anion clearance rate is 87.8 percent through detection.
When the sequence of the antioxidant peptide contains hydrophobic amino acids such as Leu, Tyr, Val, Ala, Leu, Met, Phe and the like, the solubility of fat can be increased, the hydrophobic amino acids interact with free radicals, and the antioxidant activity of the polypeptide is enhanced.
In this example, the cleaning of the cow leather in the first step was as follows:
the cleaning method of the cow leather comprises the following steps:
s1: removing damage and spots on the surface of the cowhide, and soaking the animal skin in high-temperature water for 20min at the water temperature of 95 ℃;
s2: dehairing cowhide by dehairing equipment;
s3: soaking the dehaired calfskin in pH of 7.0, and adding edible alcohol at a ratio of 11KG/g for 23 min;
s4: taking out, and soaking in pH of 9.0 for 18 min;
s5: taking out and drying.
In this embodiment, in S2, the unhairing device comprises tweezers, a scraper; in S3, the alcohol consumption degree is 45 °.
Example 2
The difference from example 1 is that:
in this example, the cleaning of the cow leather in the first step was as follows:
the cleaning method of the cow leather comprises the following steps:
s1: removing damage and spots on the surface of the cowhide, and soaking the animal skin in high-temperature water for 15min at the water temperature of 90 ℃;
s2: dehairing cowhide by dehairing equipment;
s3: soaking the dehaired cowhide in pH of 6.5, and adding edible alcohol at a ratio of 13KG/g for 20 min;
s4: taking out, and soaking in pH of 6.5 for 20 min;
s5: taking out and drying.
In this embodiment, in S2, the unhairing device comprises tweezers, a scraper; in S3, the edible alcohol has a degree of 50 °
Example 3
The invention provides a technical scheme that: a preparation method of an antioxidant active collagen peptide specifically comprises the following steps:
the method comprises the following steps: pre-extraction: cleaning 10kg of fishbone, cutting into pieces, soaking in alkali liquor for degreasing, cleaning, adding 150kg of water with the pH value of 14, pulping, centrifuging, and taking supernatant;
step two: introducing the supernatant obtained in the first step into a phenyl hydrophobic chromatographic column, adsorbing, washing the chromatographic column with eluent containing 300g of complex enzyme (trypsin: papain: bromelain is 8: 8: 5) and 2M ammonium sulfate at pH9, wherein the flow rate is 5ml/min, and performing enzymolysis on collagen;
step three: elution and separation: eluting the collagen peptide on the chromatographic column in the second step by using an eluent with pH9 and 0.2M ammonium sulfate, and collecting the eluent at the flow rate of 5 ml/min;
step four: concentrating and drying: concentrating and drying the eluent in the third step to obtain the antioxidant active collagen peptide, wherein the hydroxyl radical clearance rate of the prepared collagen peptide is 95.3 percent and the superoxide anion clearance rate is 85.1 percent through detection.
In this embodiment, the step of washing the fishbone in the step one is as follows:
the cleaning method of the fishbone comprises the following steps:
a1: removing blood clots on the surface of the fishbone, and washing with neutral water with pH of 7.5 for 3 min;
a2: putting fishbone into neutral water with pH of 7.5, and heating the neutral water to 75 ℃ at a temperature rise rate of 15 ℃/min;
a3: fishing out the fishbone treated in A2, and washing with neutral water with pH of 7.5 for 1.5 min;
a4: taking out and drying.
Example 4
The difference from example 3 is that: in this embodiment, the step of washing the fishbone in the step one is as follows:
the cleaning method of the fishbone comprises the following steps:
a1: removing blood clots on the surface of the fishbone, and washing with neutral water with pH of 6.5 for 1.5 min;
a2: putting fishbone into neutral water with pH of 6.5, and heating the neutral water to 60 ℃ at a temperature rise rate of 10 ℃/min;
a3: fishing out the fishbone treated in A2, and washing with neutral water with pH of 6.5 for 2 min;
a4: taking out and drying.
Although embodiments of the present invention have been shown and described, it will be appreciated by those skilled in the art that changes, modifications, substitutions and alterations can be made in these embodiments without departing from the principles and spirit of the invention, the scope of which is defined in the appended claims and their equivalents.
Claims (7)
1. A preparation method of anti-oxidation active collagen peptide is characterized by comprising the following steps: the method specifically comprises the following steps:
the method comprises the following steps: pre-extraction: cleaning animal skin or bone, cutting into pieces, soaking in alkali liquor for degreasing, cleaning, pulping, centrifuging, and collecting supernatant;
step two: performing enzymolysis on a column: introducing the supernatant obtained in the step one into a hydrophobic chromatographic column, adsorbing, washing the chromatographic column by using eluent containing complex enzyme, and performing enzymolysis on collagen;
step three: elution and separation: eluting the collagen peptide on the chromatographic column in the second step by using an eluent, and collecting the eluent;
step four: concentrating and drying: concentrating and drying the eluent in the third step to obtain dried powder, namely the antioxidant active collagen peptide.
2. The method for preparing collagen peptide with antioxidant activity according to claim 1, wherein the collagen peptide comprises: in the first step, the water adding amount is 10-15 times of the weight of the animal skin or bone in the pulping process, and the pH value is 11-14.
3. The method for preparing collagen peptide with antioxidant activity according to claim 1, wherein the collagen peptide comprises: the compound enzyme used in the second step is trypsin, papain and bromelain, the enzyme adding amount is 1-3% of the weight of the animal skin or bone, and the weight ratio of the trypsin: papain: the bromelain is 5-8: 4-8: 3 to 5.
4. The method for preparing collagen peptide with antioxidant activity according to claim 1, wherein the collagen peptide comprises: the leacheate used in the second step is ammonium sulfate buffer solution with the pH value of 7-9 and the concentration of 0.5-2 mol/L, and the flow rate is 0.1-5 ml/min.
5. The method for preparing collagen peptide with antioxidant activity according to claim 1, wherein the collagen peptide comprises: the eluent used in the third step is a buffer solution with pH 7-9 and 0.1-0.2M ammonium sulfate, and the flow rate is 0.1-5 ml/min.
6. The method for preparing collagen peptide with antioxidant activity according to claim 1, wherein the collagen peptide comprises: the step one is that the animal skin or bone is cleaned by the following steps:
the cleaning method of the animal skin comprises the following steps:
s1: removing damage and spots on the surface of the animal skin, and soaking the animal skin in high-temperature water for 5-20 min at the water temperature of 90-100 ℃;
s2: unhairing animal skins through unhairing equipment;
s3: soaking the unhaired animal skin in pH 6.5-7.5, and adding edible alcohol at a ratio of 9-13 KG/g for 20-25 min;
s4: fishing out, and soaking again in a pH of 6.5-7.5 for 15-20 min;
s5: taking out and drying.
The cleaning method of the animal bone comprises the following steps:
a1: removing blood clots on the surface of the animal bone, and washing with neutral water with the pH of 6.5-7.5 for 1.5-3 min;
a2: putting the animal bones into neutral water with the pH value of 6.5-7.5, and heating the neutral water to 60-75 ℃ at the heating rate of 10-15 ℃/min;
a3: fishing out the animal bones treated in the step A2, and washing with neutral water with the pH value of 6.5-7.5 for 1.5-2 min;
a4: taking out and drying.
7. The method for preparing collagen peptide with antioxidant activity according to claim 6, wherein the collagen peptide comprises: in said S2, the unhairing device comprises tweezers, a spatula; in S3, the degree of the edible alcohol is 45-50 degrees.
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Citations (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5840848A (en) * | 1996-01-05 | 1998-11-24 | Autoimmune, Inc. | Method for preparation of type II collagen |
| CN103409489A (en) * | 2013-08-15 | 2013-11-27 | 集美大学 | Preparation method for fish collagen antioxidant peptide |
| CN104087641A (en) * | 2014-07-08 | 2014-10-08 | 天津大学 | Yak skin blood pressure-decreasing collagen polypeptide and preparation method thereof |
| CN104610446A (en) * | 2015-02-02 | 2015-05-13 | 浙江万里学院 | Jerk filefish skin collagen antioxidative peptide and preparation method thereof |
| CN105648004A (en) * | 2015-12-31 | 2016-06-08 | 浙江海洋学院 | Preparation method of dasyatis akajei cartilage antioxidative collagen peptide |
| CN108823268A (en) * | 2018-05-02 | 2018-11-16 | 金华市铁骑士生物科技有限公司 | The preparation method of fish collagen antioxidant peptide |
| CN110387397A (en) * | 2019-08-29 | 2019-10-29 | 内蒙古中科生物科技股份有限公司 | A kind of preparation method of sheepskin collagen oligopeptide |
| CN110845603A (en) * | 2019-10-31 | 2020-02-28 | 中国科学院生物物理研究所 | Human collagen 17-type polypeptide, production method and use thereof |
| CN111893156A (en) * | 2020-07-31 | 2020-11-06 | 青海瑞肽生物科技有限公司 | Preparation method of refined yak bone collagen peptide |
| CN113604532A (en) * | 2021-09-27 | 2021-11-05 | 王朝辉 | Preparation method of yak bone collagen peptide |
-
2021
- 2021-12-10 CN CN202111510111.3A patent/CN114106151A/en active Pending
Patent Citations (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5840848A (en) * | 1996-01-05 | 1998-11-24 | Autoimmune, Inc. | Method for preparation of type II collagen |
| CN103409489A (en) * | 2013-08-15 | 2013-11-27 | 集美大学 | Preparation method for fish collagen antioxidant peptide |
| CN104087641A (en) * | 2014-07-08 | 2014-10-08 | 天津大学 | Yak skin blood pressure-decreasing collagen polypeptide and preparation method thereof |
| CN104610446A (en) * | 2015-02-02 | 2015-05-13 | 浙江万里学院 | Jerk filefish skin collagen antioxidative peptide and preparation method thereof |
| CN105648004A (en) * | 2015-12-31 | 2016-06-08 | 浙江海洋学院 | Preparation method of dasyatis akajei cartilage antioxidative collagen peptide |
| CN108823268A (en) * | 2018-05-02 | 2018-11-16 | 金华市铁骑士生物科技有限公司 | The preparation method of fish collagen antioxidant peptide |
| CN110387397A (en) * | 2019-08-29 | 2019-10-29 | 内蒙古中科生物科技股份有限公司 | A kind of preparation method of sheepskin collagen oligopeptide |
| CN110845603A (en) * | 2019-10-31 | 2020-02-28 | 中国科学院生物物理研究所 | Human collagen 17-type polypeptide, production method and use thereof |
| CN111893156A (en) * | 2020-07-31 | 2020-11-06 | 青海瑞肽生物科技有限公司 | Preparation method of refined yak bone collagen peptide |
| CN113604532A (en) * | 2021-09-27 | 2021-11-05 | 王朝辉 | Preparation method of yak bone collagen peptide |
Non-Patent Citations (4)
| Title |
|---|
| NAGAI等: "Collagen from common minke whale (Balaenoptera acutorostrata) unesu", FOOD CHEMISTRY, vol. 111, no. 02, pages 296 - 301 * |
| 庄永亮等: "酶解海蜇胶原蛋白制备抗氧化肽工艺", 农业工程学报, vol. 25, no. 1, pages 129 - 133 * |
| 成晓瑜等: "猪骨胶原蛋白多肽制备过程中的脱色研究", 肉类研究, vol. 26, no. 10, pages 18 - 21 * |
| 朱夕波等: "猪皮胶原蛋白水解产物中的抗氧化活性肽的分离及其氨基酸组分", 天然产物研究与开发, vol. 21, no. 01, pages 122 - 124 * |
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