CN111363772A - Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof - Google Patents
Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof Download PDFInfo
- Publication number
- CN111363772A CN111363772A CN202010268016.6A CN202010268016A CN111363772A CN 111363772 A CN111363772 A CN 111363772A CN 202010268016 A CN202010268016 A CN 202010268016A CN 111363772 A CN111363772 A CN 111363772A
- Authority
- CN
- China
- Prior art keywords
- bone
- collagen peptide
- drying
- bovine bone
- enzymolysis
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 210000000988 bone and bone Anatomy 0.000 title claims abstract description 73
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 60
- 102000008186 Collagen Human genes 0.000 title claims abstract description 47
- 108010035532 Collagen Proteins 0.000 title claims abstract description 47
- 229920001436 collagen Polymers 0.000 title claims abstract description 47
- 238000000034 method Methods 0.000 title claims abstract description 41
- 241000283690 Bos taurus Species 0.000 title claims abstract description 40
- 230000003301 hydrolyzing effect Effects 0.000 title claims abstract description 14
- 239000004365 Protease Substances 0.000 claims abstract description 24
- 108091005804 Peptidases Proteins 0.000 claims abstract description 18
- 238000007710 freezing Methods 0.000 claims abstract description 18
- 230000008014 freezing Effects 0.000 claims abstract description 18
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 17
- 238000001035 drying Methods 0.000 claims abstract description 17
- 102000004190 Enzymes Human genes 0.000 claims abstract description 9
- 108090000790 Enzymes Proteins 0.000 claims abstract description 9
- 238000000926 separation method Methods 0.000 claims abstract description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 9
- 238000004140 cleaning Methods 0.000 claims abstract description 7
- 230000009849 deactivation Effects 0.000 claims abstract description 7
- 238000000227 grinding Methods 0.000 claims abstract description 7
- 238000001914 filtration Methods 0.000 claims abstract description 6
- 239000012528 membrane Substances 0.000 claims abstract description 6
- 238000007670 refining Methods 0.000 claims abstract description 5
- 230000000694 effects Effects 0.000 claims abstract description 3
- 235000019419 proteases Nutrition 0.000 claims description 16
- 229940088598 enzyme Drugs 0.000 claims description 8
- 238000006243 chemical reaction Methods 0.000 claims description 6
- 239000011552 falling film Substances 0.000 claims description 6
- 239000002245 particle Substances 0.000 claims description 6
- 230000035484 reaction time Effects 0.000 claims description 6
- 238000001694 spray drying Methods 0.000 claims description 6
- 108090000145 Bacillolysin Proteins 0.000 claims description 5
- 108091005507 Neutral proteases Proteins 0.000 claims description 5
- 102000035092 Neutral proteases Human genes 0.000 claims description 5
- 238000004108 freeze drying Methods 0.000 claims description 5
- 238000004321 preservation Methods 0.000 claims description 4
- 108091005658 Basic proteases Proteins 0.000 claims description 3
- 108010004032 Bromelains Proteins 0.000 claims description 3
- 108090000526 Papain Proteins 0.000 claims description 3
- 238000005054 agglomeration Methods 0.000 claims description 3
- 230000002776 aggregation Effects 0.000 claims description 3
- 235000019835 bromelain Nutrition 0.000 claims description 3
- 238000005469 granulation Methods 0.000 claims description 3
- 230000003179 granulation Effects 0.000 claims description 3
- 229940055729 papain Drugs 0.000 claims description 3
- 235000019834 papain Nutrition 0.000 claims description 3
- 108010019160 Pancreatin Proteins 0.000 claims description 2
- 108090000284 Pepsin A Proteins 0.000 claims description 2
- 102000057297 Pepsin A Human genes 0.000 claims description 2
- 102000004142 Trypsin Human genes 0.000 claims description 2
- 108090000631 Trypsin Proteins 0.000 claims description 2
- 235000013601 eggs Nutrition 0.000 claims description 2
- 229940055695 pancreatin Drugs 0.000 claims description 2
- 229940111202 pepsin Drugs 0.000 claims description 2
- 239000012588 trypsin Substances 0.000 claims description 2
- 229960001322 trypsin Drugs 0.000 claims description 2
- 238000009777 vacuum freeze-drying Methods 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 abstract description 13
- 108090000623 proteins and genes Proteins 0.000 abstract description 13
- 230000008569 process Effects 0.000 abstract description 6
- 230000000050 nutritive effect Effects 0.000 abstract description 3
- 150000001413 amino acids Chemical class 0.000 description 6
- 102000007079 Peptide Fragments Human genes 0.000 description 4
- 108010033276 Peptide Fragments Proteins 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 238000004090 dissolution Methods 0.000 description 4
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 239000002893 slag Substances 0.000 description 3
- 239000002253 acid Substances 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 235000016709 nutrition Nutrition 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 206010006956 Calcium deficiency Diseases 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 238000000889 atomisation Methods 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000002308 calcification Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000009690 centrifugal atomisation Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000005461 lubrication Methods 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- 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
-
- 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]
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a method for preparing collagen peptide by hydrolyzing bovine bone and the collagen peptide, which comprises the following steps: taking bovine bones, cleaning, and freezing and preserving at-20 to-1 ℃ for 3 to 11 hours; grinding the frozen and preserved bovine bone in the step S1 into bone residues; adding 0.5-1.5 times of water into the bone residues obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions; and (3) after the enzymolysis is finished, carrying out enzyme deactivation treatment, filtering by a plate-and-frame filter press or membrane separation, purifying, refining, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide. The process method has the advantages of short enzymolysis time, good enzymolysis effect, high nutritive value and good dispersibility, and the obtained protein peptide product is easy to dissolve in water.
Description
Technical Field
The invention relates to the field of preparation of protein peptides, in particular to a method for preparing collagen peptides by hydrolyzing bovine bones and the collagen peptides.
Background
Collagen is a structural protein of extracellular matrix, a main component in animal connective tissue, and is also a functional protein with the largest content and the widest distribution in mammals, and has close relation with the formation, maturation and intercellular information transmission of tissues, joint lubrication, wound healing, calcification, blood coagulation, aging and the like. Collagen peptide has not only a lot of physiological activities of collagen but also properties that collagen does not have. Compared with collagen, the collagen peptide is a small molecular peptide, has lower molecular weight and better digestion and absorption, can be directly absorbed by intestinal tracts and enters blood to reach various parts of the body such as skin, liver, kidney and the like.
The bovine bone collagen peptide is mainly collagen extracted from bovine bones, and the collagen peptide is easy to be absorbed by a human body, so that the elasticity of skin can be effectively increased, and the strength of bones can be effectively increased. Not only can whiten the skin, but also can reduce the osteoporosis phenomenon caused by the calcium deficiency. The mineral substances contained in the composition are rich, and can regulate electrolyte balance in human body. Can promote the repair of body cells, and prevent and resist cancer.
At present, the common process methods for producing bovine bone collagen peptide comprise: acid hydrolysis, base hydrolysis and protease hydrolysis. Although the yield is high in the process of producing the protein peptide by the acid and alkali hydrolysis process, amino acid in the product is seriously damaged during hydrolysis, so that the nutritive value of the protein peptide product is reduced, in addition, a large amount of salt is brought in the production process of the method, and desalting treatment is carried out if necessary. In contrast, the process conditions for producing the protein peptide by the enzyme method are mild, and the amino acid cannot be damaged in the production process, so that the protein peptide product prepared by the enzyme method has higher nutritional value. For example, patent publication No. CN108342441B discloses a fatigue-relieving and antioxidant yak bone protein peptide and a preparation method thereof, which comprises the steps of carrying out pretreatment such as high-frequency ultrasonic wave and ultrahigh-pressure micro-jet on yak bone protein liquid, carrying out stepwise enzymolysis by using various compound proteases under the condition of not adding any acid and alkali, and carrying out separation by membrane separation, gel separation and reversed-phase HPLC separation technologies. However, the high-frequency ultrasonic equipment and the ultrahigh-pressure micro-jet equipment adopted in the patent are expensive, and large-scale industrial production is difficult to realize.
Disclosure of Invention
The invention aims to: in order to solve the problems, the invention provides a method for preparing collagen peptide by hydrolyzing bovine bone and the collagen peptide thereof, which have better dispersity and solubility.
The technical scheme adopted by the invention is as follows:
a method for preparing collagen peptide by hydrolyzing bovine bone comprises the following steps:
s1, cleaning the ox bone, and preserving the ox bone for 3-11 hours at-20 to-1 ℃;
s2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues;
s3, adding 0.5-1.5 times of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions;
and S4, carrying out enzyme deactivation treatment after the enzymolysis is finished, filtering by a plate and frame filter press or membrane separation, purifying, refining, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide.
Preferably, the specific method for freezing preservation of bovine bones is as follows: the frozen preserved eggs are firstly preserved at the temperature of minus 20 to minus 15 ℃ for 2 to 3 hours, then preserved at the temperature of minus 10 to minus 5 ℃ for 4 to 5 hours, and finally preserved at the temperature of minus 4 to minus 1 ℃ for 2 to 3 hours.
Preferably, the specific method for freezing preservation of bovine bones is as follows: freezing and preserving for 5-8 h at-10 to-5 ℃.
Preferably, the particle size of the bone residue in the step S2 is 1000-10000 meshes.
Preferably, the conditions of the enzymolysis in step S3 are as follows: the pH value is 6-8, the reaction temperature is 55-75 ℃, and the reaction time is 30-50 min.
Preferably, the protease is one or a mixture of papain, neutral protease, alkaline protease, bromelain, trypsin, pepsin, pancreatin and compound protease of Novixin.
Preferably, in the step (4), a falling film type double-effect concentrator is adopted for concentration treatment; the drying method is freeze drying or spray drying.
Preferably, the freeze-drying is performed using a vacuum freeze-dryer.
Preferably, the drying treatment is carried out by using a pressure type spray drying tower or a centrifugal type atomization drying tower or an agglomeration granulation drying tower.
A collagen peptide prepared based on the method of any one of claims 1 to 9.
Compared with the prior art, the invention has the beneficial effects that:
1) the process method has the advantages of short enzymolysis time, good enzymolysis effect, high nutritive value and good dispersibility, and the obtained protein peptide product is easy to dissolve in water.
2) The protein peptide developed by the invention has good flavor and can be widely applied to special foods and nutritional foods.
3) The invention develops the bone protein peptide, wherein the proportion of the peptide with the molecular weight less than 1000 is more than 90 percent, and the bone protein peptide has a more definite peptide composition.
Detailed Description
The present invention will be described in further detail in order to make the objects, technical solutions and advantages of the present invention more apparent. It should be understood that the detailed description and specific examples, while indicating the preferred embodiment of the invention, are intended for purposes of illustration only and are not intended to limit the scope of the invention.
Example 1
A method for preparing collagen peptide by hydrolyzing bovine bone comprises the following steps:
s1, cleaning the ox bone, freezing and preserving at-20 to-15 ℃ for 2.5h, then freezing and preserving at-10 to-5 ℃ for 4.5h, and finally freezing and preserving at-4 to-1 ℃ for 2.5 h.
S2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues; the particle size of the bone residues in the step S2 is 5000 meshes.
S3, adding 1 time of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions; the enzymolysis conditions are as follows: the pH value is 6-8, the reaction temperature is 65 ℃, and the reaction time is 40 min; the protease is neutral protease.
And S4, carrying out enzyme deactivation after the enzymolysis is finished, filtering by a plate-frame filter press, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide. A falling film type double-effect concentrator is adopted for concentration treatment; and (4) carrying out freeze drying by using a vacuum freeze dryer.
The protein content of the bovine bone collagen peptide prepared by the method is 89%; contains 18 kinds of amino acids; the peptide segment content with the molecular mass of 1000 Da-5000 Da is 8.0%; the content of peptide fragment with molecular mass less than 1000Da is more than 90 percent; the dissolution rate is 10 min; the dispersity of 60s is 100%, and the dispersity of 20s is 93%; the appearance of the solution is light yellow, clear and bright.
Example 2
A method for preparing collagen peptide by hydrolyzing bovine bone comprises the following steps:
s1, cleaning ox bone, freezing and preserving at-20 deg.C for 2h, freezing and preserving at-10 deg.C for 4h, and freezing and preserving at-4 deg.C for 2 h.
S2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues; the particle size of the bone slag in the step S2 is 6000 meshes.
S3, adding 1.5 times of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions; the enzymolysis conditions are as follows: the pH value is 6-8, the reaction temperature is 55-75 ℃, and the reaction time is 35 min; the protease is neutral protease.
And S4, carrying out enzyme deactivation after enzymolysis, carrying out membrane separation, purification and refining, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide. A falling film type double-effect concentrator is adopted for concentration treatment; a pressure type spray drying tower is adopted.
The protein content of the bovine bone collagen peptide prepared by the method is 88%; contains 18 kinds of amino acids; the peptide segment content with the molecular mass of 1000 Da-5000 Da is 6.0%; the content of peptide fragment with molecular mass less than 1000Da is more than 92 percent; the dissolution rate is 8 min; the dispersion degree of 60s is 100%, and the dispersion degree of 20s is 94%; the appearance of the solution is light yellow, clear and bright.
Example 3
A method for preparing collagen peptide by hydrolyzing bovine bone comprises the following steps:
s1, cleaning ox bone, and freezing and preserving at-1 ℃ for 11 h; freezing and preserving at-15 deg.C for 3h, freezing and preserving at-5 deg.C for 5h, and freezing and preserving at-1 deg.C for 3 h.
S2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues; the particle size of the bone slag in the step S2 is 6000 meshes.
S3, adding 0.5 time of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions; the enzymolysis conditions are as follows: the pH value is 6-8, the reaction temperature is 55-75 ℃, and the reaction time is 45 min; the compound protease of the protease Novixin company.
And S4, carrying out enzyme deactivation after the enzymolysis is finished, filtering by a plate-frame filter press, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide. A falling film type double-effect concentrator is adopted for concentration treatment; a centrifugal atomization drying tower is adopted.
The protein content of the bovine bone collagen peptide prepared by the method is 89%; contains 18 kinds of amino acids; the peptide segment content with the molecular mass of 1000 Da-5000 Da is 9.0%; the content of peptide fragment with molecular mass less than 1000Da is more than 90 percent; the dissolution rate is 8 min; the dispersion degree of 60s is 100 percent, and the dispersion degree of 20s is 90 percent; the appearance of the solution is light yellow, clear and bright.
Example 4
A method for preparing collagen peptide by hydrolyzing bovine bone comprises the following steps:
s1, taking the ox bone, cleaning and freezing and preserving for 7 hours at the temperature of minus 10 to minus 5 ℃.
S2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues; the particle size of the bone slag in the step S2 is 6000 meshes.
S3, adding 0.5 time of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions; the enzymolysis conditions are as follows: the pH value is 6-8, the reaction temperature is 55-75 ℃, and the reaction time is 40 min; the protease is a mixture of papain, neutral protease, alkaline protease and bromelain.
And S4, carrying out enzyme deactivation treatment after the enzymolysis is finished, filtering by a plate and frame filter press or membrane separation, purifying, refining, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide. A falling film type double-effect concentrator is adopted for concentration treatment; and drying by adopting an agglomeration granulation drying tower.
The protein content of the bovine bone collagen peptide prepared by the method is 87%; contains 18 kinds of amino acids; the peptide segment content with the molecular mass of 1000 Da-5000 Da is 9.0%; the content of peptide fragment with molecular mass less than 1000Da is more than 91 percent; the dissolution rate is 10 min; the dispersity of 60s is 100%, and the dispersity of 20s is 92%; the appearance of the solution is light yellow, clear and bright.
The above-mentioned embodiments only express the specific embodiments of the present application, and the description thereof is more specific and detailed, but not construed as limiting the scope of the present application. It should be noted that, for those skilled in the art, without departing from the technical idea of the present application, several changes and modifications can be made, which are all within the protection scope of the present application.
Claims (10)
1. A method for preparing collagen peptide by hydrolyzing bovine bone is characterized by comprising the following steps:
s1, cleaning the ox bone, and preserving the ox bone for 3-11 hours at-20 to-1 ℃;
s2, grinding the cattle bone which is frozen and preserved in the step S1 into bone residues;
s3, adding 0.5-1.5 times of water into the bone dregs obtained in the step S2, homogenizing, adjusting the temperature to 40-50 ℃, adding protease, and performing enzymolysis under certain conditions;
and S4, carrying out enzyme deactivation treatment after the enzymolysis is finished, filtering by a plate and frame filter press or membrane separation, purifying, refining, carrying out double-effect concentration, and drying to obtain the bovine bone collagen peptide.
2. The method for preparing collagen peptide by hydrolyzing bovine bone according to claim 1, wherein the specific method for freezing preservation of bovine bone is as follows: the frozen preserved eggs are firstly preserved at the temperature of minus 20 to minus 15 ℃ for 2 to 3 hours, then preserved at the temperature of minus 10 to minus 5 ℃ for 4 to 5 hours, and finally preserved at the temperature of minus 4 to minus 1 ℃ for 2 to 3 hours.
3. The method for preparing collagen peptide by hydrolyzing bovine bone according to claim 1, wherein the specific method for freezing preservation of bovine bone is as follows: freezing and preserving for 5-8 h at-10 to-5 ℃.
4. The method for preparing collagen peptide according to claim 1, wherein the particle size of the bone residue in step S2 is 1000-10000 mesh.
5. The method for preparing collagen peptide according to claim 1, wherein the conditions of enzymolysis in step S3 are as follows: the pH value is 6-8, the reaction temperature is 55-75 ℃, and the reaction time is 30-50 min.
6. The method for preparing collagen peptide according to claim 1, wherein the protease is one or more selected from papain, neutral protease, alkaline protease, bromelain, trypsin, pepsin, pancreatin, and complex protease of Novitin.
7. The method for preparing collagen peptide by hydrolyzing bovine bone according to claim 1, wherein in the step (4), a falling film type double effect concentrator is adopted for concentration treatment; the drying method is freeze drying or spray drying.
8. The method for preparing collagen peptide according to claim 7, wherein a vacuum freeze-drying machine is used for freeze-drying.
9. The method for preparing collagen peptide according to claim 7, wherein the drying treatment is performed by a pressure type spray drying tower, a centrifugal type spray drying tower or an agglomeration granulation drying tower.
10. A collagen peptide prepared based on the method of any one of claims 1 to 9.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010268016.6A CN111363772A (en) | 2020-04-08 | 2020-04-08 | Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010268016.6A CN111363772A (en) | 2020-04-08 | 2020-04-08 | Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN111363772A true CN111363772A (en) | 2020-07-03 |
Family
ID=71203163
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202010268016.6A Pending CN111363772A (en) | 2020-04-08 | 2020-04-08 | Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN111363772A (en) |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| CN111944866A (en) * | 2020-07-31 | 2020-11-17 | 青海瑞肽生物科技有限公司 | Method for preparing yak hide small molecule collagen peptide by continuous rotary evaporation, desolventizing and double enzymolysis |
| CN112568321A (en) * | 2020-12-15 | 2021-03-30 | 内蒙古阿荣旗牧原康肽实业有限公司 | Method for producing and purifying bone collagen peptide |
| CN113234140A (en) * | 2021-05-24 | 2021-08-10 | 湖南康琪壹佰生物科技有限公司 | Food for improving skin moisture and preparation method thereof |
| CN113912703A (en) * | 2021-03-15 | 2022-01-11 | 陕西医赛尔生物科技有限公司 | Preparation method and application of whitening and spot-lightening active bovine achilles tendon collagen peptide |
| CN115251401A (en) * | 2022-06-17 | 2022-11-01 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide nutritional supplement composition beneficial to immunity improvement and application thereof |
| CN115251400A (en) * | 2022-06-16 | 2022-11-01 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide nutritional supplement composition capable of increasing bone density and application thereof |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102229971A (en) * | 2011-05-10 | 2011-11-02 | 苏州瑞蓝博中药技术开发有限公司 | Method for preparing collagen peptides by using fresh yak bones |
| EP2426138A1 (en) * | 2009-04-28 | 2012-03-07 | Meiji Co., Ltd. | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| CN102827911A (en) * | 2012-09-24 | 2012-12-19 | 平凉市华科生物技术有限公司 | Preparation method of animal peptone by double-enzyme enzymolysis |
| CN103468771A (en) * | 2013-05-27 | 2013-12-25 | 河北考力森生物科技有限公司 | Method for extracting collagens from bovine achilles tendon |
| CN105018554A (en) * | 2015-07-30 | 2015-11-04 | 北京天肽生物科技有限公司 | Small molecule bovine bone collagen peptide and preparation method thereof |
| CN109735591A (en) * | 2019-03-14 | 2019-05-10 | 舜甫科技(固安)有限公司 | A kind of ox bone collagen protein peptides and its production method |
| CN110923285A (en) * | 2019-12-12 | 2020-03-27 | 陶红梅 | Bovine bone peptide and preparation process thereof |
-
2020
- 2020-04-08 CN CN202010268016.6A patent/CN111363772A/en active Pending
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2426138A1 (en) * | 2009-04-28 | 2012-03-07 | Meiji Co., Ltd. | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| CN102229971A (en) * | 2011-05-10 | 2011-11-02 | 苏州瑞蓝博中药技术开发有限公司 | Method for preparing collagen peptides by using fresh yak bones |
| CN102827911A (en) * | 2012-09-24 | 2012-12-19 | 平凉市华科生物技术有限公司 | Preparation method of animal peptone by double-enzyme enzymolysis |
| CN103468771A (en) * | 2013-05-27 | 2013-12-25 | 河北考力森生物科技有限公司 | Method for extracting collagens from bovine achilles tendon |
| CN105018554A (en) * | 2015-07-30 | 2015-11-04 | 北京天肽生物科技有限公司 | Small molecule bovine bone collagen peptide and preparation method thereof |
| CN109735591A (en) * | 2019-03-14 | 2019-05-10 | 舜甫科技(固安)有限公司 | A kind of ox bone collagen protein peptides and its production method |
| CN110923285A (en) * | 2019-12-12 | 2020-03-27 | 陶红梅 | Bovine bone peptide and preparation process thereof |
Non-Patent Citations (1)
| Title |
|---|
| 胡颀等: "牛骨源胶原蛋白肽的制备及其生理活性研究进展", 《食品工业科技》 * |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| CN111944866A (en) * | 2020-07-31 | 2020-11-17 | 青海瑞肽生物科技有限公司 | Method for preparing yak hide small molecule collagen peptide by continuous rotary evaporation, desolventizing and double enzymolysis |
| CN111944866B (en) * | 2020-07-31 | 2023-06-20 | 青海瑞肽生物科技有限公司 | Method for preparing small molecular collagen peptide of yak leather by continuous rotary steaming desolventizing double enzymolysis |
| CN112568321A (en) * | 2020-12-15 | 2021-03-30 | 内蒙古阿荣旗牧原康肽实业有限公司 | Method for producing and purifying bone collagen peptide |
| CN113912703A (en) * | 2021-03-15 | 2022-01-11 | 陕西医赛尔生物科技有限公司 | Preparation method and application of whitening and spot-lightening active bovine achilles tendon collagen peptide |
| CN113234140A (en) * | 2021-05-24 | 2021-08-10 | 湖南康琪壹佰生物科技有限公司 | Food for improving skin moisture and preparation method thereof |
| CN115251400A (en) * | 2022-06-16 | 2022-11-01 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide nutritional supplement composition capable of increasing bone density and application thereof |
| CN115251401A (en) * | 2022-06-17 | 2022-11-01 | 兆鑫堂(山东)生物科技有限公司 | Collagen peptide nutritional supplement composition beneficial to immunity improvement and application thereof |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN111363772A (en) | Method for preparing collagen peptide by hydrolyzing bovine bone and collagen peptide thereof | |
| Grzonka et al. | Cysteine proteases | |
| CN103789381A (en) | Method for rapidly extracting fish collagen | |
| CN113088548A (en) | Preparation method of oyster antioxidant active peptide | |
| CN105112478B (en) | Preparation method of squid skin active polypeptide | |
| Suo-Lian et al. | Technology for extracting effective components from fish scale | |
| CN110592053A (en) | Collagen hydrolysis complex enzyme, protein oligopeptide and preparation method thereof | |
| CN113754759A (en) | Process for extracting multiple nutritional ingredients from fish scales | |
| CN113789361A (en) | Cod peptide and preparation method and application thereof | |
| JP2004149736A (en) | Chondroitin sodium sulfate, chondroitin sulfate-containing substance, and method for producing them | |
| CN111567672B (en) | Method for preparing fibrous peanut protein gel by using endogenous protease | |
| CN115368454B (en) | Gelatin and preparation method thereof | |
| Ledward et al. | Recovery and utilisation of by‐product proteins of the meat industry | |
| CN107488696B (en) | Chicken bone double-enzymolysis method | |
| WO2023082523A1 (en) | Method for improving extraction rate of chondroitin sulfate prepared from tilapia skull | |
| CN105002246A (en) | Fish polypeptide with uniform molecular weight distribution, and preparation method thereof | |
| CN111485010B (en) | Preparation method of protein for lowering cholesterol | |
| CN111926050A (en) | Purification process of globefish seminal vesicle collagen peptide | |
| CN114907470B (en) | Method for preparing hydrolyzed collagen from animal skin and hydrolyzed collagen | |
| CN1584044A (en) | Preparing method for antler polypeptide or tortoise plastron polypeptide | |
| RU2800775C1 (en) | Method for obtaining low molecular weight collagen from fish skins | |
| CN111548433B (en) | Method for extracting chondroitin sulfate from longsnout catfish bones | |
| RU2325814C2 (en) | Manufacturing method of protein preparation from the by-products of category ii | |
| RU2816709C1 (en) | Method of producing an extract for preparing functional beverages | |
| RU2821928C1 (en) | Method of producing extract for preparing functional beverages |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20200703 |
|
| RJ01 | Rejection of invention patent application after publication |