CN109384842A - A kind of preparation method of non denatured II collagen of industrialization - Google Patents
A kind of preparation method of non denatured II collagen of industrialization Download PDFInfo
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- CN109384842A CN109384842A CN201811592383.0A CN201811592383A CN109384842A CN 109384842 A CN109384842 A CN 109384842A CN 201811592383 A CN201811592383 A CN 201811592383A CN 109384842 A CN109384842 A CN 109384842A
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- 102000008186 Collagen Human genes 0.000 title claims abstract description 72
- 108010035532 Collagen Proteins 0.000 title claims abstract description 72
- 229920001436 collagen Polymers 0.000 title claims abstract description 44
- 238000002360 preparation method Methods 0.000 title claims abstract description 17
- 239000000843 powder Substances 0.000 claims abstract description 50
- 210000000845 cartilage Anatomy 0.000 claims abstract description 37
- 239000007788 liquid Substances 0.000 claims abstract description 23
- 238000000034 method Methods 0.000 claims abstract description 17
- 238000001035 drying Methods 0.000 claims abstract description 8
- 238000000926 separation method Methods 0.000 claims abstract description 5
- HEMHJVSKTPXQMS-UHFFFAOYSA-M sodium hydroxide Inorganic materials [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 45
- 238000004108 freeze drying Methods 0.000 claims description 24
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 14
- 238000001914 filtration Methods 0.000 claims description 13
- 239000000284 extract Substances 0.000 claims description 12
- 238000005119 centrifugation Methods 0.000 claims description 11
- 239000008367 deionised water Substances 0.000 claims description 11
- 229910021641 deionized water Inorganic materials 0.000 claims description 11
- 239000013049 sediment Substances 0.000 claims description 10
- 108090000284 Pepsin A Proteins 0.000 claims description 9
- 102000057297 Pepsin A Human genes 0.000 claims description 9
- 229940111202 pepsin Drugs 0.000 claims description 9
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 claims description 6
- 150000004676 glycans Chemical class 0.000 claims description 6
- 229920001282 polysaccharide Polymers 0.000 claims description 6
- 239000005017 polysaccharide Substances 0.000 claims description 6
- 108091005508 Acid proteases Proteins 0.000 claims description 5
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 claims description 5
- 239000000920 calcium hydroxide Substances 0.000 claims description 5
- 229910001861 calcium hydroxide Inorganic materials 0.000 claims description 5
- 238000004140 cleaning Methods 0.000 claims description 5
- 238000005360 mashing Methods 0.000 claims description 5
- 235000013372 meat Nutrition 0.000 claims description 5
- 210000001519 tissue Anatomy 0.000 claims description 5
- 241000287828 Gallus gallus Species 0.000 claims description 3
- 241000272525 Anas platyrhynchos Species 0.000 claims description 2
- 239000007900 aqueous suspension Substances 0.000 claims description 2
- 210000001188 articular cartilage Anatomy 0.000 claims description 2
- 239000003292 glue Substances 0.000 claims 1
- SQDAZGGFXASXDW-UHFFFAOYSA-N 5-bromo-2-(trifluoromethoxy)pyridine Chemical compound FC(F)(F)OC1=CC=C(Br)C=N1 SQDAZGGFXASXDW-UHFFFAOYSA-N 0.000 abstract description 3
- 229920001287 Chondroitin sulfate Polymers 0.000 abstract description 3
- 229940059329 chondroitin sulfate Drugs 0.000 abstract description 3
- 238000000605 extraction Methods 0.000 abstract description 3
- 102000004169 proteins and genes Human genes 0.000 abstract description 3
- 108090000623 proteins and genes Proteins 0.000 abstract description 3
- 239000002351 wastewater Substances 0.000 abstract description 3
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 abstract description 2
- 238000007796 conventional method Methods 0.000 abstract description 2
- 229920002674 hyaluronan Polymers 0.000 abstract description 2
- 229960003160 hyaluronic acid Drugs 0.000 abstract description 2
- 230000007062 hydrolysis Effects 0.000 abstract description 2
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 2
- 239000012535 impurity Substances 0.000 abstract description 2
- 238000004519 manufacturing process Methods 0.000 abstract description 2
- 238000001157 Fourier transform infrared spectrum Methods 0.000 description 4
- 238000002791 soaking Methods 0.000 description 4
- 238000004659 sterilization and disinfection Methods 0.000 description 4
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 3
- 239000003513 alkali Substances 0.000 description 3
- 238000007710 freezing Methods 0.000 description 3
- 230000008014 freezing Effects 0.000 description 3
- 239000011591 potassium Substances 0.000 description 3
- 229910052700 potassium Inorganic materials 0.000 description 3
- 229920002683 Glycosaminoglycan Polymers 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 241000272201 Columbiformes Species 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 108010067787 Proteoglycans Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 210000000038 chest Anatomy 0.000 description 1
- 238000005238 degreasing Methods 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000002386 leaching Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000011017 operating method Methods 0.000 description 1
- 238000012805 post-processing Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 238000009738 saturating Methods 0.000 description 1
- 238000012360 testing method Methods 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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- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
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- Gastroenterology & Hepatology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
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Abstract
The present invention relates to bioengineering fields, and in particular to a kind of preparation method of non denatured II collagen of industrialization, including cartilage pretreatment, lye extraction, separation drying and enzymolysis step.The present invention is using first progress low-temperature alkaline liquid extraction, the method for removing most of impurity such as soluble protein, fat and chondroitin sulfate, hyaluronic acid in cartilage, be conducive to the separation drying of subsequent insoluble non denatured II collagen protein powder, with the Hydrolysis kinetics of non denatured II collagen soluble in enzymolysis step, and it can be omitted the operation such as saltout, dialyse of enzymolysis step in conventional method, preparation method step is simple, and working hour is short, it is more advantageous to industrialized production, and a large amount of waste water will not be generated.The present invention is worth with market potential.
Description
Technical field
The present invention relates to bioengineering fields, and in particular to a kind of preparation method of non denatured II collagen of industrialization.
Background technique
The technology of preparing of existing non denatured II collagen substantially uses cartilage degreasing, except directly digesting after foreign protein,
Then it repeatedly saltouts, dialysing obtains the technique of non denatured II collagen type, such as patent CN105132502A: a kind of from pigeon breast
The method that pure II collagen type is extracted in cartilage just discloses this method, but this method needs repeatedly saltout, dialyse
Non denatured II collagen type could be obtained, the polysaccharide impurity such as chondroitin sulfate, hyaluronic acid is difficult to remove, and method and step is numerous
It is trivial, process route is long, be only applicable to laboratory preparation, be difficult to be mass produced, and generate the waste water of a large amount of high concentrations, be processed into
This is higher.
Summary of the invention
The technical problem to be solved by the present invention is to how to overcome the shortcomings of the prior art, a kind of simple industry is provided
Change the preparation method of non denatured II collagen.
The technical solution of the invention is as follows: a kind of preparation method of non denatured II collagen of industrialization, including following
Step: (1) cartilage pre-processes: after meat is picked in cartilage cleaning, with the H of mass concentration 0.1~10%2O2Soaking disinfection 18~for 24 hours, with
By treated, cartilage is smashed to pieces for tissue mashing machine;(2) lye extracts: the cartilage after smashing to pieces is 12~30 in the lye of 0.1~4M
Impregnate 6 at DEG C~it extracts for 24 hours, removal soluble protein, fat and polysaccharide;(3) it separates drying: separating or filter with centrifuge
To sediment, after sediment is crushed with pulverizer plus aqueous suspension, freeze-drying obtain insoluble non denatured II collagen protein powder.
Further, further comprising the steps of: insoluble non denatured II collagen protein powder that freeze-drying obtains is placed in
In reactor tank, 1~5 times of deionized water of albumen powder quality is added, the pepsin or acidity of albumen powder quality 0.05~5% is added
Protease adjusts pH value 1.5~4.5, and 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying are digested at 4~30 DEG C
Obtain soluble non denatured II collagen protein powder.
Further, lye is sodium hydroxide or calcium hydroxide or potassium hydroxide.
Further, cartilage is pig, ox, chicken, the articular cartilage of duck or chest cartilage.
Further, step (3) centrifuge centrifuge separation operating condition is 5000rpm, 4 DEG C, 10min or more.
Present invention process route is simple, and efficiently, be produced on a large scale solvable, insoluble two kinds of non denatured II collagen
Albumen.The present invention uses low-temperature alkaline extracting technology, and the pretreated raw material of cartilage is extracted under low temperature temperate condition by alkali
Make proteoglycans that glycosidic bond chain rupture occur, the glycosaminoglycans such as chondroitin sulfate enter in leaching liquor as far as possible, extract by control
Condition, so that remaining cartilage raw material almost seldom contains glycosaminoglycan, meanwhile, alkali extraction can remove fat and solubility is miscellaneous
Albumen, a step can realize the purifying of non denatured II collagen, be conducive to subsequent insoluble non denatured II collagen protein powder
Separation drying and enzymolysis step in soluble non denatured II collagen Hydrolysis kinetics.The cartilage that alkali extracts is saturating
It is bright porous, it easily digests very much, removes end peptide in low temperature Controlled-enzymatic Hydrolysis with pepsin or acid protease and obtain the non-of solubility
It is denaturalized II collagen, insoluble non denatured II collagen can be obtained in directly freeze-drying, it is convenient to omit step is digested in conventional method
The rapid operating procedures such as saltout, dialyse.The method of the present invention is without saltouing, dialysing, and suitable for large-scale production, simple working hour is short, and
The wastewater flow rate of generation is less, is conducive to post-processing.The present invention is worth with market potential.
Detailed description of the invention
Fig. 1 is the scanning electron microscope (SEM) photograph of insoluble non denatured II collagen of 1 product of embodiment;
Fig. 2 is the electrophoretogram of non denatured II collagen of solubility of 2 product of embodiment;
Fig. 3 is the FTIR spectrum figure of insoluble non denatured II collagen of 1 product of embodiment;
Fig. 4 is the FTIR spectrum figure of non denatured II collagen of solubility of 2 product of embodiment.
Specific embodiment
With reference to embodiments, a kind of preparation method of non denatured II collagen of industrialization that the present invention will be described in detail.
Embodiment 1
A kind of preparation method of non denatured II collagen of industrialization, comprising the following steps: (1) cartilage pre-processes: cartilage
After meat is picked in cleaning, with the H of mass concentration 0.1~10%2O2Soaking disinfection 18~for 24 hours, will treated cartilage with tissue mashing machine
It smashs to pieces;(2) lye extracts: cartilage after smashing to pieces impregnates 6 in the lye of 0.1~4M at 12 DEG C~it extracts for 24 hours, and removal is soluble
Albumen, fat and polysaccharide;(3) it separates drying: with the isolated sediment of centrifuge, water is added after sediment is crushed with pulverizer
It suspends, freeze-drying obtains insoluble non denatured II collagen protein powder.Wherein lye is sodium hydroxide or calcium hydroxide or hydrogen-oxygen
Change one of potassium, cartilage is chicken cartilage, and it is 5000rpm, 4 DEG C, 10min or more that centrifuge, which is centrifugated operating condition,.
Embodiment 2
Embodiment 2 is on the basis of embodiment 1, further comprising the steps of: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 4 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
Embodiment 3
Embodiment 3 is on the basis of embodiment 1, further comprising the steps of: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 20 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
Embodiment 4
Embodiment 4 is on the basis of embodiment 1, further comprising the steps of: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 30 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
Embodiment 5
A kind of preparation method of non denatured II collagen of industrialization, comprising the following steps: (1) cartilage pre-processes: cartilage
After meat is picked in cleaning, with the H of mass concentration 0.1~10%2O2Soaking disinfection 18~for 24 hours, will treated cartilage with tissue mashing machine
It smashs to pieces;(2) lye extracts: cartilage after smashing to pieces impregnates 6 in the lye of 0.1~4M at 30 DEG C~it extracts for 24 hours, and removal is soluble
Albumen, fat and polysaccharide;(3) separate drying: to be separated by filtration to obtain sediment, after sediment is crushed with pulverizer plus water hangs
Floating, freeze-drying obtains insoluble non denatured II collagen protein powder.Wherein lye is sodium hydroxide or calcium hydroxide or hydroxide
One of potassium, cartilage are pig cartilage.
Embodiment 6
Embodiment 6 is further comprising the steps of on the basis of embodiment 5: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Acid protease, adjust pH value 1.5~4.5,24~72h digested at 4 DEG C, enzymolysis liquid centrifugation or filtering, clear liquid freezing are dry
It is dry to obtain soluble non denatured II collagen protein powder.
Embodiment 7
Embodiment 7 is further comprising the steps of on the basis of embodiment 5: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Acid protease, adjust pH value 1.5~4.5,24~72h digested at 20 DEG C, enzymolysis liquid centrifugation or filtering, clear liquid freezing are dry
It is dry to obtain soluble non denatured II collagen protein powder.
Embodiment 8
Embodiment 8 is further comprising the steps of on the basis of embodiment 5: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Acid protease, adjust pH value 1.5~4.5,24~72h digested at 30 DEG C, enzymolysis liquid centrifugation or filtering, clear liquid freezing are dry
It is dry to obtain soluble non denatured II collagen protein powder.
Embodiment 9
A kind of preparation method of non denatured II collagen of industrialization, comprising the following steps: (1) cartilage pre-processes: cartilage
After meat is picked in cleaning, with the H of mass concentration 0.1~10%2O2Soaking disinfection 18~for 24 hours, will treated cartilage with tissue mashing machine
It smashs to pieces;(2) lye extracts: cartilage after smashing to pieces impregnates 6 in the lye of 0.1~4M at 20 DEG C~it extracts for 24 hours, and removal is soluble
Albumen, fat and polysaccharide;(3) it separates drying: with the isolated sediment of centrifuge, water is added after sediment is crushed with pulverizer
It suspends, freeze-drying obtains insoluble non denatured II collagen protein powder.Wherein lye is sodium hydroxide or calcium hydroxide or hydrogen-oxygen
Change one of potassium, cartilage is ox cartilage, and it is 5000rpm, 4 DEG C, 10min or more that centrifuge, which is centrifugated operating condition,.
Embodiment 10
Embodiment 10 is further comprising the steps of on the basis of embodiment 9: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 4 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
Embodiment 11
Embodiment 11 is further comprising the steps of on the basis of embodiment 9: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 20 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
Embodiment 12
Embodiment 12 is further comprising the steps of on the basis of embodiment 9: freeze-drying being obtained insoluble non denatured
II collagen protein powder is placed in reactor tank, and 1~5 times of deionized water of albumen powder quality is added, and albumen powder quality 0.05~5% is added
Pepsin, adjust pH value 1.5~4.5, at 30 DEG C digest 24~72h, enzymolysis liquid centrifugation or filtering, clear liquid freeze-drying
Obtain soluble non denatured II collagen protein powder.
The test of embodiment properties of product
Fig. 1 is the scanning electron microscope (SEM) photograph of insoluble non denatured II collagen of embodiment 1, and Fig. 2 is the solubility of embodiment 2
The electrophoretogram of non denatured II collagen, Fig. 3 are the FTIR spectrum of insoluble non denatured II collagen of embodiment 1
Figure, Fig. 4 are the FTIR spectrum figure of non denatured II collagen of solubility of embodiment 2.Table 1 is that each embodiment is produced
The collagen content of product and non denatured II collagen content situation table.Wherein collagen content is in the method for GB5009.5
It is detected, non denatured II collagen content is detected with ELISA method.
1 collagen content of table and non denatured II collagen content situation table
As can be seen from Table 1, collagen content of the embodiment 1 into 12 product of embodiment is insoluble 90% or more
Property non denatured II collagen content 30~40% or so, the content of soluble non denatured II collagen is 60~65%
Left and right.Compared with the product of other production methods, collagen and non denatured II collagen include solvable containing with insoluble
Amount is that purity is higher.
Simply to illustrate that technical concepts and features of the invention, its purpose is allows in the art above-described embodiment
Those of ordinary skill cans understand the content of the present invention and implement it accordingly, and it is not intended to limit the scope of the present invention.It is all
It is the equivalent changes or modifications that the essence of content according to the present invention is made, should be covered by the scope of protection of the present invention.
Claims (5)
1. a kind of preparation method of non denatured II collagen of industrialization, it is characterised in that the following steps are included:
(1) cartilage pre-processes: after meat is picked in cartilage cleaning, with the H of mass concentration 0.1~10%2O2It impregnates
18~sterilize for 24 hours, with tissue mashing machine, by treated, cartilage is smashed to pieces;
(2) lye extracts: cartilage after smashing to pieces impregnates 6 in the lye of 0.1~4M at 12~30 DEG C~it extracts for 24 hours, and removal can
Dissolubility albumen, fat and polysaccharide;
(3) it separates drying: being separated with centrifuge or sediment is obtained by filtration, aqueous suspension is added after sediment is crushed with pulverizer,
Freeze-drying obtains insoluble non denatured II collagen protein powder.
2. a kind of preparation method of non denatured II collagen of industrialization according to claim 1, it is characterised in that also wrap
It includes following steps: insoluble non denatured II collagen protein powder that freeze-drying obtains is placed in reactor tank, albumen silty is added
1~5 times of deionized water of amount, the pepsin or acid protease of addition albumen powder quality 0.05~5%, adjusting pH value 1.5~
4.5,24~72h, enzymolysis liquid centrifugation or filtering are digested at 4~30 DEG C, clear liquid is freeze-dried to obtain soluble non denatured II glue
Former albumen powder.
3. a kind of preparation method of non denatured II collagen of industrialization according to claim 1, it is characterised in that: lye
For sodium hydroxide or calcium hydroxide or potassium hydroxide.
4. a kind of preparation method of non denatured II collagen of industrialization according to claim 1, it is characterised in that: cartilage
For pig, ox, chicken, the articular cartilage of duck or chest cartilage.
5. a kind of preparation method of non denatured II collagen of industrialization according to claim 1, it is characterised in that: step
(3) centrifuge centrifuge separation operating condition is 5000rpm, 4 DEG C, 10min or more.
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Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110922503A (en) * | 2019-12-10 | 2020-03-27 | 美泰科技(青岛)股份有限公司 | Novel extraction process of chondroitin sulfate |
| CN112778412A (en) * | 2019-11-09 | 2021-05-11 | 兰州大学 | Preparation method of low-endotoxin collagen |
| CN113520900A (en) * | 2021-04-13 | 2021-10-22 | 甘肃天际生物科技有限公司 | Hypoallergenic and anti-aging yak collagen composition and application thereof |
| CN113527466A (en) * | 2021-04-13 | 2021-10-22 | 甘肃天际生物科技有限公司 | Preparation method of implant-grade type II collagen |
| CN113563458A (en) * | 2021-07-19 | 2021-10-29 | 嘉兴恒杰生物制药股份有限公司 | Preparation method of non-denatured type II collagen |
| CN116253791A (en) * | 2023-02-10 | 2023-06-13 | 完美(广东)日用品有限公司 | Preparation method and application of non-denatured type II collagen with effect of improving bone joint health |
| CN116284344A (en) * | 2023-04-13 | 2023-06-23 | 中科康盛(河北)生物科技有限公司 | A kind of preparation method of non-denatured type II collagen and chondroitin sulfate of calf shoulder cartilage |
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| CN105331662A (en) * | 2015-11-30 | 2016-02-17 | 四川大学 | Non-denatured II type collagen of animal cartilage source and preparation method for non-denatured II type collagen |
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| CN112778412B (en) * | 2019-11-09 | 2022-07-08 | 胶原蛋白(武汉)生物科技有限公司 | Preparation method of low-endotoxin collagen |
| CN110922503A (en) * | 2019-12-10 | 2020-03-27 | 美泰科技(青岛)股份有限公司 | Novel extraction process of chondroitin sulfate |
| CN113520900A (en) * | 2021-04-13 | 2021-10-22 | 甘肃天际生物科技有限公司 | Hypoallergenic and anti-aging yak collagen composition and application thereof |
| CN113527466A (en) * | 2021-04-13 | 2021-10-22 | 甘肃天际生物科技有限公司 | Preparation method of implant-grade type II collagen |
| CN113527466B (en) * | 2021-04-13 | 2023-06-13 | 胶原蛋白(武汉)生物科技有限公司 | Preparation method of implant grade II type collagen |
| CN113563458A (en) * | 2021-07-19 | 2021-10-29 | 嘉兴恒杰生物制药股份有限公司 | Preparation method of non-denatured type II collagen |
| CN116253791A (en) * | 2023-02-10 | 2023-06-13 | 完美(广东)日用品有限公司 | Preparation method and application of non-denatured type II collagen with effect of improving bone joint health |
| CN116253791B (en) * | 2023-02-10 | 2024-02-23 | 完美(广东)日用品有限公司 | Preparation method and application of non-denatured type II collagen with effect of improving bone joint health |
| CN116284344A (en) * | 2023-04-13 | 2023-06-23 | 中科康盛(河北)生物科技有限公司 | A kind of preparation method of non-denatured type II collagen and chondroitin sulfate of calf shoulder cartilage |
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