[go: up one dir, main page]

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 PDF

Info

Publication number
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
Authority
CN
China
Prior art keywords
collagen
non denatured
cartilage
preparation
industrialization
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
Application number
CN201811592383.0A
Other languages
Chinese (zh)
Inventor
张亮
张雷
于明晓
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
MEITEK TECHNOLOGY (QINGDAO) Co Ltd
Original Assignee
MEITEK TECHNOLOGY (QINGDAO) Co Ltd
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by MEITEK TECHNOLOGY (QINGDAO) Co Ltd filed Critical MEITEK TECHNOLOGY (QINGDAO) Co Ltd
Priority to CN201811592383.0A priority Critical patent/CN109384842A/en
Publication of CN109384842A publication Critical patent/CN109384842A/en
Pending legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/06Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products

Landscapes

  • 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)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Medicinal Chemistry (AREA)
  • Biophysics (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biotechnology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Microbiology (AREA)
  • Toxicology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • Peptides Or Proteins (AREA)
  • Cosmetics (AREA)

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

A kind of preparation method of non denatured II collagen of industrialization
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.
CN201811592383.0A 2018-12-25 2018-12-25 A kind of preparation method of non denatured II collagen of industrialization Pending CN109384842A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN201811592383.0A CN109384842A (en) 2018-12-25 2018-12-25 A kind of preparation method of non denatured II collagen of industrialization

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN201811592383.0A CN109384842A (en) 2018-12-25 2018-12-25 A kind of preparation method of non denatured II collagen of industrialization

Publications (1)

Publication Number Publication Date
CN109384842A true CN109384842A (en) 2019-02-26

Family

ID=65430621

Family Applications (1)

Application Number Title Priority Date Filing Date
CN201811592383.0A Pending CN109384842A (en) 2018-12-25 2018-12-25 A kind of preparation method of non denatured II collagen of industrialization

Country Status (1)

Country Link
CN (1) CN109384842A (en)

Cited By (7)

* Cited by examiner, † Cited by third party
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

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101063161A (en) * 2007-05-21 2007-10-31 上海阿敏生物技术有限公司 Coproduction technique for collagen and chondroitin sulfate
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
CN106916870A (en) * 2017-04-26 2017-07-04 北京盛美诺生物技术有限公司 A kind of preparation method of the cartilage extracts of the collagen types of II containing non denatured
CN107177658A (en) * 2017-07-28 2017-09-19 美泰科技(青岛)股份有限公司 A kind of preparation method of Cartilage collagen peptide
CN107312812A (en) * 2017-07-11 2017-11-03 安达市旭朗生物科技有限公司 A kind of preparation method of ox Cartilage collagen peptide

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101063161A (en) * 2007-05-21 2007-10-31 上海阿敏生物技术有限公司 Coproduction technique for collagen and chondroitin sulfate
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
CN106916870A (en) * 2017-04-26 2017-07-04 北京盛美诺生物技术有限公司 A kind of preparation method of the cartilage extracts of the collagen types of II containing non denatured
CN107312812A (en) * 2017-07-11 2017-11-03 安达市旭朗生物科技有限公司 A kind of preparation method of ox Cartilage collagen peptide
CN107177658A (en) * 2017-07-28 2017-09-19 美泰科技(青岛)股份有限公司 A kind of preparation method of Cartilage collagen peptide

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
郭休玉等: "鱿鱼软骨II型胶原蛋白提取方法及结构分析", 《生物医学工程学进展》 *

Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN112778412A (en) * 2019-11-09 2021-05-11 兰州大学 Preparation method of low-endotoxin collagen
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

Similar Documents

Publication Publication Date Title
CN109384842A (en) A kind of preparation method of non denatured II collagen of industrialization
CN102488713B (en) Method for preparing sheep placenta extract and sheep placenta hydrolyzed collagen concentrated solution
CN101120776B (en) Method for extracting beta-glucan from cereal bran using membrane separation technology
CN101402986A (en) Method for producing collagen, glutin or collagen by degreasing and deliming of fish scale
CN111793145A (en) Process for improving quality and yield of sodium chondroitin sulfate co-produced collagen peptide
CN101851300A (en) Process for extracting chondroitin sulfate
CN106967169A (en) A kind of extracting method of Isin glue collagen
CN107586821A (en) A kind of extracting method and purposes of saline cistanche polypeptide
CN107080778A (en) A kind of multiplex-enzyme extraction technique of longan pulp solid carbon dioxide insoluble active thing and application
CN102146144A (en) Method for extracting and refining inulin
CN102850466B (en) A kind of method of Os Bovis grunniens chondroitin sulfate
CN106046188B (en) A kind of preparation method of fucoidin
JP2017521451A (en) Method for extracting soluble proteins from microalgal biomass
CN118027247A (en) Method for extracting chitin from hermetia illucens larvae
CN102775511B (en) Method for extracting pepper polysaccharide from pepper residue
CN103193897B (en) Method for coproduction of sodium alginate, mannitol and iodine by enzymolysis approach
CN102268827A (en) Method for extracting celluloses from tobaccos based on ferric chloride pretreatment
CN109608539A (en) A kind of combined preparation process of non denatured II collagen type and chondroitin sulfate
CN115368486B (en) Ternary eutectic solvent and application thereof in procambarus clarkia shell chitin extraction
CN1861638A (en) Process for preparing pectin and heavy metallic ion adsorber by soybean peel combined production
CN105622779B (en) Clarify the preparation method of chondroitin sulfate enzymolysis liquid
CN116240255A (en) Eggshell membrane extract high in chondroitin sulfate and oligopeptide and preparation method thereof
CN108774283A (en) A kind of method that high-pressure pulse electric coupling biological enzymolysis prepares Tea Saponin
CN109549955A (en) A kind of preparation method of cattle liver extracting solution
CN109384861A (en) A kind of method of heparin sodium pulp thickening dermatan sulfate

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
RJ01 Rejection of invention patent application after publication

Application publication date: 20190226