Method for purifying type I collagen

A collagen and protease technology, applied in the field of purifying type I collagen, can solve the problems of increasing commodity production cost, time-consuming, complicated operation process, etc., and achieve the effects of low production cost, simple operation and simple method.

Inactive Publication Date: 2017-11-17
GUANGDONG MEDICAL UNIV
View PDF7 Cites 8 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Due to the traditional collagen purification technology, it usually takes a long time, the operation process is cumbersome, and the cost of commodity production is increased. Therefore, it is necessary to seek new purification technology to purify type I collagen

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Method for purifying type I collagen
  • Method for purifying type I collagen

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0027] A method for purifying type I collagen, comprising the following steps:

[0028] Step 1. Degrease the animal tissue rich in type I collagen, remove fascia and fat, and then pulverize it, then extract it at low temperature by combining acid and protease, and collect it after high-speed centrifugation. Serum; in this embodiment, the animal tissue rich in type I collagen is derived from one or any combination of two or more of cattle, pigs, sheep, chickens, fish, donkeys, deer, jellyfish or sea cucumbers, so Said animal tissue is one or any combination of two or more of skin, tendon, bone, cartilage or basement membrane; in this embodiment, the protease is collagenase, pepsin, trypsin, papain, bromelain, pancreatic One or any combination of two or more of chymotrypsin and bovine trypsin; in this embodiment, the acid is one or any combination of two or more of organic acids, inorganic acids, or buffer pairs; wherein, The organic acid is acetic acid, formic acid, malic acid...

Embodiment 2

[0032] A method for purifying type I collagen, comprising the following steps:

[0033] Step 1. Degrease the animal tissue rich in type I collagen, remove fascia and fat, and then pulverize it, then extract it at low temperature by combining acid and protease, and collect it after high-speed centrifugation. Serum; in the present embodiment, the animal tissue rich in type I collagen is derived from cattle, and the animal tissue is skin; in the present embodiment, the protease is collagenase; in the present embodiment, the acid is an organic acid; wherein, The organic acid is acetic acid; in the present embodiment, the low temperature condition is 8°C;

[0034] Step 2. Adjust the supernatant obtained in step 1 to neutral with a 20% alkali solution, filter, the insoluble matter is type I collagen, then wash the insoluble matter with a large amount of pure water, filter again, and repeat the above Steps are repeated until collagen swelling occurs, and then an appropriate amount o...

Embodiment 3

[0038] A method for purifying type I collagen, comprising the following steps:

[0039] Step 1. Degrease the animal tissue rich in type I collagen, remove fascia and fat, and then pulverize it, then extract it at low temperature by combining acid and protease, and collect it after high-speed centrifugation. Serum; in the present embodiment, the animal tissue rich in type I collagen is derived from pigs, and the animal tissue is tendon; in the present embodiment, the protease is pepsin; in the present embodiment, the acid is an inorganic acid; wherein, The inorganic acid is hydrochloric acid; in the present embodiment, the low temperature condition is 5°C;

[0040] Step 2. Adjust the supernatant obtained in step 1 to neutral with a concentration of 5% alkaline solution, filter, the insoluble matter is type I collagen, then wash the insoluble matter with a large amount of pure water, filter again, and repeat the above The steps are repeated until the collagen protein swells, an...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
molecular weightaaaaaaaaaa
concentrationaaaaaaaaaa
molecular weightaaaaaaaaaa
Login to view more

Abstract

The invention relates to the technical field of collagen purification, in particular to a method for purifying type I collagen. The method for purifying the type I collagen comprises the following steps: S1: adopting a proper method to extract the type I collagen; S2: obtaining a type I collagen dilute solution; S3: obtaining the purified type I collagen. Compared with the prior art, the method for purifying the type I collagen has the advantages that the purification time of the type I collagen can be obviously shortened, and an ideal purification effect can be achieved. According to the method, only 12-24 hours are required for an ultrafiltration purification technology to purify the collagen to achieve required purification and concentration, but time of about one week is required for the dialysis method purification of the prior art to achieve the same purity and concentration. The method for purifying the type I collagen has the characteristics of simple method, convenience in operation and low production cost and can be suitable for industrial large-scale application.

Description

technical field [0001] The invention relates to the technical field of collagen purification, in particular to a method for purifying type I collagen. Background technique [0002] Type I collagen has the advantages of good biocompatibility, low immunogenicity, promotion of cell survival and growth, promotion of platelet aggregation and biodegradability. Type Ⅰ collagen has been widely used clinically in surgical sutures, hemostatic fibers, artificial skin, artificial blood vessels, and artificial bones. Surgical sutures made of type I collagen not only have high strength similar to natural silk, but also have absorbability, are not easy to damage body tissues during operation, and have good adhesion to wounds. Type I collagen is made into powdery, flat and sponge-like hemostatic agents, which can achieve a satisfactory hemostatic effect with only a short period of compression. At the same time, because the collagen molecule contains a large number of hydroxyl groups, it h...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(China)
IPC IPC(8): C12P21/06C07K14/78C07K1/34
CPCC07K14/78C12P21/06
Inventor 彭新生周艳芳周艳星崔碧玲刘雯恩范志强王勤欧荞菲
Owner GUANGDONG MEDICAL UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap