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Collagen polypeptide which is prepared by aid of enzyme membrane coupling methods and has uniform molecular weights

A technology coupled with collagen peptides and enzyme membranes, applied in the field of biomaterial preparation, can solve problems such as analysis and use interference, purification, and difficulties

Inactive Publication Date: 2019-05-24
南杰
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0002] Whether it is in the analysis of the primary structure of collagen or in the preparation of collagen biomaterials, it is often necessary to cut the collagen due to the limitation of the quantitative reaction or the special requirements of the material properties. The traditional method is to use trypsin , pepsin, etc., but because the enzyme is also a special protein, the residue after its action is completed becomes the impurity in the product, which will cause interference and purification difficulties to the later analysis and use

Method used

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Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0011] Dissolve 10 mg of commercially available or self-made collagen in 20 ml of 70% (v / v) acetic acid solution, and pass through ammonia gas for 10 minutes to remove oxygen. Add 40 mg of solid CNBr, and pass ammonia gas for 2 minutes again. The reaction was stirred and reacted in a sealed container for 4 hours, and the reaction temperature was controlled at 30°C. After the reaction was completed, 8 times of deionized water was added to dilute and freeze-dried. The freeze-dried sample was then diluted with 5-fold deionized water and freeze-dried, and this was repeated twice. A commercially available propylmethylcellulose chromatography packing material was used. The starting buffer is 0.02mol / L sodium citrate (PH3.6) buffer. The elution buffer is 0.18mol / L sodium citrate (PH3.6) buffer. The column cleaning buffer is 0.01mol / L NaOH buffer. The column filling temperature was 45°C, the column filling buffer was the column cleaning buffer, and the column equilibration was per...

Embodiment 2

[0013] Take 10 mg of commercially available or self-made collagen and dissolve it in 50 ml of 50% (v / v) acetic acid solution, and pass ammonia gas for 15 minutes to remove oxygen. Add 70 mg of solid CNBr, and pass ammonia gas for 5 minutes again. The reaction was stirred and reacted in a sealed container for 8 hours, and the reaction temperature was controlled at 10°C. After the reaction was completed, 10 times of deionized water was added to dilute and freeze-dried. The freeze-dried sample was then diluted with 8-fold deionized water and freeze-dried, and this was repeated twice. Use commercially available cellulose ethanol chromatography media. The starting buffer is 0.05mol / L sodium citrate (PH2.2) buffer. The elution buffer is 0.23mol / L sodium citrate (PH2.2) buffer. The column washing buffer is 0.1mol / L NaOH buffer. The column filling temperature was 35°C, the column filling buffer was the column cleaning buffer, and the column equilibration was performed with the ini...

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PUM

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Abstract

The invention discloses a collagen polypeptide which is prepared by the aid of enzyme membrane coupling methods and has uniform molecular weights, and belongs to the technical field of biology. The collagen polypeptide has the advantages that the problem of disturbance on the purity of products when collagen is decomposed by the aid of enzyme methods at present mainly can be solved by the aid of the collagen polypeptide, and the shortcoming of disturbance on test results or influence on preparation and purification of biological materials due to enzymatic hydrolysis of the traditional collagenpeptide fragments can be overcome by the aid of the collagen polypeptide.

Description

technical field [0001] The invention relates to the preparation of uniform molecular weight collagen polypeptides by an enzyme-membrane coupling method, and the prepared peptides can be used for collagen typing, electrophoresis and bridging analysis, and can also be used for the preparation of biological materials. Background technique [0002] Whether it is in the analysis of the primary structure of collagen or in the preparation of collagen biomaterials, it is often necessary to cut the collagen due to the limitation of the quantitative reaction or the special requirements of the material properties. The traditional method is to use trypsin , pepsin, etc., but because the enzyme is also a special protein, the residue after its action is completed becomes an impurity in the product, which will cause interference and difficulty in purification for later analysis and use. The present invention utilizes CNBr to react with the methionine residue in the protein to generate a pe...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/78C07K1/16
Inventor 南杰
Owner 南杰