Preparation And Structural Characterization Of High-Purity Bovine Collagen
Keywords
Beef Bone, Collagen, Purification, Structural Characterization
Abstract
This experiment uses bovine bone as raw material and provides a method for preparing natural bovine collagen through steps such as crushing, defatting, decalcification, enzymatic hydrolysis, salting out, purification, and freeze-drying. SDS-PAGE gel electrophoresis, ultraviolet absorption spectrum, infrared absorption spectrum, and amino acid content analysis methods were used to characterize its structure. The results show that the purity of the purified natural bovine collagen reaches 99%, belongs to type I collagen ([¦Á1(I)]2¦Á2(I)), and completely maintains the triple helix structure of collagen. The relative molecular weight of the two peptide chains is For ¦Á1=123kD, ¦Á2=112kD
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Original research was done by Feng Ping, Cheng Xiaoyu, Pei Xianqing, Chen Wenhua
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