FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (7): 29-32.doi: 10.7506/spkx1002-6630-200907005

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Purification and Characterization of Bovine Bone Collagen

CHENG Xiao-yu CHEN Wen-hua PEI Xian-qing FENG Ping   

  1. (China Meat Research Center, Beijing 100068, China)
  • Received:2008-07-14 Revised:2008-06-11 Online:2009-04-01 Published:2010-12-29
  • Contact: CHENG Xiao-yu E-mail:chxyey@yahoo.com.cn

Abstract:

In this study, high-purity bone collagen was prepared from bovine bone via smashing, degreasing, decalcifying, hydrolyzing with enzyme, salting out, purifying and freeze-drying, and then its characterization was analyzed by SDS-PAGE electrophoresis, ultraviolet absorption spectrum, infrared absorption spectrum and amino acid component analysis. The results showed that the purity of the collagen product reaches 99%; it belongs to type I collagen ([α1(I)]2α2(I)) with integrated three helical structure, and the related molecular weights of its peptide chainsα1 andα2 are 123 kDa and 112 kDa, respectively.

Key words: bovine bone, collagen, purification, characterization

CLC Number: