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Optimal Expression, Purification and Renaturation of BMP-2 in E.coli BL 21(DE3)

YANG Chun-yu 1,YANG Chun-li2,LIU Xiao-fei1,HE Mei1   

  1. 1. Key Laboratory of Food Science and Engineering of Heilongjiang Province, College of Food Engineering, Harbin University of
    Commerce, Harbin 150076, China; 2. College of Light Industry, Harbin University of Commerce, Harbin 150028, China
  • Online:2013-08-15 Published:2013-09-03
  • Contact: YANG Chun-yu

Abstract:

The plasmid pET28a-BMP-2 based on the target gene of bone morphogenetic protein-2 (BMP-2) from E.coli
harboring plasmid BMP-2cDNA was transformed into E.coli BL 21(DE3). The successful expression of BMP-2 in E.coli BL
21(DE3) was identified by enzymatic digestion. Under optimized expression conditions, BMP-2 was purified and renaturated
to obtain enhanced bioactivity. This study provides a cost-effective way of producing BMP-2, which is expensive and
needed in large quantities in bone repair materials and investigation of its sustained release capacity.

Key words: bone morphogenetic protein -2, inducement expression, pet-28 a(+), purification, renaturation

CLC Number: