ISSN: 0973-7510

E-ISSN: 2581-690X

Haichan Huang1, Shencong Lv1, Lei Zhao1, Ziqin Yan1, Weihong Zhong1 and Fuming Zhang2
1College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, 310032, PR China.
2Department of Biochemical Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
J Pure Appl Microbiol. 2013;7(4):3009-3015
© The Author(s). 2013
Received: 23/09/2013 | Accepted: 06/11/2013 | Published: 30/12/2013
Abstract

In the present study, a recombinant E. coli BL21 strain containing heparinase II gene was utilized to express and purify soluble heparinase II. When incubated at a low culture temperature of 22°C and in an auto-induction medium, the recombinant E. coli BL21 could successfully enhance the express of heparinase II in soluble and active forms. The purified recombinant heperinase II could eliminate heparosan in vitro completely and de-polymerized in vivo the capasule heparosan of E coli K5. Heparinase II treatment on E. coli K5 capsular polysaccharide enhanced the transformation efficiency of foreign genes into K5. It will improve the metabolic engineering operation in this strain. To our knowledge, it was first report to utilize heparinase II to eliminate K5 capsule.

Keywords

Heparinase II, heparosan, Depolymerization, Capsule, E coli K5, Gene transformation

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