Much interest has been recently focused on the production of large quantities of hydrogen, due to its potential importance in our economy and needs in the petroleum and chemical industries. Formate dehydrogenase H (FDH-H) from Escherichia coli containing selenocysteine that oxidizes formate to carbon dioxide with the release of a hydrogen, is a component of the anaerobic formate hydrogen lyase complex of E. coli. In this approach, the fdhF gene was subcloned into expression vector, pET-22b(+), and a 6xHis tag was fused to FDH-H at the C-terminus and overexpressed in E. coli. However, overexpression of FDH-H in E. coli resulted in the formation of inclusion body. Several efforts including low temperature for induction and optimization of inducer concentration were tried to improve the functional expression of FDH-H.
키워드
Formate dehydrogenase Hselenocysteinebiohydrogen
저자
Young Seung SA [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
Chan Ha JUN [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
Yong Hwan KIM [ Department of Chemical Engineering, Kwangwoon University, Seoul, 139-701. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
1. 생물공학 분야의 발전을 위한 연구 협력
2. 생물공학의 실용화를 촉진시키기 위한 산학 협동
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