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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.