원문정보
초록
영어
Enantioselective kinetic resolution of recombinant epoxide hydrolase (EH) from a marine fish, Mugil cephalus, was investigated. The lyophilized recombinant whole-cell E. coli expressing the M. cephalus EH gene was used as the biocatalyst. The problem of instability and low solubility of styrene oxide substaret was overcome by using an organic solvent as the reaction medium. The effects of water contents, cell concentration, nature of solvent, adding the various lyoprotectants and substrate concentration on activity, stability and enantioselectivity of EH in an organic solvent were optimized. Various organic solvents with log P value between - 0.7 to 4.5 were screened as the reaction solvent. To select the most suitable lyoprotectant, the cells were lyophilized in the presence of various lyoprotectants and detergents. Enantioselective kinetic resolution of 20 mM styrene oxide was carried out in a shaking incubator at 30 ℃ and 250 rpm, and enantiopure (S)-strene oxide with 98% ee was readily obtained.