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영어

The analysis of conserved amino acid residues of epoxide hydrolase gene (EH) of Mugil cephalus revealed that the active site is composed of Asp199, Glu378 and His405 and two tyrosines. The Glu378 residue in the active site was replaced by an aspartic acid using site-directed mutagenesis. The mutated gene was successfully expressed in Escherichia coli. The recombinant E. coli exhibited the enantioperference toward (R)-styrene oxide when racemic styrene oxide was supplied as the substrate, and the final yield was increased up to 28.6 %.
Acknowledgement : This work was supported by the Marine and Extreme Genome Research Center Program, Ministry of Marine Affairs and Fisheries, Republic of Korea.