Development of a recombinant marine fish epoxide hydrolase and enantioselective resolution of racemic styrene oxide

Rapid amplification of cDNA ends (RACE) techniques were used to prepare the cDNA library for the cloning of epoxide hydrolase gene from Mugil cephalus (mMCEH). The characteristic catalytic triad composed of Asp238, Glu417 and His444 and two tyrosine residue were highly conserved. The cloned mMCEH gene was expressed heterologously in Escherichia coli, and the recombinant cells showed the enantiopreference toward (R)-styrene oxide. When the batch kinetic resolution was conducted with 50 mM racemic styrene oxide, we obtainedeantiopure (S)-styrene oxide with high enantiopurity of more than 99 % enantiomeric excess (ee) and 15.4 % yield. Acknowledgement : This work was supported by the Marine and Extreme Genome Research Center Program, Ministry of Marine Affairs and Fisheries, Republic of Korea.