Abstract
The cDNA of a marine fish microsomal epoxide hydrolase (mEH) gene from Mugil cephalus was cloned by rapid amplification of cDNA ends (RACE) techniques. The homology model for the mEH of M. cephalus showed a characteristic structure of α/β-hydrolase-fold main domain with a lid domain over the active site. The characteristic catalytic triad, consisting of Asp(238), His(444), and Glu(417), was highly conserved. The cloned mEH gene was expressed in Escherichia coli and the recombinant mEH exhibited (R)-preferred hydrolysis activity toward racemic styrene oxide. We obtained enantiopure (S)-styrene oxide with a high enantiopurity of more than 99% enantiomeric excess and yield of 15.4% by batch kinetic resolution of 20 mM racemic styrene oxide.
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Acknowledgement
This work was supported by the Marine and Extreme Genome Research Center Program, Ministry of Marine Affairs and Fisheries, Republic of Korea. Professor E. Y. Lee as a visiting scholar at Cornell University was financially supported by LG Yeonam Foundation via Oversea Professor Program and Kyungsung University.
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Lee, S.J., Kim, H.S., Kim, S.J. et al. Cloning, expression and enantioselective hydrolytic catalysis of a microsomal epoxide hydrolase from a marine fish, Mugil cephalus . Biotechnol Lett 29, 237–246 (2007). https://doi.org/10.1007/s10529-006-9222-4
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DOI: https://doi.org/10.1007/s10529-006-9222-4