Cloning,expression and enantioselective hydrolytic catalysis of a microsomal epoxide hydrolase from a marine fish, <Emphasis Type="Italic">Mugil cephalus</Emphasis> |
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| Authors: | Soo Jung Lee Hee Sook Kim Sang Jin Kim Sunghoon Park Beum Jun Kim Michael L Shuler Eun Yeol Lee |
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| Institution: | (1) Department of Food Science and Biotechnology, Kyungsung University, Busan, 608-736, Korea;(2) Marine Biotechnology Research Centre, Korea Ocean Research & Development Institute, Ansan, 426-755, Korea;(3) Department of Chemical and Biochemical Engineering, Pusan National University, Busan, 609-735, Korea;(4) School of Chemical and Biomolecular Engineering and Department of Biomedical Engineering, Cornell University, Ithaca, NY 14850-5201, USA |
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| 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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| Keywords: | cDNA cloning Enantiopure epoxides Marine fish epoxide hydrolase Mugil cephalus RACE |
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