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Previously we reported that the epoxide hydrolases (EHase) from Rhodobacterales bacterium HTCC2654 was cloned and expressed in E. coli. The recombinant EHase (rREH) was purified by metal affinity chromatography and further characterized (toward racemic glycidyl phenyl ether (rGPE). In this study, we could demonstrate that the purified REH was also highly enantioselective toward racemic styrene oxide derivatives (2, 3, 4-chlorostyrene oxide, 4-nitrostyrene oxide, and 2-methylstyrene oxide). Enantiopure styrene oxide derivatives are a
valuable epoxide intermediate for preparing optically active pharmaceuticals. The purified REH could be applied to bioprocess for providing valuable pharmaceutical intermediates. Acknowledgement: This work was supported by the Marine and Extreme Genome Research Center Program, Ministry of Land, Transport and Maritime Affairs, Republic of Korea.