Rhodobacterales bacterium HTCC2654로 부터 신규 Epoxide Hydrolase의 광학특이성 분석

Abstract

Genes encoding putative epoxide hydrolases (EHases) were identified by analyzing open reading frames (ORFs) of several marine microorganisms whose genome sequences are available in public. The 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. The optimal pH and temperature for the EHase activity of the purified REH were pH 7.0 and 40℃, respectively. The purified REH was highly enantioselective toward racemic styrene oxide. Acknowledgement: This work was supported by KORDI in-house program (PE98230) and the Marine and Extreme Genome Research Center Program, Ministry of Marine Affairs and Fisheries.