title: Identification and characterization of epoxide hydrolase activity of polycyclic aromatic hydrocarbon-degrading bacteria for biocatalytic resolution of racemic styrene oxide and styrene oxide derivatives.
abstract: A novel epoxide hydrolase (EHase) from polycyclic aromatic hydrocarbon (PAH)-degrading bacteria was identified and characterized. EHase activity was identified in four strains of PAH-degrading bacteria isolated from commercial gasoline and oil-contaminated sediment based on their growth on styrene oxide and its derivatives, such as 2,3- and 4-chlorostyrene oxides, as a sole carbon source. Gordonia sp. H37 exhibited high enantioselective hydrolysis activity for 4-chlorostyrene oxide with an enantiomeric ratio of 27. Gordonia sp. H37 preferentially hydrolyzed the (R)-enantiomer of styrene oxide derivatives resulting in the preparation of a (S)-enantiomer with enantiomeric excess greater than 99.9 %. The enantioselective EHase activity was identified and characterized in various PAH-degrading bacteria, and whole cell Gordonia sp. H37 was employed as a biocatalyst for preparing enantiopure (S)-styrene oxide derivatives.
authors.affiliation: Gyeongbuk Institute for Marine Bio-Industry (GIMB), Uljin, Gyeongbuk 767-813, Republic of Korea. jhwoo@gimb.or.kr
authors.forename: Jung-Hee
authors.initials: JH
authors.lastname: Woo
authors.forename: Tae-Hyung
authors.initials: TH
authors.lastname: Kwon
authors.forename: Jun-Tae
authors.initials: JT
authors.lastname: Kim
authors.forename: Choong-Gon
authors.initials: CG
authors.lastname: Kim
authors.forename: Eun Yeol
authors.initials: EY
authors.lastname: Lee
mesh_terms: D001419:Bacteria / Q000201:enzymology* / Q000302:isolation & purification / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism; D004851:Epoxide Hydrolases / Q000378:metabolism*; D004852:Epoxy Compounds / Q000378:metabolism*; D019015:Geologic Sediments / Q000382:microbiology; D006868:Hydrolysis
chemical_list: D004852:Epoxy Compounds; D002244:Carbon; C013690:styrene oxide; D004851:Epoxide Hydrolases