Cloning and characterization of an epoxide hydrolase from Novosphingobium aromaticivorans SCIE SCOPUS

Cited 19 time in WEB OF SCIENCE Cited 21 time in Scopus
Title
Cloning and characterization of an epoxide hydrolase from Novosphingobium aromaticivorans
Author(s)
Woo, Jung-Hee; Kang, Ji-Hyun; Kang, Sung Gyun; Hwang, Young-Ok; Kim, Sang-Jin
KIOST Author(s)
Kang, Sung Gyun(강성균)
Publication Year
2009-04
Abstract
A gene encoding a putative epoxide hydrolase (EHase) was identified by analyzing an open reading frame of the genome sequence of Novosphingobium aromaticivorans, retaining the conserved catalytic residues such as the catalytic triad (Asp177, Glu328, and His355) and the oxyanion hole. The enantioselective EHase gene (neh) was cloned, and the recombinant EHase could be purified to apparent homogeneity by one step of metal affinity chromatography and further characterized. The purified N. aromaticivorans enantioselective epoxide hydrolase (NEH) showed enantioselective hydrolysis toward styrene oxide, glycidyl phenyl ether, epoxybutane, and epichlorohydrin. The optimal EHase activity toward styrene oxide occurred at pH 6.5 and 45A degrees C. The purified NEH could preferentially hydrolyze (R)-styrene oxide with enantiomeric excess of more than 99% and 11.7% yield after 20-min incubation at an optimal condition. The enantioselective hydrolysis of styrene oxide was also confirmed by the analysis of the vicinal diol, 1-phenyl-1,2-ethanediol. The hydrolyzing rates of the purified NEH toward epoxide substrates were not affected by as high as 100 mM racemic styrene oxide.
ISSN
0175-7598
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4312
DOI
10.1007/s00253-008-1791-9
Bibliographic Citation
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.82, no.5, pp.873 - 881, 2009
Publisher
SPRINGER
Subject
AGROBACTERIUM-RADIOBACTER AD1; CATALYTIC MECHANISM; SEQUENCE ALIGNMENT; MARINE BACTERIUM; ENCODING GENE; EXPRESSION; ENANTIOSELECTIVITY; ERYTHROBACTER; HYDROLYSIS; ESTERASE
Keywords
Epoxide hydrolase; Enantioselectivity; Diol configuration; Genome
Type
Article
Language
English
Document Type
Article
Publisher
SPRINGER
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