Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide SCIE SCOPUS

Cited 22 time in WEB OF SCIENCE Cited 24 time in Scopus
Title
Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide
Author(s)
Kim, HS; Lee, SJ; Lee, EJ; Hwang, JW; Park, S; Kim, SJ; Lee, EY
Publication Year
2005-12-01
Abstract
Gene mining of the genome database of the zebra fish Danio rerio revealed the presence of a putative microsomal epoxide hydrolase (mEH)-like protein containing the characteristic catalytic triad composed of ASp(223), Glu(402), and His(429) as well as the oxyanion hole common to all mEH. Based on the sequence information, a new EH gene was cloned by PCR amplification of cDNA of the zebra fish Danio rerio and expressed heterologously in Escherichia coli. The recombinant E. coli exhibited the enantiopreference toward (R)-styrene oxide with the maximum hydrolytic activity of 11.4 mu mol min(-1) (mg dcw)(-1). When the kinetic resolution was conducted with 40 mM of racemic styrene oxide, enantiopure (S)-styrene oxide was obtained with an enantiomeric excess (ee) higher than 99 and 23.5% yield at 30 min. These results demonstrate that the recombinant fish EH has the possible application as a biocatalyst for the production of enantiopure epoxides. (c) 2005 Elsevier B.V. All rights reserved.
ISSN
1381-1177
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4989
DOI
10.1016/j.molcatb.2005.09.003
Bibliographic Citation
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.37, no.1-6, pp.30 - 35, 2005
Publisher
ELSEVIER SCIENCE BV
Subject
RHODOTORULA-GLUTINIS; ENANTIOSELECTIVE HYDROLYSIS; ASPERGILLUS-NIGER; PURIFICATION; HALOHYDRINS; EXPRESSION; YEASTS; ENZYME
Keywords
enantiopure styrene oxide; Danio rerio; epoxide hydrolase; gene mining; kinetic resolution
Type
Article
Language
English
Document Type
Article
Publisher
ELSEVIER SCIENCE BV
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