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Screening enantioselective epoxide hydrolase activities from marine microorganisms: detection of activities in Erythrobacter spp
Hwang, Y.-O.; Kanga, S.-G.; Woo, J.-H.; Kwon, K.K.; Sato, T.I.; Lee, E.Y.; Han, M.S.; Kim, S.-J. (2008). Screening enantioselective epoxide hydrolase activities from marine microorganisms: detection of activities in Erythrobacter spp. Mar. Biotechnol. 10(4): 366-373. https://dx.doi.org/10.1007/s10126-007-9070-9
In: Marine Biotechnology. Springer-Verlag: New York. ISSN 1436-2228; e-ISSN 1436-2236, more
Peer reviewed article  

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Keywords
    Peptides > Proteins > Enzymes > Hydrolases > Epoxide hydrolase
    Screening
    Marine/Coastal
Author keywords
    screening; epoxide hydrolase; marine microorganism; Erythrobacter

Authors  Top 
  • Hwang, Y.-O.
  • Kanga, S.-G.
  • Woo, J.-H.
  • Kwon, K.K.
  • Sato, T.I.
  • Lee, E.Y.
  • Han, M.S.
  • Kim, S.-J.

Abstract
    To develop an enantioselective epoxide hydrolase (EHase) from marine microorganisms, marine samples were collected from a variety of marine environments. Strains isolated by the capability of living on styrene oxide (SO) were screened for retaining enantioselective EHase activities toward SO by combining spectrophotometric, GC, and HPLC analysis. Consequently, one strain, JCS358, was selected, and the sequence analysis of 16S rRNA gene showed that the strain belonged to Erythrobacter cluster. Twelve additional Erythrobacter strains from this study or acquired from culture collections were thereby tested for displaying EHase activities, and most of tested strains showed enantioselective hydrolysis toward SO and glycidyl phenyl ether. Kinetic resolution of racemic SO using whole cell of Erythrobacter sp. JCS358 was performed. Enantiopure (S)-SO could be obtained with an enantiomeric excess (ee) higher than 99% after 15 h incubation. The determination of 1-phenyl-1,2-ethanediol configuration derived from racemic SO confirmed the enantioselective hydrolyzing activity of Erythrobacter sp. JCS358.

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