Enantioselective hydrolysis of racemic epichlorohydrin using an epoxide hydrolase from Novosphingobium aromaticivorans.
Previously we reported that an epoxide hydrolase (EHase) from Novosphingobium aromaticivorans could preferentially hydrolyze (R)-styrene oxide. In this study, we demonstrate that the purified NEH could be also effective in chiral resolution of racemic epichlorohydrin (ECH). Particularly, the purified NEH showed excellent hydrolyzing activity toward ECH to complete the reaction at a short period of incubation time. Enantiopure (S)-ECH could be obtained with a high enantiopurity of more than 99.99% enantiomeric excess (ee) and yield of 20.7% (theoretical, 50%). The chiral resolution of the purified NEH toward ECH was not susceptible to substrate inhibition by 500 mM racemic ECH.
Woo
Jung-Hee
JH
Marine Biotechnology Research Center, Korea Ocean Research & Development Institute, Ansan, P. O. Box 29, 425-600, Korea.
Hwang
Young-Ok
YO
Kang
Ji-Hyun
JH
Lee
Hyun Sook
HS
Kim
Sang-Jin
SJ
Kang
Sung Gyun
SG
D020561:Alphaproteobacteria / Q000201:enzymology*; D004811:Epichlorohydrin / Q000138:chemical synthesis*; D004851:Epoxide Hydrolases / Q000737:chemistry*; D004852:Epoxy Compounds / Q000737:chemistry*; D013237:Stereoisomerism
D004852:Epoxy Compounds; D004811:Epichlorohydrin; D004851:Epoxide Hydrolases