Marine Biotechnology Research Center, Korea Ocean Research & Development Institute, Ansan, P. O. Box 29, 425-600, Korea.
J Biosci Bioeng. 2010 Sep;110(3):295-7. doi: 10.1016/j.jbiosc.2010.02.014. Epub 2010 Mar 17.
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.
此前我们报道过，一种来自芳香环丛菌的环氧化物水解酶（EHase）可以优先水解（R）-苯乙烯氧化物。在本研究中，我们证明了纯化后的 NEH 也可以有效地对消旋表氯醇（ECH）进行手性拆分。特别是，纯化后的 NEH 对 ECH 具有出色的水解活性，可在短孵育时间内完成反应。可以获得对映体纯的（S）-ECH，其对映体过量（ee）值大于 99.99%，收率为 20.7%（理论值为 50%）。纯化后的 NEH 对 ECH 的手性拆分不受 500mM 消旋 ECH 底物抑制的影响。
