Utilization of One Novel Microbial Esterase WDEst9 in the Kinetic Resolution of (5)-Methyl 2-chloropropionate and (5)-Ethyl 2-chloropropionate
作者机构：CAS Key Laboratory of Tropical Marine Bio-Resources and EcologySouth China Sea Institute of OceanologyChinese Academy of SciencesGuangzhou 510301P.R.China Guangdong Key Laboratory of Marine Materia MedicaSouth China Sea Institute of OceanologyChinese Academy of SciencesGuangzhou 510301P.R.China Affiliated Hospital of Shandong University of Traditional Chinese MedicineJinan 250014P.R.China
出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)
年 卷 期：2019年第35卷第5期
页 面：830-836页
核心收录：
基 金：Supported by the Scientific and Technological Project of Ocean and Fishery from Guangdong Province,China the Senior User Project of RV KEXUE the Priority Research Program of the Chinese Academy of Sciences,China
主 题：Biocatalysis Novel esterase Asymmetric hydrolysis Complementary enantio-preference (5)-Methyl 2-chloropropionate (S)-Ethyl 2-chloropropionate
摘 要：One novel microbial esterase WDEst9 from Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085 was functionally characterized and the results demonstrated that the enantio-preference of WDEst9 was opposite to that of three other microbial esterases(BSE01701, PHE14 and Bae02030) in the kinetic resolution of racemic methyl lactate. We further investigated the potential of esterase WDEst9 in the kinetic resolution of both (±)-methyl 2-chloropropionate and (±)-ethyl 2-chioropropionate. The enantio-preference of WDEst9 was also interestingly opposite to that of esterases EST 12-7 and EstC10, and generated (S)-methyl 2-chloropropionate and (S)-ethyl 2-chloropropionate with high enantiomeric excess(both e.e.98%) and high yield after many iterations of process optimization. Through genome mining, microbial esterase WDEst9 was characterized to be a novel esterase which may provide valuable complementary enantio-selectivity and possesses very good potential in the kinetic resolution of high value-added chiral chemicals.
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