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Utilization of One Novel Microbial Esterase WDEst9 in the Kinetic Resolution of (5)-Methyl 2-chloropropionate and (5)-Ethyl 2-chloropropionate 被引量:2
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作者 WANG Yilong XU Yongkai +2 位作者 ZHANG Yun SUN Aijun HU Yunfeng 《Chemical Research in Chinese Universities》 SCIE CAS CSCD 2019年第5期830-836,共7页
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 th... 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. 展开更多
关键词 BIOCATALYSIS NOVEL ESTERASE Asymmetric HYDROLYSIS Complementary enantio-preference (5)-Methyl 2-chloropropionate (S)-Ethyl 2-chloropropionate
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