文献类型：期刊文献

英文题名：Characterization of an ene-reductase from Meyerozyma guilliermondii for asymmetric bioreduction of α,β-unsaturated compounds

作者：Zhang, Baoqi[1];Zheng, Liandan[1];Lin, Jinping[1];Wei, Dongzhi[1]

机构：[1]East China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2016

卷号：38

期号：9

起止页码：1527

外文期刊名：BIOTECHNOLOGY LETTERS

收录：;EI(收录号：20162202445022);WOS:【SCI-EXPANDED(收录号:WOS:000382008200014)】；

基金：This work was financially supported by the National Key Basic Research Development Program of China ("973" Program, No. 2012CB721003), the Natural Science Foundation of China (No. 21276084), Shanghai Natural Science Foundation (No. 15ZR1408600) and National Major Science and Technology Projects of China (No. 2012ZX09304009).

语种：英文

外文关键词：Bioreduction; (R)-Carvone; Dihydrocarvone; Ene-reductase; NADPH dehydrogenase; Old yellow enzyme; alpha,beta-Unsaturated compounds

摘要：To characterize a novel ene-reductase from Meyerozyma guilliermondii and achieve the ene-reductase-mediated reduction of activated C=C bonds. The gene encoding an ene-reductase was cloned from M. guilliermondii. Sequence homology analysis showed that MgER shared the maximal amino acid sequence identity of 57 % with OYE2.6 from Scheffersomyces stipitis. MgER showed the highest specific activity at 30 A degrees C and pH 7 (100 mM sodium phosphate buffer), and excellent stereoselectivities were achieved for the reduction of (R)-carvone and ketoisophorone. Under the reaction conditions (30 A degrees C and pH 7.0), 150 mM (R)-carvone could be completely converted to (2R,5R)-dihydrocarvone within 22 h employing purified MgER as catalyst, resulting in a yield of 98.9 % and an optical purity of > 99 % d.e. MgER was characterized as a novel ene-reductase from yeast and showed great potential for the asymmetric reduction of activated C=C bonds of alpha,beta-unsaturated compounds.