文献类型：期刊文献

英文题名：Biocatalytic resolution of nitro-substituted phenoxypropylene oxides with Trichosporon loubierii epoxide hydrolase and prediction of their enantiopurity variation with reaction time

作者：Xu, Y; Xu, JH; Pan, J; Zhao, L; Zhang, SL

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biocatalysis & Bioproc, Shanghai 200237, Peoples R China

年份：2004

卷号：27

期号：4-6

起止页码：155

外文期刊名：JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000220344900002)】；

语种：英文

外文关键词：nitro-substituted plienoxypropylene oxide; Trichosporon loubierii; epoxide hydrolase; kinetic resolution; theoretical prediction; enantioselective hydrolysis

摘要：Biocatalytic resolution of 3-(2'-nitrophenoxy)propylene oxide (1a), 3-(3'-nitrophenoxy)propylene oxide (1b) and 3-(4'-nitrophenoxy)propylene oxide (1c) were exploited by using lyophilized cells of yeast Trichosporon loubierii ECU1040 with epoxide hydrolase (EH) activity, which preferentially hydrolyzes (S)-enantiomers of the epoxides (1a-c), yielding (S)-diols and (R)-epoxides. The activity increased as the nitro group in the phenyl ring was shifted from 4'-position (1c) to T-position (1a). When the substrate concentration of la was increased from 10 to 80 mM. the E-value increased at first, until reaching a peak at 40 mM, and then decreased at higher concentrations (>40 mM). The optically active epoxide (R)-1a was prepared at gram-scale (97% ee, 41% yield). Furthermore, a simple method was developed to predict the enantiomeric excess of substrate (ee(s)) at any time of the whole reaction course based on the ee(s) value determined at a certain reaction time at a relatively lower substrate concentration. This will be helpful for terminating the reaction at a proper time to get both higher optical purity and higher yield of the remaining epoxides. (C) 2003 Elsevier B.V. All rights reserved.