文献类型：期刊文献

英文题名：Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration

作者：Cui, Zhi-Mei[1];Zhang, Jian-Dong[1];Fan, Xiao-Jun[1];Zheng, Gao-Wei[2];Chang, Hong-Hong[1];Wei, Wen-Long[1]

机构：[1]Taiyuan Univ Technol, Dept Biol & Pharmaceut Engn, Coll Chem & Chem Engn, 79 West Yingze St, Taiyuan 030024, Shanxi, Peoples R China;[2]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomanufacture, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China

年份：2017

卷号：243

起止页码：1

外文期刊名：JOURNAL OF BIOTECHNOLOGY

收录：;EI(收录号：20170103210585);WOS:【SCI-EXPANDED(收录号:WOS:000393929100001)】；

基金：This work was financially supported by the Qualified Personnel Foundation of Taiyuan University of Technology (grant No. tyut-rc201484a), the Youth Foundation of Taiyuan University of Technology (grant No.1205-0020202) and the Scientific and Technological Innovation Programs of Higher Education Institutions in Shanxi (STIP) (grant No. 2015132).

语种：英文

外文关键词：Highly enantioselective; Carbonyl reductase; 2-Hydroxyacetophenone; Chiral 1-phenyl-1,2-ethanediol; Cofactor regeneration

摘要：Optically pure 1-phenyl-1,2-ethanediol is a very important chiral building block and intermediate in fine chemical and pharmaceutical industries. Reduction of 2-hydroxyacetophenone provides a straightforward approach to access these important compounds. In this study, two enantiocomplementary carbonyl reductases, BDHA (2,3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) were discovered for the first time to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) and (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, respectively. The two enzymes were purified and characterized. In vitro bioreduction of 2 -HAP catalyzed by BDHA and GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration were demonstrated, affording both (R)-PED and (S)-PED in >99% ee and 99% conversion. Recombinant Escherichia coli whole cells co-expressing both GDH and BDHA or GoSCR genes were used to asymmetric reduction of 2 -HAP to (R)-PED or (S)-PED. Under the optimized conditions, the bioreduction of 400 nM (54 g/L) substrate was proceeded smoothly without the external addition of cofactor, and the product (R)-PED and (S)-PED were obtained with 99% yield, >99% ee and 18.0 g/L/h volumetric productivity. These results offer a practical biocatalytic method for the preparation of both (R)-PED and (S)-PED with high volumetric productivity. (C) 2016 Elsevier B.V. All rights reserved.