文献类型：期刊文献

英文题名：Overexpression of Serratia marcescens lipase in Escherichia coli for efficient bioresolution of racemic ketoprofen

作者：Long, Zhang-De[1,2]; Xu, Jian-He[1]; Zhao, Li-Li[1]; Pan, Jiang[1]; Yang, Sheng[3]; Hua, Ling[4]

机构：[1] Laboratory of Biocatalysis and Bioprocessing, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China; [2] Agricultural College, Guangxi University, 100 East Daxue Road, Nanning, 530004, China; [3] Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China; [4] Department of Chemistry, Southern Methodist University, Dallas, TX 75275, United States

年份：2007

卷号：47

期号：3-4

起止页码：105

外文期刊名：Journal of Molecular Catalysis B: Enzymatic

收录：EI(收录号：20072810697310)

语种：英文

外文关键词：Biocatalysts - Enantioselectivity - Esters - Lipases - Optimization - Substrates - Surface active agents

摘要：Lipase from Serratia marcescens ECU1010 was cloned and overexpressed in E. coli. After optimization, the maximum lipase activities reached 5000-6000 U/l and this recombinant lipase could enantioselectively hydrolyze (S)-ketoprofen esters into (S)-ketoprofen. Among six alkyl esters of racemic ketoprofen investigated, this lipase showed the best enantioselectivity for the kinetic resolution of ketoprofen ethyl ester, with an eep (enantiomeric excess of product) of 91.6% and E-value of 63 obtained at 48.2% conversion. Twelve nonionic surfactants were tested for enhancing the enantioselectivity of this lipase in the bioresolution of ketoprofen ethyl ester. A very high E-value of 1084 was achieved, with an optical purity of >99% eep and a yield of 42.6% in the presence of 3% Brij 92V. Further studies showed that the selectivity of the lipase was improved with the increase of Brij 92V concentration. The substrate (ketoprofen ethyl ester) does not inhibit the lipase activity, while the product (S)-ketoprofen inhibits the lipase activity to some extent. These results indicate that the S. marcescens lipase is very useful for biocatalytic production of chiral profens such as (S)-ketoprofen. ? 2007 Elsevier B.V. All rights reserved.