文献类型：期刊文献

英文题名：Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis

作者：Li, Su-Xia[1];Ma, Qiang[1];Lin, Kang[1];Wu, Jiao-Jiao[1];Wu, Yi-Xin[2];Xu, Jian-He[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Hamamatsu Univ Sch Med, Dept Biochem, Hamamatsu, Shizuoka 4313192, Japan

年份：2014

卷号：172

期号：6

起止页码：2945

外文期刊名：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

收录：;EI(收录号：20141817658728);WOS:【SCI-EXPANDED(收录号:WOS:000334432400012)】；

基金：This work was financially supported by the National High-tech R&D (863) Program (No. 2007AA02Z225) and the National Special Fund for State Key Laboratory of Bioreactor Engineering (no. 2060204), People's Republic of China.

语种：英文

外文关键词：Lipase; Site-directed mutagenesis; Organic solvent stability; Molecular modeling; Serratia marcescens ECU1010

摘要：A novel lipase lipB from Serratia marcescens ECU1010 is highly stable in the presence of organic solvents. By sequence and structure comparison with homologous lipase lipA, three amino acid residues were found to be different between them. To identify the residues which increase the organic solvent stability of lipB, residues that potentially provide this stability were mutated to the ones of lipA at equivalent positions. The replacement of Gly at position 33 by Asp obviously decreased its stability in organic solvents. Molecular modeling and structural analysis also suggested that the Gly33 residue is important for the organic solvent stability of lipB.