文献类型：期刊文献

英文题名：Soluble expression of a novel feruloyl esterase from Burkholderia pyrrocinia B1213 in Escherichia coli and optimization of production conditions

作者：Fu, Zhilei[1,2,3]; Fan, Guangsen[1,2]; Zhu, Yuting[1,2]; Teng, Chao[1,2]; Li, Hehe[1,2]; Liu, Qian[3]; Yang, Ran[1,2]; Li, Xiuting[1,2]

第一作者：Fu, Zhilei

通讯作者：Li, Xiuting

机构：[1] Laboratory of Food Microbiology and Enzyme Engineering, Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University, Beijing, China; [2] Laboratory of Food Microbiology and Enzyme Engineering, School of Food and Health, Beijing Technology and Business University, Beijing, China; [3] Beijing Key Laboratory of Bioactive Substances and Functional Foods, College of Biochemical Engineering, Beijing Union University, Beijing, China

第一机构：Laboratory of Food Microbiology and Enzyme Engineering, Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University, Beijing, China

年份：2020

卷号：34

期号：1

起止页码：732-746

外文期刊名：Biotechnology and Biotechnological Equipment

收录：EI(收录号：20203409077941);Scopus(收录号：2-s2.0-85089469626)

语种：英文

外文关键词：Enzymes - Esters

摘要：This report examines the soluble expression of a novel feruloyl esterase, BpFae, from Burkholderia pyrrocinia in Escherichia coli overexpression systems using three expression vectors, pET28a, pCold-TF and pGEX-4T-1. BpFae was overexpressed as insoluble inclusion bodies when pET28a was used as the expression vector. BpFae was overexpressed in the soluble form when using pCold-TF; however, the overexpressed protein showed negligible activity. Recombinant BpFae was produced in the soluble form and active when E. coli cells were transformed with the pGEX-4T-1-BpFae vector. Optimal conditions for soluble overexpression of recombinant BpFae were determined, and the highest activity of recombinant BpFae was 2.54 U?mL?1. Multiple sequence alignment, phylogenetic analysis and construction of a three-dimensional model indicated that BpFae is a unique FAE from B. pyrrocinia with underlying research value. ? 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.