文献类型：期刊文献

英文题名：Soluble expression of a novel feruloyl esterase fromBurkholderia pyrrociniaB1213 inEscherichia coliand optimization of production conditions

作者：Fu, Zhilei[1,2];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, XT[1]

机构：[1]Beijing Technol & Business Univ, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Lab Food Microbiol & Enzyme Engn, Beijing, Peoples R China;[2]Beijing Technol & Business Univ, Sch Food & Hlth, Lab Food Microbiol & Enzyme Engn, Beijing, Peoples R China;[3]Beijing Union Univ, Coll Biochem Engn, Beijing Key Lab Bioact Subst & Funct Foods, Beijing, Peoples R China

第一机构：Beijing Technol & Business Univ, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Lab Food Microbiol & Enzyme Engn, Beijing, Peoples R China

通讯机构：[1]corresponding author), Beijing Technol & Business Univ, 11 Fucheng St, Beijing 100084, Peoples R China.

年份：2020

卷号：34

期号：1

起止页码：732-746

外文期刊名：BIOTECHNOLOGY & BIOTECHNOLOGICAL EQUIPMENT

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000560908500001)】；

基金：This research was supported by the National Natural Science Foundation of China (Grant Nos. 31830069, 31701592 and 31701567), General Project of Scientific Research Program of Beijing Municipal Education Commission (Grant No. KM201910011006/PXM2019_014213_000007), Beijing Natural Science Foundation (Grant No. 6164029), General Scientific Research Project of Beijing Educational Committee (Grant No. KM201811417003), Quality Construction of Talents Training/First-class Speciality Construction/Food Science and Engineering (PXM2019_014213_000010) and Science and Technology Innovation Service Capability/Construction of Provincial-level Scientific Research Platform/Beijing Advanced Innovation Center for Food Nutrition and Human Health(19008020101).

语种：英文

外文关键词：Burkholderia pyrrocinia; feruloyl esterase; optimization; pGEX-4T-1; soluble expression

摘要：This report examines the soluble expression of a novel feruloyl esterase, BpFae, fromBurkholderia pyrrociniainEscherichia colioverexpression 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 whenE. colicells 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 fromB. pyrrociniawith underlying research value.