食品科学2012，Vol.33Issue(7)：198-203,6.
重组融合蛋白MBP-BSH在大肠杆菌中的表达及其纯化、功能鉴定
Expression in Escherichia coli, Purification and Functional Characterization of Recombination Fusion Protein MBP-BSH
摘要
Abstract
The protein BSH, from Lactobacillu plantarum Y1, can form inclusion body when expressed in E. coli. The fusion tag IF2 can improve its solubility on the basis of our previous studies. In the present study, five fusion tags such as SUMO, GST, NusA, MBP and IF2 were used to improve the solubility of BSH. The results showed that an obvious protein band of MBP-BSH in the culture supernatant of recombinant E. coli Rosetta （DE3） （pLS932-BSH）was observed during the examination of SDS-PAGE. However, after induction, its solubility was greatly improved. Meanwhile, Ni-NTA resin exhibited better purification efficiency for MBP-BSH protein than Amylose resin. In addition, His-Tag linked at the C-terminal was favorable for the binding of nickel ions and as a result, MBP-BSH containing less impurities was obtained in a higher yield. The enzymatic activity of purified BSH was 2.4282 U/mg （115.14 AU/mg） as determined by ninhydrin color reaction.关键词
融合蛋白MBP-BSH/表达纯化/功能鉴定/胆盐水解酶Key words
fusion protein MBP-BSH: expression and purification: functional characterization: bile salt hydrolase分类
轻工纺织引用本文复制引用
黄茜,黄璐,潘道东,杨瑶..重组融合蛋白MBP-BSH在大肠杆菌中的表达及其纯化、功能鉴定[J].食品科学,2012,33(7):198-203,6.基金项目
江苏省高校自然科学基金项目 （）
