生物技术通报2016，Vol.32Issue(3)：178-183,6.DOI:10.13560/j.cnki.biotech.bull.1985.2016.03.028
漆酶N端融合His-tag或S-tag标签促进其在大肠杆菌中可溶性表达
Promotion of Soluble Expression of Laccase inEscherichia coliby Fusion of His-tag or S-tag on the N-terminal of It
摘要
Abstract
Laccase fromBacillus licheniformis has the advantages of high catalytic efficiency,wide range of substrates,etc.,thus it owns the broad application prospect in industrial and agricultural fields. However,the expression level of the enzyme in the foreign gene expression system is low,which greatly limits its application in the agricultural and industrial fields. His-tag or S-tag is the small peptide with low molecular weight and usually can not affect the characteristics of heterologous fusion protein,and they are beneficial to be applied in the purification and detection of heterologous proteins. In this study,fusion of His-tag and/or S-tag on the N-terminal of the laccase CotA fromB. licheniformiswas constructed into pET-22b vector,and the vector was transferred intoEscherichia coliBL(DE3),then we found that the soluble expression level of laccase significantly increased inE. coliBL(DE3). Compared with the construction without no fusion of any tags on N-terminal,the expression level with His-tag was about 37 folds,20 folds with S-tag,and 28 folds with both His-tag and S-tag,respectively.关键词
漆酶/His-tag/S-tag/高效表达Key words
laccase/His-tag/S-tag/high expression引用本文复制引用
岳青霞,张丽洁,田健,伍宁丰,姚冬生..漆酶N端融合His-tag或S-tag标签促进其在大肠杆菌中可溶性表达[J].生物技术通报,2016,32(3):178-183,6.基金项目
国家“863”计划项目 （）
