Soluble Expression and Rapid Quantification of GFP-hepA Fusion Protein in Recombinant Escherichia coli

作     者：陈银 邢新会 叶逢春 况莹 CHEN Yin;XING Xinhui;YE Fengchun;KUANG Ying

作者机构：Department of Chemical Engineering Tsinghua University Beijing 100084 China Department of Biological Sciences the University of Warwick Coventry CV4 7AL UK Department of Chemical Engineering Tsinghua University Beijing 100084 China 

出 版 物：《Chinese Journal of Chemical Engineering》 (中国化学工程学报（英文版）)

年 卷 期：2007年第15卷第1期

页      面：122-126页

核心收录：

学科分类：0710[理学-生物学] 0830[工学-环境科学与工程（可授工学、理学、农学学位）] 07[理学] 0817[工学-化学工程与技术] 071007[理学-遗传学] 0703[理学-化学] 

基　　金：Supported by the National Natural Science Foundation of China (No.20336010 and No.20176025). 

主　　题：重组体大肠杆菌 GFP-hepA融合蛋白 肝素酶 可溶性表达 快速定量分析 

摘      要：To establish a rapid quantification method for heparinase I during its production in recombinant Es-cherichia coli, a translational fusion vector was constructed by fusing the N terminus of heparinase I to the C ter-minus of a green fluorescent protein mutant (GFPmut1). As a result, not only was the functional recombinant ex-pression of heparinase I in E. coli accomplished, but also a linear correlation was obtained between the GFP fluores-cence intensity and heparinase I activity, allowing enzyme activity to be quantified rapidly during the fermentation.