文献类型：期刊文献

英文题名：One-step purification and immobilization of his-tagged protein via Ni2+-functionalized Fe3O4@polydopamine magnetic nanoparticles

作者：Yang, Jianbing[1];Ni, Kefeng[1];Wei, Dongzhi[1];Ren, Yuhong[1]

机构：[1]E China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：20

期号：5

起止页码：901

外文期刊名：BIOTECHNOLOGY AND BIOPROCESS ENGINEERING

收录：;EI(收录号：20154801619380);WOS:【SCI-EXPANDED(收录号:WOS:000365537900011)】；

基金：This project was supported by the National Natural Foundation of China (No. 21076079), the National Special Fund for State Key Laboratory of Bioreactor Engineering (No. 2060204), and the Fundamental Research Funds for the Central Universities and National Major Science.

语种：英文

外文关键词：His-tagged protein; immobilization; magnetic nanoparticles; polydopamine; purification

摘要：Ni2+-functionalized Fe3O4@polydopamine magnetic nanoparticles (Ni2+-PD-MNPs) were designed and synthesized by in situ coating of magnetic nanoparticles with polydopamine, followed by conjugation of Ni2+ to the polydopamine film. The Ni2+-PD-MNPs were used to purify His-tagged red fluorescent protein (His-RFP) via affinity interaction between Ni2+ and the His-tag. The results showed that the Ni2+-PD-MNPs had extraordinary selectivity for His-RFP purification. In addition, a Histagged transaminase (omega-transaminase BJ110) was selectively immobilized onto the Ni2+-PD-MNPs without purification, and the immobilized enzyme showed improved specific activity, as well as enhanced stability and reusability.