期刊
CHEMICAL COMMUNICATIONS
卷 57, 期 36, 页码 4460-4463出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc01575c
关键词
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资金
- ScholarshChinaip Council (CSC) [201708330279, 201708330280]
- Bundesministerium fur Bildung und Forschung'' (BMBF) [FKZ: 031B0297]
This study presents a facile and reversible method to immobilize a wide range of His(6)-tagged proteins on the E. coli cell surface through Fe(iii)-metal complexes. Successfully, an eGFP and four enzymes with His(6)-tag were immobilized on the cell surface. Moreover, a hydrogel sheath around E. coli cells was generated by immobilizing the His(6)-tagged HRP.
We report a facile and reversible method to immobilize a broad range of His(6)-tagged proteins on the E. coli cell surface through Fe(iii)-metal complexes. A His(6)-tagged eGFP and four His(6)-tagged enzymes were successfully immobilized on the cell surface. Additionally, a hydrogel sheath around E. coli cells was generated by immobilized His(6)-tagged HRP.
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