Engineering the Escherichia coli outer membrane protein OmpC for metal bioadsorption

被引：17

作者：

Cruz, N ^{[1
]}

Le Borgne, S ^{[1
]}

Hernández-Chávez, G ^{[1
]}

Gosset, G ^{[1
]}

Valle, F ^{[1
]}

Bolivar, F ^{[1
]}

机构：

[1] Univ Nacl Autonoma Mexico, Inst Biotecnol, Dept Mol Microbiol, Cuernavaca 62271, Morelos, Mexico

来源：

BIOTECHNOLOGY LETTERS | 2000年 / 22卷 / 07期

关键词：

Escherichia coli; genetic engineering; metal-binding; OmpC; protein engineering;

D O I：

10.1023/A:1005637920766

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The outer membrane protein, OmpC, from Escherichia coli was used to display metal-binding poly-histidine peptides on the surface of this bacterium. SDS-PAGE analysis of outer membrane protein preparations confirmed the expression of the metal-binding epitopes inserted in position 162 of the mature OmpC protein. Display of these epitopes was confirmed by epifluorescence microscopy of cells bound to Ni2+-NTA-agarose beads and metal adsorption experiments. The cells harboring one or two copies of the metal binding epitope were able to adsorb 3 to 6 times more Zn2+ (13.8 mu mol g(-1) cell), Fe3+ (35.3 mu mol g(-1) cell), and Ni2+ (9.9 mu mol g(-1) cell) metallic ions than control cells expressing the wild-type OmpC.

引用

页码：623 / 629

页数：7

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