Engineering the Escherichia coli outer membrane protein OmpC for metal bioadsorption |
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Authors: | Norberto Cruz Sylvie Le Borgne Georgina Hernández-Chávez Guillermo Gosset Fernando Valle Francisco Bolivar |
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Institution: | (1) Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Apdo. Postal 510-3, Cuernavaca, Morelos, CP 62271, Mexico |
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Abstract: | 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 mol g–1 cell), Fe3+ (35.3 mol g–1 cell), and Ni2+ (9.9 mol g–1 cell) metallic ions than control cells expressing the wild-type OmpC. |
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Keywords: | Escherichia coli genetic engineering metal-binding OmpC protein engineering |
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