Repository of Research and Investigative Information

Repository of Research and Investigative Information

Baqiyatallah University of Medical Sciences

Surface Display of Organophosphorus Hydrolase on E. coli Using N-Terminal Domain of Ice Nucleation Protein InaV

(2012) Surface Display of Organophosphorus Hydrolase on E. coli Using N-Terminal Domain of Ice Nucleation Protein InaV. Journal of Microbiology and Biotechnology. pp. 234-238. ISSN 1017-7825

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Abstract

Recombinant Escherichia coli displaying organophosphorus hydrolase (OPH) was used to overcome the diffusion barrier limitation of organophosphorus pesticides. A new anchor system derived from the N-terminal domain of ice-nucleation protein from Pseudomonas syringae InaV (InaV-N) was used to display OPH onto the surface. The designed sequence was cloned in the vector pET-28a(+) and then was expressed in E. coli. Tracing of the expression location of the recombinant protein using SDS PAGE showed the presentation of OPH by InaV-N on the outer membrane, and the ability of recombinant E. coli to utilize diazinon as the sole source of energy, without growth inhibition, indicated its significant activity. The location of OPH was detected by comparing the activity of the outer membrane fraction with the inner membrane and cytoplasm fractions. Studies revealed that recombinant E. coli can degrade 50 of 2 mM chlorpyrifos in 2 min. It can be concluded that InaV-N can be used efficiently to display foreign functional protein, and these results highlight the high potential of an engineered bacterium to be used in bioremediation of pesticide-contaminated sources in the environment.

Item Type: Article
Keywords: Ice nucleation protein organophosphorus hydrolase surface display diazinon chlorpyrifos escherichia-coli Biotechnology & Applied Microbiology Microbiology
Divisions:
Page Range: pp. 234-238
Journal or Publication Title: Journal of Microbiology and Biotechnology
Journal Index: ISI
Volume: 22
Number: 2
Identification Number: https://doi.org/10.4014/jmb.1104.04011
ISSN: 1017-7825
Depositing User: مهندس مهدی شریفی
URI: http://eprints.bmsu.ac.ir/id/eprint/6382

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