Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase

  1. Mark Shimazu1,2,
  2. Ashok Mulchandani1,*,
  3. Wilfred Chen1,*

Article first published online: 12 NOV 2001

DOI: 10.1002/bit.10095

Issue

Biotechnology and Bioengineering

Biotechnology and Bioengineering

Volume 76, Issue 4, pages 318–324, December 2001

Additional Information

How to Cite

Shimazu, M., Mulchandani, A. and Chen, W. (2001), Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase. Biotechnol. Bioeng., 76: 318–324. doi: 10.1002/bit.10095

Author Information

  1. 1

    Department of Chemical and Environmental Engineering, University of California, Riverside, California 92521, USA; fax: 909-787-2425

  2. 2

    Environmental Toxicology Program, University of California, Riverside, California 92521, USA; fax: 909-787-2425

*Department of Chemical and Environmental Engineering, University of California, Riverside, California 92521, USA; fax: 909-787-2425

Publication History

  1. Issue published online: 12 NOV 2001
  2. Article first published online: 12 NOV 2001
  3. Manuscript Accepted: 10 AUG 2001
  4. Manuscript Received: 2 APR 2001

Funded by

  • National Science Foundation
  • U.S. Environmental Protection Agency
  • UC Toxic Substances Teaching and Research Program. Grant Numbers: BES9731513, R827227

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

Get PDF (195K)

Keywords:

  • detoxification;
  • nerve agents;
  • OPH;
  • organophosphates;
  • decontamination

Abstract

Moraxella sp., a native soil organism that grows on p-nitrophenol (PNP), was genetically engineered for the simultaneous degradation of organophosphorus (OP) pesticides and p-nitrophenol (PNP). The truncated ice nucleation protein (INPNC) anchor was used to target the pesticide-hydrolyzing enzyme, organophosphorus hydrolase (OPH), onto the surface of Moraxella sp., alleviating the potential substrate uptake limitation. A shuttle vector, pPNCO33, coding for INPNC–OPH was constructed and the translocation, surface display, and functionality of OPH were demonstrated in both E. coli and Moraxellasp. However, whole cell activity was 70-fold higher in Moraxellasp. than E. coli. The resulting Moraxella sp. degraded organophosphates as well as PNP rapidly, all within 10 h. The initial hydrolysis rate was 0.6 μmol/h/mg dry weight, 1.5 μmol/h/mg dry weight, and 9.0 μmol/h/mg dry weight for methyl parathion, parathion, and paraoxon, respectively. The possibility of rapidly degrading OP pesticides and their byproducts should open up new opportunities for improved remediation of OP nerve agents in the future. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 76: 318–324, 2001.

Get PDF (195K)