Volume 17, Issue 6 pp. 717-723

Study of the mechanism of Flavobacterium sp. for hydrolyzing organophosphate pesticides

M.L. Ortiz-Hernández

M.L. Ortiz-Hernández

Laboratorio de Investigaciones Ambientales, Centro de Investigación en Biotecnología, Universidad Autónoma del Estado de Morelos, Cuernavaca Morelos, México

Search for more papers by this author
R. Quintero-Ramírez

R. Quintero-Ramírez

Laboratorio de Investigaciones Ambientales, Centro de Investigación en Biotecnología, Universidad Autónoma del Estado de Morelos, Cuernavaca Morelos, México

Search for more papers by this author
A.A. Nava-Ocampo

A.A. Nava-Ocampo

Department of Anesthesia and Respiratory Therapy, Hospital Infantil de México ‘Federico Gómez’, México DF, México

Division of Clinical Pharmacology & Toxicology, The Hospital for Sick Children, Toronto, Canada

Search for more papers by this author
A.M. Bello-Ramírez

Corresponding Author

A.M. Bello-Ramírez

Centro de Investigaciones Químicas, Universidad Autónoma del Estado de Morelos, Cuernavaca Morelos, México

Leslie Dan Faculty of Pharmacy, Molecular Design and Information Technology Center, University of Toronto, Toronto, Canada

* Correspondence and reprints: [email protected]Search for more papers by this author
First published: 18 November 2003
Citations: 57

Abstract

The biotransformation by Flavobacterium sp. of the following organophosphate pesticides was experimentally and theoretically studied: phorate, tetrachlorvinphos, methyl-parathion, terbufos, trichloronate, ethoprophos, phosphamidon, fenitrothion, dimethoate and DEF. The Flavobacterium sp. ATCC 27551 strain bearing the organophosphate-degradation gene was used. Bacteria were incubated in the presence of each pesticide for a duration of 7 days. Parent pesticides were identified and quantified by means of a gas-chromatography mass spectrum system. Activity was considered as the amount (μmol) of each pesticide degraded by Flavobacterium sp. Also, structural parameters obtained by means of the CAChe program package for biomolecules, the reactivity index of phosphorus, of oxygen at the P=O function and of sulfur at the P=S function, and lipophilicity (log Poct) (ALOGPS v. 2.0) were obtained for each pesticide. Pesticides were hydrolyzed at the bond between phosphorous and the heteroatom, producing phosphoric acid and three metabolites. Enzymatic activity was significantly explained by the following multiple linear relationship:

image
Finally, a mechanism of Flavobacterium sp. to hydrolyze pesticides was proposed.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.