ISSN:
0006-3592
Keywords:
enzyme treatment
;
parathion hydrolase
;
pesticide treatment
;
toxic wastes
;
waste minimization
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The increasing amounts of pesticides used throughout the world, as well as the increasingly stringent governmental regulations concerning waste disposal, mandates improved techniques of waste disposal and minimization. In this article, parathion hydrolase, an enzyme with proven effectiveness at hydrolyzing organophosphates, was used to treat a cattle dipping liquid containing the pesticide, coumaphos, which is used to kill a disease-causing tick. Waste is generated from this process when a toxic dechlorination product of coumaphos, potasan, accumulates to concentrations hazardous to the cattle. This pesticide system was used as a model to demonstrate how enzyme technology can be applied to waste treatment and minimization. Kinetic experiments showed that the hydrolysis of the two organophosphate substrates can be modeled as first-order reactions with identical rate constants. It was further shown that the enzyme is capable of hydrolyzing only dissolved substrates. Because of the eightfold greater solubility of potasan than coumaphos (16.9 vs. 2.2 μmol/L), it was possible to utilize the enzyme to hydrolyze potasan selectively. Thus, by limiting the amount of enzyme, it is possible to remove potasan selectively to extend the lifetime of the cattle dipping liquid, thereby reducing the amount of waste generated. Based upon experimental results, a mathematical model describing the system was developed and verified. The mathematical model was then used to simulate the ability of the enzyme to hydrolyze the total amount of organophosphates, and to degrade selectively all of the toxic potasan without a significant loss of coumaphos.
Additional Material:
10 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260390707
Permalink
