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Appl Environ Microbiol. 1977 March; 33(3): 503-507
Copyright © 1977 American Society for Microbiology. All Rights Reserved.

Properties of an Immobilized Pesticide-Hydrolyzing Enzyme

Institut für Bodenbiologie, Forschungsanstalt für Landwirtschaft, D 3300 Braunschweig, Federal Republic of Germany

ABSTRACT

A bacterial enzyme(s) capable of hydrolyzing nine organophosphate insecticides was covalently bound to glass. The efficiency of this binding reaction ranged from 4 to 17%. Under continuous column operation, the immobilized enzyme(s) had an extrapolated half-life of 280 days. The specific activity of this glass-covalently bound hydrolase activity for parathion varied from 0.035 to 0.15 µmol/min per g of glass. The bound activity increased with decreasing glass particle size; however, the flow resistance also increased. Immobilized enzyme(s) kinetics were approximately 50% slower than those of the free enzyme(s), but there was no significant difference in the effect pH and temperature had on the activity of immobilized and free enzyme(s).