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Indian J Biochem Biophys ; 2011 Feb; 48(1): 29-34
Article in English | IMSEAR | ID: sea-135297


Bacterial organophosphate hydrolases (OPH) have been shown to hydrolyze structurally diverse group of organophosphate (OP) compounds and nerve agents. Due to broad substrate range and unusual catalytic properties, the OPH has successfully been used to develop eco-friendly strategies for detection and decontamination of OP compounds. However, their usage has failed to gain necessary acceptance, due to short half-life of the enzyme and loss of activity during process development. In the present study, we report a simple procedure for immobilization of OPH on biocompatible gelatin pads. The covalent coupling of OPH using glutaraldehyde spacer has been found to dramatically improve the enzyme stability. There is no apparent loss of OPH activity in OPH-gelatin pads stored at room temperature for more than six months. As revealed by a number of kinetic parameters, the catalytic properties of immobilized enzyme are found to be comparable to the free enzyme. Further, the OPH‑gelatin pads effectively eliminate OP insecticide methyl parathion and nerve agent sarin.

Enzyme Stability , Enzymes, Immobilized/chemistry , Escherichia coli/enzymology , Escherichia coli/genetics , Gelatin/chemistry , Hydrolysis , Insecticides/poisoning , Methyl Parathion/chemistry , Organophosphorus Compounds/chemistry , Phosphoric Monoester Hydrolases/genetics , Phosphoric Monoester Hydrolases/isolation & purification , Phosphoric Monoester Hydrolases/metabolism , Sarin/chemistry , Substrate Specificity