Immobilization of organophosphate hydrolase on biocompatible gelatin pads and its use in removal of organophosphate compounds and nerve agents.
Loading...
Date
2011-02
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
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.
Description
Keywords
Organophosphates, Organophosphorus hydrolase (OPH), Enzyme immobilization, Detoxification, Sarin, Methyl parathion, Gelatin
Citation
Kanugula Anantha KoteswaraRao, Repalle Elisha Raju, Pandey Jay Prakash, Sripad Gunwar, Mitra Chanchal Kumar, Dubey Devender Kumar, Siddavattam Dayananda. Immobilization of organophosphate hydrolase on biocompatible gelatin pads and its use in removal of organophosphate compounds and nerve agents. Indian Journal of Biochemistry & Biophysics. 2011 Feb; 48(1): 29-34.