Immobilization of organophosphate hydrolase on biocompatible gelatin pads and its use in removal of organophosphate compounds and nerve agents.

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dc.contributor.authorKanugula, Anantha KoteswaraRao
dc.contributor.authorRepalle, Elisha Raju
dc.contributor.authorPandey, Jay Prakash
dc.contributor.authorSripad, Gunwar
dc.contributor.authorMitra, Chanchal Kumar
dc.contributor.authorDubey, Devender Kumar
dc.contributor.authorSiddavattam, Dayananda
dc.date.accessioned2011-11-15T08:14:04Z
dc.date.available2011-11-15T08:14:04Z
dc.date.issued2011-02
dc.description.abstractBacterial 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.en_US
dc.identifier.citationKanugula 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.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/135297
dc.language.isoenen_US
dc.source.urihttps://nopr.niscair.res.in/bitstream/123456789/11102/4/IJBB%2048%281%29%2029-34.pdfen_US
dc.subjectOrganophosphatesen_US
dc.subjectOrganophosphorus hydrolase (OPH)en_US
dc.subjectEnzyme immobilizationen_US
dc.subjectDetoxificationen_US
dc.subjectSarinen_US
dc.subjectMethyl parathionen_US
dc.subjectGelatinen_US
dc.subject.meshEnzyme Stability
dc.subject.meshEnzymes, Immobilized --chemistry
dc.subject.meshEscherichia coli --enzymology
dc.subject.meshEscherichia coli --genetics
dc.subject.meshGelatin --chemistry
dc.subject.meshHydrolysis
dc.subject.meshInsecticides --poisoning
dc.subject.meshMethyl Parathion --chemistry
dc.subject.meshOrganophosphorus Compounds --chemistry
dc.subject.meshPhosphoric Monoester Hydrolases --genetics
dc.subject.meshPhosphoric Monoester Hydrolases --isolation & purification
dc.subject.meshPhosphoric Monoester Hydrolases --metabolism
dc.subject.meshSarin --chemistry
dc.subject.meshSubstrate Specificity
dc.subject.otherPhosphoric Monoester Hydrolases --chemistry
dc.titleImmobilization of organophosphate hydrolase on biocompatible gelatin pads and its use in removal of organophosphate compounds and nerve agents.en_US
dc.typeArticleen_US
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