Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/2378
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dc.contributor.authorGhosh, Kallol K-
dc.contributor.authorVerma, Santosh Kumar-
dc.date.accessioned2008-11-06T04:14:55Z-
dc.date.available2008-11-06T04:14:55Z-
dc.date.issued2008-10-
dc.identifier.issn0301-1208-
dc.identifier.urihttp://hdl.handle.net/123456789/2378-
dc.description350-353en_US
dc.description.abstractThe kinetics of α-chymotrypsin (α-CT) catalyzed hydrolysis of 4-nitrophenyl acetate has been studied in aqueous solution of alkyldimethylethanolammonium bromide (cetyl, dodecyl, decyl) surfactants at concentrations below and above their critical micelle concentration. From Michaelis-Menten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of α-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJBB Vol.45(5) [October 2008]en_US
dc.subjectα-Chymotrypsinen_US
dc.subject4-Nitrophenyl acetateen_US
dc.subjectHydrolysisen_US
dc.subjectMicellar enzymologyen_US
dc.subjectAlkyldimethyl ethanolammonium bromideen_US
dc.subjectSurfactantsen_US
dc.titleKinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactantsen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.45(5) [October 2008]

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