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|Title:||Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants|
|Authors:||Ghosh, Kallol K|
Verma, Santosh Kumar
|Keywords:||α-Chymotrypsin;4-Nitrophenyl acetate;Hydrolysis;Micellar enzymology;Alkyldimethyl ethanolammonium bromide;Surfactants|
|Abstract:||The 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.|
|Appears in Collections:||IJBB Vol.45(5) [October 2008]|
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