Kinetics of alpha-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants.
The kinetics of alpha-chymotrypsin (alpha-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-Mcnten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of alpha-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate.