Kinetics of alpha-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants.
Indian J Biochem Biophys
;
2008 Oct; 45(5): 350-3
Article
Dans Anglais
| IMSEAR
| ID: sea-26600
ABSTRACT
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.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Tensioactifs
/
Cinétique
/
Chymotrypsine
/
Éthanolamine
/
Biocatalyse
/
Hydrolyse
/
Nitrophénols
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
2008
Type:
Article
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