Abstract
This paper, 2nd of our studies on the effect s of detergent components on protease activity, reports a kinetic interpretation of the enhancement of the activity by nonionic surfactants.
Initial velocity of the hydrolysis of casein was measured at 25°C and pH 10.5 for a protease of Bacillus subtilis origin and a commercial protease product in the presence of dodecyl poly (ethylene glycol) (n=7), hexadecyl poly (ethylene glycol) (n= 15) and octyloxyphenyl poly (ethylene glycol) (n=10). The enhancement of the velocity found for the systems mentioned is successfully interpreted by a kinetic scheme which takes into account the binding of the surfactant micelle to the protease. The dissociation constant of the micelle incorporated protease-casein complex is reduced to about 1/20 of the non-incorporated one, giving rise to an acceleration of the overall velocity.
