The effect of high pressure on the rates of proteolytic hydrolysis. II. Trypsin

Abstract

The interpretation of the volume change of activation for varying conditions of proteolytic hydrolysis is discussed. A volume change of activation of −36 ml. was calculated from the acceleration of the rate of hydrolysis of β-lactoglobulin by crystalline trypsin. While the rates of hydrolysis of α-benzoyl- l-argininamide and α-benzoyl- l-arginine isopropyl ester were unaffected by pressures of 8000 lb./in. 2, the hydrolysis of l-arginine methyl ester was slightly accelerated, the volume change of activation being −6 ml. At 54.5 °C. and pH 8.1 high pressures accelerate the hydrolysis of α-benzoyl- l-argininamide by crystalline trypsin indicating that heat inactivation is retarded at higher pressures.