Pressure inactivation of enzyme : some kinetic aspects of pressure inactivation of trypsin

Abstract

The inactivation process of trypsin by high pressure of 5000-10000kg/cm^2 has been examined kinetically at temperature of 15-45℃. The results art as follows; the inactivation of trypsin increases with pressure increase, but above the critical pressure (about 8000 kg/cm^2) no more inactivation occurs. The process of inactivation is of the first order kinetics, and thermodynamic quantities of inactivation process are similar to the protein denaturation of ovalbumin and hemoglobin by pressure except the sign of enthalpy of activation, i.e. ΔF≠>0, ΔH≠>0, ΔS≠<0, ΔV≠<0.