Reduced thermal inactivation of trypsin and marugoto e by high-pressure treatment

Abstract

To evaluate the effect of high-pressure treatment on thermal inactivation of proteases, two mesophilic model proteases, trypsin and Marugoto E, that showed pressure-tolerance against an isobaric-isothermal treatment at 300 MPa and 37°C were determined for the kinetics of thermal inactivation at appropriate time intervals for 1 h at 300 MPa and ambient pressure in 0.5 and 2.5 mg/mL concentrations, respectively. At all heating temperatures and time of heat-treatment, the residual activities of trypsin and Marugoto E solutions that were heat-treated at high pressure were significantly higher than those of the same solutions that were heat-treated at ambient pressure. First-order reaction rate constants for thermal inactivation of the enzymes at high pressure were significantly smaller than those at ambient pressure, which led to considerable decreases in activation energies of the enzyme reactions.