High-Temperature Short-Time Inactivation of Peroxidase by Direct Heating with a Five-Channel Computer-Controlled Thermoresistometer†

Abstract

The thermal inactivation kinetics of horseradish and asparagus peroxidase in high-temperature short-time conditions was studied by heating in a five-channel computer-controlled thermoresistometer. Horseradish peroxidase was heated between 111.5 and 145°C and the reaction was analyzed assuming that two isoenzymes with EaL = 44.1 and Eas = 22.0 kcal/mol were present. Asparagus peroxidase heated from 110 to l20°C reacted with first-order kinetics, with Ea = 20 kcal/mol. The five-channel computer-controlled thermoresistometer enabled us to study the inactivation kinetics of the more labile fraction of horseradish peroxidase at temperatures above 100°C; this equipment was suitable for studying the heat resistance of peroxidase at high temperatures.