Thermal Inactivation Kinetics of Peroxidase in Coriander Leaves

Abstract

Design of efficient blanching treatments requires knowledge of critical factors such as enzyme inactivation kinetic parameters and relative proportions of heat-labile and heat-resistant fractions, which is unique in each vegetable. Thermal inactivation curves for peroxidase in coriander leaves were determined in the temperature range of 70 to 100 °C and in steam. The isothermal data were statistically treated using both linear and nonlinear regression. Applicability of various enzyme inactivation models available in the literature was critically evaluated. The two-fraction first-order model was found to be the best model to describe the peroxidase inactivation kinetics in coriander leaves (R² > 0.97). Kinetic parameters were determined for heat-labile and heat-resistant isoenzyme fractions. The temperature dependence of the rate parameters in the present study did not follow the Arrhenius relationship.