Analysis of the inactivation and reactivation kinetics of horseradish peroxidase in mixtures of phosphate buffer/dimethylformamide

Abstract

In this work, the kinetics of the thermal inactivation and reactivation of horseradish peroxidase were analysed in buffered solutions of dimethylformamide at severa1 concentrations (up to 40% vlv) and temperatures ranging fiom 70 to 85 "C. The experimental data of the inactivation and reactivation processes showed a biphasic behaviour, which was well described by a series-type model. The significant activity regain at low temperature of the thermal inactivated enzyme had a strong influence on the estimated value for the a parameter of the model, thus reflecting a clear change of the profile of the experimental curves.