The effect of thermal treatment on the activity of laccase from Trametes polyzona WRF03 was studied at pH and temperature ranges of 3.0 to 6.5 and of 40 to 70 oC respectively. Kinetic data revealed that the heat inactivation of Trametes polyzona WRF03 laccase (TpL) was pH dependent and followed first-order kinetics. There was a positive correlation between activation energy (Ea) for thermal inactivation of TpL and the reaction pH. Highest activation energy, Ea, value of 175.49 kJ/mol was obtained at pH 6.0. On the contrary, the z-value decreased with a lowest value of 12.37 oC at pH 6.0. The high Ea value and low z-value were indicative of the thermo-stable nature of TpL which suggests that pH 6.0 had a compensatory stabilizing effect on TpL against its thermal denaturation. There was a gradual decrease in the enthalpy of denaturation (∆Ho) and Gibb’s free-energy with every 10 % rise in temperature within the investigated pH range, suggesting that TpL was more stable at 40 oC. Positive values of entropy of inactivation (ΔSº) at each temperature indicated that there was no aggregation during the inactivation processes. Thus, these results provided useful information about the behaviour of TpL under certain pH and temperature combination with respect to biotechnological application. Thus, the kinetic and thermodynamic data could be used to design a model to predict the thermal inactivation of TpL during industrial application.