RESUMEN
ABSTRACT For optimization of biochemical processes in food and pharmaceutical industries, the evaluation of enzyme inactivation kinetic models is necessary to allow their adequate use. Kinetic studies of thermal inactivation of β-galactosidase from Aspergillus oryzae were conducted in order to critically evaluate mathematical equations presented in the literature. Statistical analysis showed that Weibull model presented the best adequacy to residual enzymatic activity data through the processing time and its kinetic parameters as a function of the temperature, in the range of 58-66 ºC. The investigation suggests the existence of a non-sensitive heat fraction on the enzyme structure, which is relatively stable up to temperatures close to 59 ºC. Thermodynamic parameters were evaluated and showed that such β-galactosidase presents activation energy of 277 kJ mol-1 and that the enzyme inactivation is due to molecular structural changes. Results shown that the enzyme is quite stable for biotechnological applications.