Thermal inactivation kinetics of peroxidase and lipoxygenase from fresh pinto beans (Phaseolus vulgaris)

 Thermal inactivation kinetics of crude peroxidase (POX) and lipoxygenase (LOX) in fresh pinto beans were studied over the temperature range of 55–90°C. The inactivation of both enzymes followed first-order kinetics. The biphasic inactivation curves for POX indicate the existence of several isoenzymes of varying heat stability. In the temperature range of 55–70°C, the activation energies (E _a) of POX were 46.5 kcal·mol^–1 for the heat-labile portion and 37.6 kcal·mol^–1 for the heat-stable portion. On the other hand, the LOX enzyme had an E _a value of 42.26 kcal·mol^–1 at 55–75°C and 49.1 kcal·mol^–1 at 55–90°C. Received: 28 July 1997 / Revised version: 16 October 1997