Kinetics of thermal inactivation of alkaline phosphatase in bovine and caprine milk and buffer.

摘要

The thermal inactivation of alkaline phosphatase (ALP) in raw bovine and caprine milk was investigated in the temperature range 54 to 69 degrees C. To assess the stabilizing effect of milk compounds on ALP, inactivation experiments were also carried out in 0.1 M potassium phosphate buffer, pH 6.6. Each set of inactivation experiments was fitted simultaneously using kinetic models that were based on either one-step or two-step mechanisms. The parameters of the Arrhenius equation showed that the stabilization effect of milk compounds on ALP had an entropic character. They also indicated a different structure of bovine and caprine milk ALPs, which was reflected by a higher stability of the bovine milk enzyme..