Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation kinetics of beta-lactoglobulin in raw milk under isothermal and dynamic temperature conditions

A detailed kinetic study of alkaline phosphatase; lactoperoxidase and beta -lactoglobulin was carried out in the context of identifying intrinsic time -temperature indicators for controlling the heat processing of milk. The he at inactivation or denaturation of alkaline phosphatase, lactoperoxidase an d beta -lactoglobulin under isothermal conditions was found to follow first order kinetics. Experimental results were analysed using both a two step l inear regression and a one step non-linear regression method. Results obtai ned using the two statistical techniques were comparable, but the 95% confi dence interval for the predicted values was smaller when the one step non-l inear regression method was used, indicating its superiority for estimating kinetic parameters. Thermal inactivation of alkaline phosphatase and lacto peroxidase was characterized by z values of 5.3 deg C (D-60 degreesC = 24.6 min) and 4.3 deg C (D-71 degreesC = 38.6 min) respectively. For the denatu ration of beta -lactoglobulin we found z values of 7.9 deg C (D-75 degreesC = 49.9 min) in the temperature range 70-80 degreesC and 24.2 deg C (D-85 d egreesC = 3.53 min) in the range 83-95 degreesC. D-ref and z were evaluated under dynamic temperature conditions. To estimate the statistical accuracy of the parameters, 90 % joint confidence regions were constructed.