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

  • WENDIE L. CLAEYS (a1), LINDA R. LUDIKHUYZE (a1), ANN M. VAN LOEY (a1) and MARC E. HENDRICKX (a1)

Abstract

A detailed kinetic study of alkaline phosphatase, lactoperoxidase and β-lactoglobulin was carried out in the context of identifying intrinsic time–temperature indicators for controlling the heat processing of milk. The heat inactivation or denaturation of alkaline phosphatase, lactoperoxidase and β-lactoglobulin under isothermal conditions was found to follow first order kinetics. Experimental results were analysed using both a two step linear regression and a one step non-linear regression method. Results obtained using the two statistical techniques were comparable, but the 95% confidence interval for the predicted values was smaller when the one step non-linear regression method was used, indicating its superiority for estimating kinetic parameters. Thermal inactivation of alkaline phosphatase and lactoperoxidase was characterized by z values of 5·3 deg C (D60 °C = 24·6 min) and 4·3 deg C (D71 °C = 38·6 min) respectively. For the denaturation of β-lactoglobulin we found z values of 7·9 deg C (D75 °C = 49·9 min) in the temperature range 70–80 °C and 24·2 deg C (D85 °C = 3·53 min) in the range 83-95 °C. Dref and z were evaluated under dynamic temperature conditions. To estimate the statistical accuracy of the parameters, 90% joint confidence regions were constructed.

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

  • WENDIE L. CLAEYS (a1), LINDA R. LUDIKHUYZE (a1), ANN M. VAN LOEY (a1) and MARC E. HENDRICKX (a1)

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