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Heat-induced changes of whey proteins in skim milk were studied, Kinetic parameters(activaion energy, frequency factor, and reaction order) for the heat denaturation of total albumin (TA) and non-casein nitrogen (NCN) were determined by applying both an isothermal (modified partial sterilization) and a non-isothermal (linearly increasing temperature) method. Kinetics of heat denaturation of β-lactoglobulin (β-LG) were also investigated by the latter method. Although the TA and the NCN are composed of complex proteins with varying heat stability, the kinetics of heat denaturation can be expressed simply by a second order reaction model with one activation energy in the range of 60~90℃, Heat denaturation of β-LG measured by the linearly increasing temperature method followed a second order kinetic and its kinetic parameters (activation energy, 275.6kl/mole; frequency factor, 2.07×10³??/mole/sec) agreed well with the literature values.
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