The kinetics of the neat-induced irreversible denaturation of β-lacto-globulins (β-LG) A and B and of α-lactalbumin (α-LA) in milk were examined over a wide temperature/time range (70-150°C, 2-5400 sec). Denaturation of β-LG was best described with an apparent reaction order of 1.5 (α-LA; first order). The abrupt changes in the temperature dependence of the rate constants (β-LG at 90°C, α-LA at 80°C) were interpreted in terms of the different activation energies and entropies occurring in the two temperature ranges. By using the kinetic parameters for calculating lines of equal degrees of denaturation in a plot of log-time versus 1/absolute temperature it was possible to predict the effect of different heat treatments on the denaturation of individual proteins.