In order to describe the kinetics of rennet coagulation, measurements of turbidity as a function of wavelength were used to determine the weight-average degree of polymerization, x¯w, during renneting of milk at three different concentrations of enzyme and three concentrations of casein, including the normal casein concentration of milk. The change of x¯w as a function of time was described using Von Smoluchowski's equation, testing a number of expressions for the aggregation rate constant, kij. The best description was achieved when kij was taken as a function of an energy barrier against aggregation that was diminished by the proteolysis of κ-casein. The initial value of the energy barrier partly depended on the casein concentration, and had a value >25 kBT at normal casein concentration, where kB is Boltzmann's constant and T the absolute temperature. When the proteolysis of κ-casein was complete, the energy barrier was reduced to 11 kBT and was independent of casein concentration.