Factors affecting the action of rennin in heated milk

Summary The effect of temperature and time of heating whole milk on the renninclotting time, the primary phase of rennin action and the protein (mainly β-lactoglobulin) soluble in 2% trichloroacetic acid (TCA), have been studied. Considerable changes in these parameters occurred above 60°C. The primary phase was inhibited (the degree of inhibition being both temperature and time-dependent), the clotting time was increased, and the protein soluble in 2% TCA decreased considerably. It is suggested that the inhibition of the primary phase was due to complex formation between κ-casein and β-lactoglobulin, the increase in clotting time to a combination of complex formation and a change in the distribution of Ca, and the decrease in β-lactoglobulin to both its interaction with κ-casein and its heat denaturation. The relevance of such changes to the heat stability of milk is discussed.