The influence of temperature on the flocculation rate of renneted casein micelles.

The flocculation rate constant of completely renneted casein micelles in milk ultrafiltrate was measured by Rayleigh light scattering between 20 and 35 degrees C. In this temperature range an apparent energy of activation of 103 kJ mol (+/-11 kJ mol : n = 50) was measured. At 15 degrees C clotting was not longer perceptible. The activation of the flocculation between 20 and 35 degrees C is explained not so much by the height of the energy barrier separating the clotting micelles, as by the very negative temperature coefficient of that barrier. In line with this conclusion it is suggested that renneted micelles adhere through hydrophobic bonding. The flocculation rate constant of renneted casein micelles is independent of micelle size at the four temperature levels studied.