Mechanism for the ethanol-dependent heat-induced dissociation of casein micelles.

An explanation as to how casein micelles dissociate when heated in the presence of ethanol is presented. Dissociation of casein micelles in milk-ethanol mixtures was studied using (1)H NMR, and the effects of addition of CaCl(2), NaCl, or EDTA or alteration of milk pH on this dissociation were studied. It is proposed that at low temperatures, ethanol reduces the solvent quality of milk serum, but above a critical temperature (approximately 30 degrees C in a 35% ethanol solution), ethanol enhances solvent quality and dissociates the casein micelles. Ethanol reduced protein hydrophobicity and increased the pK(a) value of phosphoserine, effects that are likely to be significant in the dissociating effect of ethanol at elevated temperatures.