The ethanol-influenced changes in proteins and some mineral compounds of milk were examined. Despite apparent phasing (induction and post-induction phases), the ethanol coagulation of milk was found to be a continuous process, lasting until 75% of proteins was coagulated and about 20% of proteins was changed into proteozo-peptone and non-protein nitrogen. It was shown that αs2-casein and β-lactoglobulin were more resistant to the action of alcohol than to heating. The solubility of mineral compounds of milk was found to decrease upon the alcohol addition and the Ca/P weight ratio was indicative of variability in the form of salts being precipitated.
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