INFLUENCE OF PROCESSING ON THE MOLECULAR MODIFICATIONS OF MILK-PROTEINS IN THE COURSE OF ENZYMATIC COAGULATION

The formation of hydrophobic sites on the surface of casein micelles a s a consequence of enzymic coagulation of industrially heat-treated mi lk was studied by following the distribution of a fluorescent hydropho bic probe between a free and an aggregated protein fraction. Results w ere compared with those obtained when coagulation of the same milk sam ples was followed rheologically in a Gelograph apparatus and by tristi mulus colorimetry. Thermal treatment of milk appeared to affect the ac cessibility of casein to enzyme action, while homogenization influence d the rate of cooperative aggregation of casein subjected to proteolys is.