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Influence of processing on the molecular modifications of milk proteins in the course of enzymic coagulation
Published online by Cambridge University Press: 01 June 2009
Summary
The formation of hydrophobic sites on the surface of casein micelles as a consequence of enzymic coagulation of industrially heat-treated milk was studied by following the distribution of a fluorescent hydrophobic probe between a free and an aggregated protein fraction. Results were compared with those obtained when coagulation of the same milk samples was followed rheologically in a Gelograph apparatus and by tristimulus colorimetry. Thermal treatment of milk appeared to affect the accessibility of casein to enzyme action, while homogenization influenced the rate of cooperative aggregation of casein subjected to proteolysis.
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- Copyright © Proprietors of Journal of Dairy Research 1993
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