Abstract
Temperature and pressure affect the conformation of the (globular) whey proteins as well as the structure of the colloidal casein aggregates — casein micelles — but also the equilibrium state of dissolved and colloidal (casein-bound) calcium phosphate in milk. The relations between temperature- and pressure-induced changes of calcium phoshate equilibria were evaluated in original and ultra-high- temperature treated milks, in corresponding ultrafiltration retentates and permeates and in synthetic milk salt solutions. By high pressure treatment the heat- induced changes of calcium phosphate can be largely reversed to their original values. These changes can be related to the pressure-induced structural changes of the micellar casein and to interactions of casein with temperature- or pressure- denaturated whey proteins.
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