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Hydration of Native and Rennin Coagulated Caseins as Determined by Differential Scanning Calorimetry and Gravimetric Sorption Measurements

Federal Dairy Research Station, 3097 Liebefeld-Berne, Switzerland
¹ Institute for Organic Chemistry, University of Berne, 3000 Berne, Switzerland

ABSTRACT

Differential Scanning Calorimetry and an automatic sorption apparatus were used to study hydration of native caseins and rennin coagulated caseins (paracaseins). Similar to other protein-water systems, determination of the heat and temperature of fusion of the adsorbed water allowed resolution of the water into four states. For both native and paracasein the amounts and thawing intervals for the different water fractions were not significantly different. However, the adsorption and desorption isotherms and the differential sorption rates were different for native and freshly coagulated paracasein. Paracasein did not alter water binding capacity when syneresis was induced. From the water sorption data and structural features of native-and paracaseins one may conclude that changes in the water binding capacity play only a minor role in the secondary phase of casein coagulation by rennin and that the phenomenon of syneresis is not accompanied by changes in the nature of hydration.