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

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Abstract
Differential Scanning Calorimetry and an automatic sorption apparatus were used to study hydration of native caseins and rennin coagulated caseins (para- caseins). Similar to other protein-water systems, determination of the heat and temperatm-e of fusion of the adsorbed water allowed resolution of the water into four states. For both native, and para- casein the amounts and thawing intervals for the different water fractions were not significantly different. However, the ad- sorption and desorption isotherms and the differential sorption rates were dif- ferent for native and freshly coagulated paracasein. Paraeasein did not alter water binding capacity when syneresis was induced. From the water sorption data and structural features of native- and paracaseins one may conc!ude that changes in the water binding capacity play only a minor role in the secondary phase of casei~ eo~gu!ation bv rennin and that the phenomenon of syneresis is not accompanied bv changes in the na- ture of hydration.

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