Abstract
In order to clarify the interaction of calcium ion with casein, the volume change associated with the interaction was measured by dilatometric procedures. When CaCl2 was added to the casein solutions at neutral pH, a volume increase occurred and reached a constant saturated value of about 700 ml per 106 g protein with increasing CaCl2 concentrations for whole-, αs- and β-casein solutions, but there was no volume change for κ-casein solution. On the other hand, the binding of calcium ion to the casein fractions was determined by a gel filtration procedure at pH 6.0 to 9.0. The number of Ca2+ ions bound to the caseins increased with the CaCl2 concentration and pH value, and the relative order of binding capacities for the caseins was: αs-casein > whole-casein > β-casein > κ-casein.It was found that the volume changes obtained by the dilatometry were smaller than the calculated volume increases based on the assumption that these are caused by the binding of Ca2+ ion to the caseins. Therefore it is necessary ...
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