Dairy products contain large amount of calcium which is bound to caseins and different chelating agents like citrate and polyphosphates. The present study aimed to determine the calcium-binding capacities of phosphoserine (SerP), caseinophosphopeptide (CPP), β-casein, caseinate, citrate and pyrophosphate in the same conditions of temperature, pH and ionic strength. The free calcium (Ca(2+)) was measured using a calcium ion-selective electrode and plotted as a function of total calcium concentration. The association constants and the number of calcium-binding sites were determined by fitting the experimental data to a theoretical model. The phosphate groups of caseins were the main binding sites with evidence for participation of carboxylate groups. The intrinsic association constants determined by the best fit of the data were in the order: pyrophosphate (557×10(3)M(-1))>citrate (20×10(3)M(-1))>β-casein (5×10(3)M(-1))>caseinate, CPP and SerP (∼10(3)M(-1)). These findings may be of interest for the development of calcium-enriched products to overcome calcium deficiency in specific populations.
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