Abstract
Isothermal titration calorimetry (ITC) measurements were performed using solutions of whey protein isolate (WPI) and chitosan with different deacetylation degrees (DD), in acetate buffer solutions, pH 3–6. Turbidity measurements were performed in parallel in order to follow the changes in aggregation, so as to get deeper insight on the interaction mechanism. The viscosity–average molar mass of chitosan was obtained from intrinsic viscosity measurements, and the interaction enthalpies were derived at the studied pH values. Further, the denaturation process of α-lactalbumin and β-lactoglobulin within WPI was characterized by differential scanning calorimetry (DSC). At pH 3, where both chitosan and the proteins are positively charged, a weak carbohydrate–protein interaction is observed. When the pH is raised to 6, where the protein charge is expected to be negative, a much stronger interaction takes place. The results are discussed with special emphasis on the effect of pH on the interactions observed in this complex system.
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