Binding of resveratrol with sodium caseinate in aqueous solutions

The interaction between resveratrol (Res) and sodium caseinate (Na-Cas) has been studied by measuring fluorescence quenching of the protein by resveratrol. Quenching constants were determined using Stern–Volmer equation, which suggests that both dynamic and static quenching occur between Na-Cas and Res. Binding constants for the complexation between Na-Cas and Res were determined at different temperatures. The large binding constants (3.7–5.1 × 105 M−1) suggest that Res has strong affinity for Na-Cas. This affinity decreases as the temperature is raised from 25 to 37 °C. The binding involves both hydrogen bonding and hydrophobic interaction, as suggested by negative enthalpy change and positive entropy change for the binding reaction. The present study indicates that Na-Cas, a common food protein, may be used as a carrier of Res, a bioactive polyphenol which is insoluble in both water and oils.

• The large binding constant indicates a strong affinity between Res and Na-Cas.
• The binding constant decreases as the temperature is raised from 25 to 37 °C.
• The binding involves both hydrogen bonding and hydrophobic interactions.