title: Binding of resveratrol with sodium caseinate in aqueous solutions.
abstract: 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 (3.7-5.1×10(5)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.
authors.affiliation: CSIRO Preventative Health National Research Flagship, Food and Health Sciences, 671 Sneydes Road, Werribee, VIC 3030, Australia. Durga.Acharya@csiro.au
authors.forename: Durga P
authors.initials: DP
authors.lastname: Acharya
authors.forename: Luz
authors.initials: L
authors.lastname: Sanguansri
authors.forename: Mary Ann
authors.initials: MA
authors.lastname: Augustin
mesh_terms: D002364:Caseins / Q000737:chemistry*; D007700:Kinetics; D000077185:Resveratrol; D013267:Stilbenes / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
chemical_list: D002364:Caseins; D013267:Stilbenes; D000077185:Resveratrol