ABSTRACT: Interactions of vanillin with soy, casein, and whey proteins were studied in aqueous model systems using a thermodynamic approach. Vanillin-protein binding was examined at 12 and 4 °C using 3 proteins and 6 vanillin concentrations. The results were analyzed using a Klotz plot. Number of binding sites (n) and dissociation constants (Kd) were derived from the plots. The thermodynamic parameters (ΔG°, ΔH°, and ΔS°) for the bindings were calculated. Under identical experimental conditions, whey protein was found to have higher affinity to vanillin than the other 2 proteins. Bindings of vanillin with casein and whey protein were enthalpy driven, while the interaction of vanillin with soy protein was highly entropy driven. The results inferred that conformational changes of soy protein might be important in binding of vanillin.