Effects of physico-chemical parameters of a model wine on the binding of γ-decalactone on bovine serum albumin

• Published in: Food chemistry Vol. 53; no. 2; pp. 203 - 207
• Main Authors: Druaux, C., Lubbers, S., Charpentier, C., Voilley, A.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 1995; Elsevier
• Subjects: binding; binding sites; Biological and medical sciences; bovine serum albumin; comparisons; energy; ethanol; Fermented food industries; flavor; Food industries; Fundamental and applied biological sciences. Psychology; interactions; ionized compounds; ions; lactones; odor compounds; odors; temperature; volatile compounds; water; wines; Wines and vinegars; Volatile compound; Proteins; Wine; Temperature; Ethanol; Ionic strength; Albumin; pH; Environmental factor; Molecular interaction; Models; Aroma
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/0308-8146(95)90789-A

To understand the effect of temperature, pH and the composition of alcoholic beverages in flavour-protein interactions, the binding of γ-decalactone to bovine serum albumin (BSA) was investigated using the equilibrium dialysis method. Thermodynamic analysis revealed that the affinity of aroma compound for BSA is higher at 10 °C than at 20 and 30 °C, while the number of binding sites ( n = 6–7) is not modified at the three temperatures. pH did not have any appreciable effect on flavour binding in the presence of ethanol, but it was observed that a decrease of 1.8 pH unit reduces binding by 40% in its absence. The presence of ethanol has no effect on the number of binding sites and on the standard free energy (ΔG °) of the interactions. On the other hand, the binding constant ( k) was 4.8-fold higher in water than in model wine (pH 3.5, ionized compounds, 10% w/w ethanol); so, the affinity of volatile compound was clearly lower in the model wine than in water.