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

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