Physicochemical Interactions Between Aroma Compounds and Milk Proteins: Effect of Water and Protein Modification

The physicochemical interactions between aroma compounds and sodium caseinate were studied by complementary techniques involving the protein in aqueous solution at 25 or 75 g/L (exponential dilution and equilibrium dialysis) or in a solid state (sorption and infrared spectroscopy). No retention of acetone, ethyl acetate, and 2-propanol in aqueous solutions was found by exponential dilution and equilibrium dialysis. Diacetyl and benzaldehyde interacted with sodium caseinate through strong and weak bonds, as found by equilibrium dialysis. The results obtained by sorption differ from those obtained in aqueous solutions. The compounds that sorbed best to sodium caseinate were acetone and ethyl …