Interactions between β-lactoglobulin and flavour compounds

The aim of this study was to report on the interactions between a well characterised macromolecule, β-lactoglobulin, and a wide range of flavour compounds, in different media. Flavour compounds interacting with the protein were screened using different methods, and thermodynamic constants were calculated. Within the same chemical class, the affinity constant increased with increasing chain length, suggesting hydrophobic interactions. The influence of ethanol, NaCl, pH and temperature were discussed as a function of the protein conformation. The influence of β-lactoglobulin at the oil–water interface, on the release of different flavour compounds, was investigated in model oil/water emulsions. Even if the addition of fat induces a greater change in flavour release than the addition of protein in water solution, β-lactoglobulin at the oil/water interface limits the transfer of hydrophobic compounds from oil to water and thus induces a lower flavour perception.