The aim of this study was to report on the interactions between a well char
acterised macromolecule, beta-lactoglobulin, and a wide range of flavour co
mpounds, in different media. Flavour compounds interacting with the protein
were screened using different methods, and thermodynamic constants were ca
lculated. Within the same chemical class, the affinity constant increased w
ith increasing chain length, suggesting hydrophobic interactions. The influ
ence of ethanol, NaCl, pH and temperature were discussed as a function of t
he protein conformation. The influence of beta-lactoglobulin at the oil-wat
er interface, on the release of different flavour compounds, was investigat
ed in model oil/water emulsions. Even if the addition of fat induces a grea
ter change in flavour release than the addition of protein in water solutio
n, beta-lactoglobulin at the oil/water interface limits the transfer of hyd
rophobic compounds from oil to water and thus induces a lower flavour perce
ption. (C) 2000 Elsevier Science Ltd. All rights reserved.