This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is only affected if strong binding occurs.