Interactions between beta-lactoglobulin and aroma compounds: Different binding behaviors as a function of ligand structure

Laurette Tavel (1) , Isabelle Andriot (1) , Céline Moreau (1) , Elisabeth Guichard (1)

1 FLAVIC - FLAveur, VIsion et Comportement du consommateur

Interactions between β-lactoglobulin (BLG) in its monomeric form and a wide range of aroma compounds were investigated by Fourier transform infrared (FT-IR) and 2D nuclear magnetic resonance (NMR) spectroscopies. A screening of the ligands was carried out by FT-IR through the amide I region changes of BLG upon binding. The location of two binding sites was determined by 2D NMR from the study of 10 selected ligands with different structures. All of the data suggest at least two binding behaviors as a function of the chemical class, the hydrophobicity, or the structure of the ligands. The binding of the elongated aroma compounds, such as 2-nonanone or ethyl pentanoate, within the central cavity involves residues located at the entrance of the calyx and Trp19. The binding onto the protein surface of aroma compounds that have or adopt a compact structure occurs in a site located between strand β-G, α helix, and strand β-I.

Mots clés: beta-lactoglobulin; FT-IR; 2D NMR; aroma compound; protein-ligand interactions; binding sites location

Domaines: Alimentation et Nutrition

Laurette Tavel, Isabelle Andriot, Céline Moreau, Elisabeth Guichard. Interactions between beta-lactoglobulin and aroma compounds: Different binding behaviors as a function of ligand structure. Journal of Agricultural and Food Chemistry, 2008, 56 (21), pp.10208-10217. ⟨10.1021/jf801841u⟩. ⟨hal-01413538⟩