0000000001025946
AUTHOR
Eunice Li-chan
showing 2 related works from this author
Hydrophobic interactions between aroma compounds and beta-Lactoglobulin using a specific fluorescent probe and NMR
2008
International audience; Many aroma compounds are known to bind with proteins, and elucidating these bindind interactions is a key in a better knowledgment of flavour perception mechanisms (1). beta-Lactoglobulin (bLg), the major whey protein of milk, has been used as a model food protein in numerous studies. Previous work have shown different binding sites on bLg for aroma compounds as a function of their chemical class, and emphasized the importance of hydrophobic interactions (2). (...)
Hydrophobic interactions between aroma compounds and beta-Lactoglobulin using NMR and a fluorescent probe
2010
International audience; beta-lactoglobulin (bLg) is known to interact with aroma compounds affecting their release, and hence, their perception. bLg, composed of two hydrophobic binding sites, was used as a simple model food protein to investigate binding mechanisms as a function of ligand nature. Indeed, binding of small ligands to bLg sites is often selective, although some ligands bind to both sites. Interactions between bLg and one ketone, beta-ionone, and one phenol, guaiacol were investigated by combining two techniques: 2D Nuclear Magnetic Resonance for binding site location, and fluorescence using the 6-propionyl-2-(N, N-dimethylamino)naphthalene (PRODAN) probe for surface hydrophob…