0000000001025944
AUTHOR
Laurette Tavel
showing 4 related works from this author
Interactions entre la beta-lactoglobuline et les arômes : impact au niveau moléculaire
2008
Interactions between β-lactoglobulin (BLG) and aroma compounds were investigated by complementary techniques for a better knowledge of binding mechanisms between proteins and aroma compounds at a molecular scale. Two binding sites have been defined for the monomeric BLG, one internal site within the central calyx, and one external site between the calyx and the α helix. In a first step, a relation between the ligand structure and its binding behaviour was established from the study of impact of a wide range of aroma compounds on the structure of native BLG. We evidenced at least two binding behaviours as a function of the chemical class, the hydrophobicity, or the structure of the ligands. …
Interactions between aroma compounds and beta-lactoglobulin in the heat-induced molten globule state
2010
; he present study aims to elucidate the binding of small hydrophobic ligands onto the molten globule state of β-lactoglobulin (BLG). The conversion of the native BLG into a molten globule state was induced by heat treatment at acidic pH. The molten globule state was evidenced by far and near-UV circular dichroism spectra. β-Ionone and guaiacol exhibited a higher binding ability to BLG in the heat-induced molten globule state compared to unheated BLG, as assessed by protein surface hydrophobicity measurements, using 6-propionyl-2-(dimethylamino)naphthalene (PRODAN) fluorescent probe. The binding sites of the two aroma compounds were determined by 2D nuclear magnetic resonance (NMR) spectro…
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…