Search results for "surface hydrophobicity"
showing 3 items of 3 documents
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…
Impact of electron beam irradiation on fish gelatin film properties
2016
International audience; The objective of this work was to display the effect of electron beam accelerator doses on properties of plasticized fish gelatin film. Electron spin resonance indicates free radical formation during irradiation, which might induce intermolecular cross-linking. Tensile strength for gelatin film significantly increases after irradiation (improved by 30% for 60 kGy). The vapour permeability is weakly affected by irradiation. Surface tension and its polar component increase significantly and are in accordance with the increase of wettability. So, irradiation may change the orientation of polar groups of gelatin at the film surface and crosslink the hydrophobic amino aci…