Bovine beta-lactoglobulin/fatty acid complexes: binding, structural, and biological properties
2014
Le Maux, Solène | Bouhallab, Said | Giblin, Linda | Brodkorb, Andre
Ligand-binding properties of β-lactoglobulin ( β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the struc-tural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding proper-ties of nativeβ-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiom-etry and the affinity of β-lg for fatty acids and consequently the biological functions ofthe complex. Finally, the fatty acid-binding properties of other whey proteins ( α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affectβ-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.
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