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Article Dans Une Revue Dairy Science & Technology Année : 2014

Bovine beta-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Résumé

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 native β-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 of the 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 affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.
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hal-01209560 , version 1 (27-05-2020)

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Solène Le Maux, Said Bouhallab, Linda Giblin, Andre Brodkorb, Thomas Croguennec. Bovine beta-lactoglobulin/fatty acid complexes: binding, structural, and biological properties. Dairy Science & Technology, 2014, 94 (5), pp.409-426. ⟨10.1007/s13594-014-0160-y⟩. ⟨hal-01209560⟩
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