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

Abstract

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 structural 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 properties 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 stoichiometry 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.

β-Lactoglobulin interactions with local anaesthetic drugs – Crystallographic and calorimetric studies

“…However, the association constant range of 10 2 -10 4 M −1 indicates very weak interactions in comparison to endogenous ligands like fatty acids (10 5 -10 9 M −1 ) [27,44].…”

Changes in the content of immunostimulating components of colostrum obtained from dairy cows at different levels of production

“…Bovine β ‐lactoglobulin ( β ‐Lg) has binding, structural, and biological properties . The concentration of β ‐Lg in the colostrum from LI and HI in the first collection was 6.940 and 7.104 gL −1 , respectively; and gradually decreased, at the end of the experiment (seventh collection) reaching the value of 1.470 and 1.890 gL −1 (Fig.…”

Heteroprotein complex coacervation: A generic process

“…β-LG has 5 cysteine residues engaged in two disulphide bonds and leaving one free sulfhydryl group hidden within the native protein structure. In aqueous solution, the β-sheets form a well-defined calyx, which constitutes an ideal binding site for hydrophobic ligands [22][23][24][25][26]. At neutral pH and room temperature, β-LG exists as non-covalent dimers in A C C E P T E D M A N U S C R I P T…”