Interactions of β-lactoglobulin variants A and B with Vitamin A. Competitive binding of retinoids and carotenoids.

β-Lactoglobulin (β-Lg) is the major whey protein of bovine milk present at a concentration of 2-3 g L(-1). Its biological role is still not well-known. However, many studies have suggested that β-Lg may play either nutritional or specific transporter role. The high affinity of β-Lg for retinol and other retinoids was reported. The results of interaction studies of β-Lg with carotenoids, that is, β-carotene, β-cryptoxanthin, and α-carotene, which display similar structures are reported in this study. The affinities of β-Lg for binding of retinoids and carotenoids were compared, providing more information about the binding site(s) of these molecules by β-Lg. Interactions were followed by the measurements of quenching of β-Lg tryptophan fluorescence and retinol fluorescence. The obtained results indicate that carotenoids are bound by β-Lg with high affinity of the order of 10(-8) M. Measurement of retinol competition with carotenoids for binding by β-Lg suggests that the binding of these two ligands occurs at two different sites of β-Lg.