Binding properties of β-lactoglobulin with polyphenols – A review

Abstract

Bovine β-lactoglobulin is the most abundant whey protein secreted in the milk of most mammals but not in the human, rodents and lagomorphs milk. The biological function of this protein is still not completely understood, but it is believed to be related to its globular structure and the presence of an internal cavity called calyx or β-barrel, where small hydrophobic molecules can bind. Recent studies revealed that β-lactoglobulin has at least three binding sites, located in the internal core of the calyx, at the dimer interface and in the hydrophobic region between α-helix and β-barrel. In particular, this review focuses on the studies presenting β– lactoglobulin as potential carrier for polyphenolic compounds, molecules wellknown for their beneficial health effects. Regarding the polyphenols binding site, several studies indicated that it is located outside the protein calyx.

Keywords

• bovine β–lactoglobulin
• binding affinity
• Tanford transition
• polyphenols