Comparative study of binding interactions between different fatty acids and β-lactoglobulin:Impact on conformation...

A comparative study was conducted to investigate the binding mechanisms and interactions between four different lengths of saturated fatty acids (C12:0 to C18:0) and two types of C18 unsaturated fatty acids (C18:1 and C18:2) with β-lactoglobulin (β-Lg). The quenching mechanism for these six fatty acids - lauric acid (LUA), myristic acid (MA), palmitic acid (PAL), stearic acid (SA), oleic acid (OA), and linoleic acid (LA) - with β-Lg were found to be static, and the interactions were predominantly driven by hydrophobic forces. The binding affinity was increased with the increase of carbon chain. While, an increase in the number of CC double bonds resulted in a decreased in binding affinity. The binding of fatty acids interfered with the micro-environment around the tyrosine (Tyr) and tryptophan (Trp) residues in protein, subsequently altering the secondary structures of β-Lg. This study will help to improve our understanding of nutrient interactions in food.