Investigation of bovine β-lactoglobulin-procyanidin complexes interactions and its utilization in O/W emulsion

Procyanidins are bioactive polyphenols that have a strong affinity to proteins. Beta-lactoglobulin (BLG) is widely used as an emulsifier in the food and other industries. This study evaluated the interaction between BLG and A-type procyanidin dimer (PA2) using the spectroscopic, thermodynamic, and molecular simulation. PA2 decreased the transmissivity and quenched the intrinsic fluorescence of BLG, suggesting that the two molecules formed a complex. The binding of PA2 reduced the surface hydrophobicity and altered the conformation of BLG with increasing the random coil regions. Thermodynamic and isothermal titration calorimetry analyses suggested that the main driving force of PA2-BLG interaction was hydrophobic attraction. Molecular docking simulations were used to identify the main interaction sites and forces in the BLG-PA2 complexes, which again indicated that hydrophobic interactions dominated. In addition, the influence of PA2 on the ability of BLG to form and stabilize O/W emulsions was analyzed. Emulsions formulated using BLG-PA2 complexes contained relatively small droplets (D4,3 ≈ 0.7 μm) and high surface potentials (absolute value >50 mV). Compared to BLG alone, BLG-PA2 complexes improved the storage stability of the emulsions. This study provides valuable new insights into the formation, properties, and application of protein-polyphenol complexes as functional ingredients in foods. •The binding force between PA2 and BLG was mainly entropy-driven hydrophobic interaction.•The binding of PA2 to BLG reduced the surface hydrophobicity.•The addition of PA2 changed the conformation of BLG.•The addition of PA2 increased the storage stability of BLG emulsion.