Binding of β-lactoglobulin to three phenolics improves the stability of phenolics studied by multispectral analysis and molecular modeling

Molecular Mechanisms and Applications of Polyphenol-Protein Complexes with Antioxidant Properties: A Review

“…As for polyphenols, they act as hydrogen donors, and their hydroxyl groups can form hydrogen bonds through interactions between the C=O groups of the amide group on the peptide chain, the oxygen or nitrogen on the side chains of amino acid residues, especially hydroxyl (–OH) and amino (–NH2) groups [ 23 , 24 ]. Zhang et al [ 25 ] found that ferulic acid, quercetin, and vanillic acid could interact via three, seven, and two hydrogen bonds with β-lactoglobulin, respectively. Wen et al [ 26 ] revealed that ovalbumin and procyanidin have a hydrogen bond-dominated interaction.…”

“…Rosmarinic acids interacted with β-lactoglobulin or α-lactalbumin with the driving forces of hydrogen bonds, hydrophobic forces, and van der Waals force [ 29 ]. The binding of ferulic acid/quercetin/vanillic acid to β-lactoglobulin involved various non-covalent interactions such as hydrogen bonds, van der Waals interactions, and hydrophobic interactions [ 25 ]. Ovalbumin-isoquercitrin complexes are formed by hydrophobic interactions, van der Waals forces, and hydrogen bonding [ 33 ].…”