A soluble fraction of faba bean protein was conjugated with tannic acid via the free-radical grafting method using a mixture of ascorbic acid and hydrogen peroxide. Surface plasmon resonance showed a strong bonding between them, while the free amino and thiol group measurements indicated tannic acid's bonding with the amino groups and cysteine residues on the proteins. Structural analysis using intrinsic fluorescence and surface hydrophobicity demonstrated tannic acid's interaction with the aromatic and hydrophobic amino acids of the protein. The conjugate showed about 77 % DPPH, 89 % ABTS, and 83 % hydroxyl radical scavenging activities and superior ferric-reducing ability compared to the protein alone and the mixture of protein and tannic acid. Electron paramagnetic resonance (EPR) spectroscopy revealed 97.8 % radical scavenging ability of the conjugate, comparable to the pure tannic acid. The exceptional antioxidative properties of conjugate can be utilized to delay lipid oxidation in protein-stabilized oil-in-water emulsions.
Keywords: Antioxidant; Faba bean protein; Protein-polyphenol conjugates; Surface Plasmon resonance; Tannic acid.
Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.