Chemical and thermodynamic characterization of antioxidant emulsifiers: The case of complex of sodium caseinate with EGCG

In this study, complexes formed by sodium caseinate (CS) and different concentrations of (−)-epigallocatechin-3-gallate (EGCG) were successfully prepared. The structures the CS–EGCG then analyzed fluorescence spectroscopy, circular dichroism, Fourier transform infrared spectroscopy (FTIR). Their thermodynamic features also Van't Hoff equation before evaluating antioxidant properties as well emulsion stability. results showed that EGCG grafting significantly altered CS structure, primarily due to their interactions. However, besides covalent bonding within CS–EGCG, analysis further highlighted presence slight interactions driven hydrophobic entropic changes. decreased surface hydrophobicity while increasing its solubility, thus improving stability protein in water. Finally, process improved thermal emulsifying properties, especially 3-ethylbenzothiazoline-6-sulfonic acid 2,2-diphenyl-1-picrylhydrazyl scavenging ferric ion reducing power. These findings can contribute study polyphenol food fields.