Abstract

In this study, the improvement of gel properties and digestibility of the water-soluble polymer of tea polyphenol (TP)-egg white protein (TEP) under heat induction (HTEP), was studied. Results indicated that the particle size and turbidity of TEP increased with TP concentration, and the absolute value of ζ-potential decreased. After heat induction, the surface hydrophobicity of HTEP decreased with TP concentration, and the degree of protein aggregation increased. Microstructure and T2 showed that the gel structure became compact and stable, and HTEP had a strong water-binding ability. The ionic and disulfide bonds were the main chemical bonds in HTEP. The hardness and disulfide bond increased, but the digestion of HTEP increased initially and then decreased (caused by the change of gel structure). Infrared spectroscopy indicated the mutual conversion of intermolecular and intramolecular β-sheets. In short, TP could modify egg white gel through forming stable disulfide bonds and dense gel network structures.

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