Structural and surface hydrophobic remodeling of whey protein-linoleic acid-EGCG complex suppresses co-oxidation, attenuates allergenicity, and enhances bioactive functionalities under oxidative stress.

This study developed a whey protein concentrate (WPC)-linoleic acid (LA)-(-)-epigallocatechin-3-gallate (EGCG) ternary complex, evaluating EGCG concentration effects (0-0.14 %, w/v) under Fenton oxidation condition. The complex suppressed WPC-LA co-oxidation in a dose-dependent manner and was maximally inhibited by 0.10 % EGCG. Synergistic α-glucosidase inhibition (0.14 % EGCG) and reduced IgE-binding capacity were demonstrated, indicating allergenicity mitigation. Antioxidant activities (2,2-diphenyl-1-picrylhydrazyl / 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid scavenging) improved significantly (P < 0.05). Molecular docking revealed non-covalent interactions (hydrogen bonds and hydrophobic/π-π/π-alkyl forces) between EGCG/LA and WPC. Structural analyses confirmed increased α-helix content, intrinsic fluorescence quenching with red shifts, reinforced covalent crosslinking in SDS-PAGE profiles, elevated particle size, and diminished zeta potential-collectively indicating altered colloidal stability. Hierarchical clustering linked suppressed co-oxidation and lowered surface hydrophobicity to attenuated allergenicity, enhanced bioactivity, and improved oxidative stability. These findings suggest that WPC-LA-EGCG complexes are multifunctional ingredients in oxygen-sensitive foods, offering reduced allergenicity, α-glucosidase inhibitory activity, and improved oxidative resilience.

• Publication year

  2025

• Venue

  Food Chemistry

• Publication date

  2025-08-13

• Fields of study

  Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/j.foodchem.2025.145950PMID 40829454
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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