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<p>Mayonnaise is a typical high-fat emulsion in which lipid oxidation and protein structural deterioration occur simultaneously and mutually accelerate destabilization during storage. In this study, it elucidated a protein–lipid co-regulation mechanism mediated by tea polyphenols (TP), representing a cooperative-effect stabilization mechanism strategy rather than a single-path antioxidant intervention. Within the tested concentration range, 0.015% TP showed the most favorable overall performance. At this level, TP enhanced interfacial adsorption, reduced the initial droplet size, and shifted the apparent zeta potential of the diluted mayonnaise dispersions to − 23.5&#xa0;mV, which was associated with improved emulsion stability under the tested conditions. Simultaneously, TP induced the transition of yolk proteins from α-helix to β-sheet through hydrogen bonding and hydrophobic interactions, promoting the formation of a more compact interfacial protein film. During the 21-day storage period, the catechol groups of TP effectively scavenged free radicals and enhanced the antioxidant capacity of the mayonnaise system, thereby suppressing lipid oxidation. LF-NMR demonstrated that bound water (T₂₁) increased by 28.82%, reducing water mobility and enhancing freeze–thaw tolerance. Molecular docking further confirmed the preferential binding of TP to yolk lipoproteins (ΔG =  − 4.63&#xa0;kcal/mol), explaining the selective stabilization of protein–lipid complexes at the interface. Collectively, these results revealed a dual-mode stabilization mechanism in which TP simultaneously regulated protein conformation and lipid oxidation, providing an innovative molecular design strategy for engineering high-stability emulsified foods.</p> Graphical Abstract <p></p>

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Impact of Tea Polyphenols on the Regulation of Emulsion Stability of Mayonnaise: A Cooperative Effect Stabilization Mechanism Based on Lipid Oxidation Inhibition and Protein Conformational Regulation

  • 期刊论文

  • 发表日期：

    2026年5月2日

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  • Xiaodan Zhang,
  • Zhaohong Bai,
  • Yuqing Lei,
  • Dezhuang Yu,
  • Ying Gao,
  • Shugang Li

摘要

Mayonnaise is a typical high-fat emulsion in which lipid oxidation and protein structural deterioration occur simultaneously and mutually accelerate destabilization during storage. In this study, it elucidated a protein–lipid co-regulation mechanism mediated by tea polyphenols (TP), representing a cooperative-effect stabilization mechanism strategy rather than a single-path antioxidant intervention. Within the tested concentration range, 0.015% TP showed the most favorable overall performance. At this level, TP enhanced interfacial adsorption, reduced the initial droplet size, and shifted the apparent zeta potential of the diluted mayonnaise dispersions to − 23.5 mV, which was associated with improved emulsion stability under the tested conditions. Simultaneously, TP induced the transition of yolk proteins from α-helix to β-sheet through hydrogen bonding and hydrophobic interactions, promoting the formation of a more compact interfacial protein film. During the 21-day storage period, the catechol groups of TP effectively scavenged free radicals and enhanced the antioxidant capacity of the mayonnaise system, thereby suppressing lipid oxidation. LF-NMR demonstrated that bound water (T₂₁) increased by 28.82%, reducing water mobility and enhancing freeze–thaw tolerance. Molecular docking further confirmed the preferential binding of TP to yolk lipoproteins (ΔG =  − 4.63 kcal/mol), explaining the selective stabilization of protein–lipid complexes at the interface. Collectively, these results revealed a dual-mode stabilization mechanism in which TP simultaneously regulated protein conformation and lipid oxidation, providing an innovative molecular design strategy for engineering high-stability emulsified foods.

Graphical Abstract