Impact of tea polyphenols on the regulation of emulsion stability of mayonnaise: a synergistic mechanism based on lipid oxidation inhibition and protein conformational regulation

Impact of tea polyphenols on the regulation of emulsion stability of mayonnaise: a synergistic mechanism based on lipid oxidation inhibition and protein conformational regulation | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Impact of tea polyphenols on the regulation of emulsion stability of mayonnaise: a synergistic mechanism based on lipid oxidation inhibition and protein conformational regulation Xiaodan Zhang, Zhaohong Bai, Yuqing Lei, Dezhuang Yu, Ying Gao, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-8763327/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted 9 You are reading this latest preprint version Abstract Mayonnaise is a model high-fat emulsion. The lipid oxidation and protein conformational deterioration in it occur simultaneously and mutually reinforce each other, which ultimately cause structural collapse during storage. In this study, it elucidated a protein–lipid co-regulation mechanism mediated by tea polyphenols (TP), representing a synergistic stabilization strategy rather than a single-path antioxidant intervention. 0.015% (w/w) TP was identified as the optimal concentration at which lipid oxidation inhibition and interfacial protein remodeling were co-activated. At this level, TP formed a compact interfacial adsorption layer, reduced droplet size, and increased the zeta potential to −23.5 mV, thereby strengthening electrostatic repulsion and suppressing early-stage lipid coalescence. Simultaneously, through hydrogen bonding and hydrophobic interactions, TP induced a conformational transition of yolk proteins from α-helix to β-sheet, resulting in a more rigid protein–lipid interfacial film capable of resisting oxidation-driven structural relaxation. The catechol groups of TP scavenged free radicals, increasing the DPPH scavenging rate to 36.63% and markedly lowering peroxide formation, thereby blocking the lipid–protein co-oxidation chain reaction. 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. Mayonnaise Tea polyphenols Molecular interaction Lipid oxidation Protein conformation Full Text Additional Declarations No competing interests reported. Supplementary Files Abstractgraphic.tif Cite Share Download PDF Status: Under Review Version 1 posted Editorial decision: Revision requested 13 Feb, 2026 Reviews received at journal 13 Feb, 2026 Reviews received at journal 10 Feb, 2026 Reviewers agreed at journal 06 Feb, 2026 Reviewers agreed at journal 04 Feb, 2026 Reviewers invited by journal 04 Feb, 2026 Editor assigned by journal 02 Feb, 2026 Submission checks completed at journal 02 Feb, 2026 First submitted to journal 02 Feb, 2026 You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-8763327","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":586532301,"identity":"cde5800b-8b15-4f26-9e44-9124fb4ffdeb","order_by":0,"name":"Xiaodan Zhang","email":"","orcid":"","institution":"Hefei University of Technology","correspondingAuthor":false,"prefix":"","firstName":"Xiaodan","middleName":"","lastName":"Zhang","suffix":""},{"id":586532303,"identity":"e6863ca5-42df-4b06-a4b1-50adbd23c4db","order_by":1,"name":"Zhaohong Bai","email":"","orcid":"","institution":"Hefei University of 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