Protein-Polyphenol Interaction Mechanisms in Food Systems
Summary
Protein–polyphenol interactions are fundamental to the structure, stability and functionality of many food products. These interactions arise through both covalent and non-covalent forces, including hydrogen bonding, hydrophobic association and van der Waals contacts. The formation of conjugates or complexes can alter the secondary and tertiary structure of proteins, leading to changes in solubility, emulsifying capacity, foaming ability and antioxidant properties. In complex matrices such as dairy, plant-based beverages and fruit-enriched formulations, the pH, temperature and processing conditions govern the balance between reversible and irreversible binding. Controlled complexation with polyphenols can improve protein functionality, enhance the stability of bioactive compounds and modulate digestion kinetics. Such phenomena contribute to the development of functional foods with tailored texture, extended shelf life and augmented nutraceutical value.
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Protein-Polyphenol Interaction Mechanisms in Food Systems publication trend
The graph below shows the total number of articles in protein-polyphenol interaction mechanisms in food systems across all publications each year (not limited to Nature Index journals).
Technical terms
Non-covalent interaction: A reversible association between protein and polyphenol molecules via hydrogen bonding, hydrophobic forces or van der Waals attractions.
Covalent conjugation: A stable, irreversible bond formed between reactive groups on protein side-chains and polyphenol moieties, often via oxidative coupling.
Fluorescence quenching: A spectroscopic method in which binding between protein and ligand reduces intrinsic protein fluorescence, allowing determination of binding constants.
Secondary structure: The local conformation of a protein’s backbone, including α-helices and β-sheets, which can be altered by ligand binding.
Emulsifying capacity: The ability of a protein or protein–polyphenol complex to stabilise oil–water interfaces, crucial for products such as dressings and beverages.
References
- A review on protein based nanocarriers for polyphenols: interaction and stabilization mechanisms. Food Innovation and Advances (2023).
- Emerging technologies to improve plant protein functionality with protein-polyphenol interactions. Trends in Food Science & Technology (2024).
- Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes. Foods (2022).
- Changes on the conformational and functional properties of soybean protein isolate induced by quercetin. Frontiers in Nutrition (2022).
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