This review examines protein-phenolic interactions and their effects on protein digestibility, phenolic bioavailability, and antioxidant delivery across different food matrices. Phenolic compounds, ranging from small phenolic acids and flavonoids to tannins and hydrophobic polyphenols such as curcumin, interact with proteins through covalent and non-covalent mechanisms. These interactions can induce conformational changes, aggregation, or steric shielding, thereby affecting enzymatic hydrolysis and phenolic stability. In simple systems, protein-phenolic interactions are primarily governed by chemical affinity, protein structure, and environmental conditions such as pH, temperature, and ionic strength. However, their behavior changes markedly within complex food matrices. Liquid systems allow more dynamic interactions that may enhance phenolic stability, whereas semi-solid and solid matrices restrict enzyme accessibility and influence release kinetics and antioxidant activity. These matrix-dependent effects determine whether phenolics enhance protein digestion or hinder hydrolysis by strengthening structural networks. Understanding the roles of phenolic size, hydrophobicity, and multivalency, together with protein type, processing conditions, and matrix structure, provides a basis for designing functional foods with improved nutritional and antioxidant properties.
Günal‐Köroğlu et al. (Mon,) studied this question.