Plant-Based Protein-Phenolic Interactions: Effect on different matrices and in vitro gastrointestinal digestion

Abstract

This review summarizes the literature on the interaction between plant-based proteins and phenolics. The structure of the phenolic compound, the plant source of proteins, matrix properties (pH, temperature), and interaction mechanism (covalent and non-covalent) change the secondary structure, ζ-potential, surface hydrophobicity, and thermal stability of proteins as well as their functional properties including solubility, foaming, and emulsifying properties. Studies indicated that the foaming and emulsifying properties may be affected either positively or negatively according to the type and concentration of the phenolic compound. Protein digestibility, on the other hand, differs depending on (1) the phenolic concentration, (2) whether the food matrix is ​​solid or liquid, and (3) the state of the food-whether it is heat-treated or prepared as a mixture without heat treatment in the presence of phenolics. This review comprehensively covers the effects of protein-phenolic interactions on the structure and properties of proteins, including functional properties and digestibility both in model systems and real food matrix.

Keywords: Dephenolization; Fluorescence quenching; Secondary structure; Thermodynamic parameters.