Understanding protein–flavor interactions: Factors, characterization techniques, and the effect of processing

Abstract The perception of flavor in a food system depends on its release from the protein matrix. Apart from hydrogen bonding, hydrophobic interactions and van der Waal's forces, the formation of covalent adducts between the flavor and protein highly impacts the release of flavor from the protein matrix. The spatial configuration and amino acid sequence of the protein govern the interactions. The properties of the flavor such as chain length, hydrophobicity, unsaturation level, and the type and position of the functional group impact the rigidity of the flavor molecule to interact with proteins. If the protein–flavor interactions are too strong, the flavor would also be extracted with the protein during protein extraction. Hence, processing operations such as extrusion and enzymatic approaches are employed to modify these interactions for suitable applications in plant‐based beverages and meats. An increase in the chain length of flavor molecule increases the binding of flavor to the protein, irrespective of the protein and the class of flavor molecule. Increased binding is due to an increase in the hydrophobicity of higher homologous flavor compounds. A flavor molecule that is weakly associated with protein is released rapidly into food, but the covalent adducts are not likely to be released easily.