Competitive binding between key aroma components of a strawberry flavoring and pea protein isolate within an aqueous model system

This study aimed to investigate the competitive binding interactions between key flavor compounds in a strawberry flavoring and pea protein isolate (PPI) within an aqueous model system by using a modified equilibrium dialysis technique with gas chromatography–mass spectrometry and sensory evaluation. The equilibration times and binding percentages of each aroma compound were examined, and the results were compared using quantitative descriptive analysis. The results showed that all flavor compounds could bind to PPI. γ-Decalactone, vanillin, ethyl hexanoate and displayed significantly higher binding affinities than the other compounds under both single and competitive binding conditions, which was likely due to their hydrophobicities (higher LogP values). Conversely, the binding efficiencies of ethyl butanoate, methyl anthranilate, furaneol, and (Z)-3-hexen-1-ol decreased under competitive binding conditions, which was not observed for ethyl 3-methylbutanoate. Sensory analyses indicated a perceptual shift in the flavor profile upon introducing PPI, transitioning it from a berry-dominant profile to a profile high in green attributes and low in creamy and berry attributes. To restore the original flavor profile to the strawberry flavoring, flavor modification was used by adjusting the concentration of each flavor compound based on its binding affinity. The final flavor profile nearly achieved a fully balanced profile. However, challenges persisted owing to some remaining green notes. This study was the first of its kind and could serve as a foundation for future investigations into flavor–protein interactions, This data could be helpful for recommending adjustments to flavor formulations, helping manufacturers produce flavorings that are better suited for high-protein food products, especially high-protein beverages.