Non-covalent interactions of selected flavors with pea protein: Role of molecular structure of flavor compounds

Abstract

The influence of the molecular structures of flavor compounds (specifically, variations in chain length and functional groups) on the binding of the flavor compounds (Z)-2-penten-1-ol, hexanal, and (E)-2-octenal to pea protein was investigated. The results showed that the molecular structures of the flavor compounds strongly influenced their binding affinity for pea protein. Specifically, (E)-2-octenal exhibited a higher binding affinity and a higher Stern-Volmer constant with pea protein than both hexanal and (Z)-2-penten-1-ol. Thermodynamic analysis indicated that the flavor compound-pea protein interactions were spontaneous. Hydrophobic interactions were dominant in the non-covalent interactions between (E)-2-octenal/(Z)-2-penten-1-ol and pea protein, whereas hydrogen bonding was dominant in the non-covalent interactions between hexanal and pea protein. Surface hydrophobicity measurements, the use of bond-disrupting agents, and molecular docking further supported the hypothesis that hydrogen bonding, as well as hydrophobic interactions, occurred between the flavor compounds and pea protein.

Keywords: Binding affinity; Flavor compound; Interaction mechanism; Molecular docking; Pea protein; Spectroscopic analysis.