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

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.

Automated summary

The molecular structures of flavor compounds have a strong influence on their binding affinity with pea protein. Different functional groups and chain lengths affect the binding abilities of the flavor compounds. Hydrophobic interactions play a dominant role in the binding between (E)-2-octenal/(Z)-2-penten-1-ol and pea protein, while hydrogen bonding is dominant in the binding between hexanal and pea protein.