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.

风味化合物的分子结构（特别是链长和官能团的变化）对风味化合物 ( Z )-2-penten-1-ol、己醛和 ( E )-2-octenal 与豌豆蛋白进行了研究。结果表明，风味化合物的分子结构强烈影响其与豌豆蛋白的结合亲和力。具体来说，与己醛和 ( Z )-2-penten-1-ol相比，( E )-2-octenal 与豌豆蛋白的结合亲和力更高，Stern-Volmer 常数也更高。热力学分析表明风味化合物与豌豆蛋白的相互作用是自发的。（ E）之间的非共价相互作用中疏水相互作用占主导地位)-2-octenal/( Z )-2-penten-1-ol 和豌豆蛋白，而氢键在己醛和豌豆蛋白之间的非共价相互作用中占主导地位。表面疏水性测量、键破坏剂的使用和分子对接进一步支持了在风味化合物和豌豆蛋白之间发生氢键以及疏水相互作用的假设。