Non-covalent interactions of selected flavors with pea protein: Role of molecular structure of flavor compounds was written by Bi, Shuang;Pan, Xin;Zhang, Wentao;Ma, Zhuo;Lao, Fei;Shen, Qun;Wu, Jihong. And the article was included in Food Chemistry in 2022.Reference of 57-55-6 This article mentions the following:
The influence of the mol. 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 mol. 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. Thermodn. anal. 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 mol. docking further supported the hypothesis that hydrogen bonding, as well as hydrophobic interactions, occurred between the flavor compounds and pea protein. In the experiment, the researchers used many compounds, for example, 1,2-Propanediol (cas: 57-55-6Reference of 57-55-6).
1,2-Propanediol (cas: 57-55-6) belongs to alcohols. A strong base can deprotonate an alcohol to yield an alkoxide ion (R―O−). For example, sodamide (NaNH2), a very strong base, abstracts the hydrogen atom of an alcohol. Under carefully controlled conditions, simple alcohols can undergo intermolecular dehydration to give ethers. This reaction is effective only with methanol, ethanol, and other simple primary alcohols.Reference of 57-55-6
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts