绿豆
发酵
风味
食品科学
化学
豌豆蛋白
乳酸菌
生物化学
生物
作者
Yuqi Xue,Jie Chen,Lei Wang,Yuwen Wang,Fei Xu
标识
DOI:10.1016/j.lwt.2025.117450
摘要
The combination of mung bean protein (MBP) and beany flavor compounds results in an unpleasant soy-like flavor. This study investigated the binding mechanism between MBP and beany flavor substances. The effect of structural changes in MBP during Lactobacillus fermentation on the interaction with flavor compounds was analyzed. The study also examined the changes in volatile flavor compounds. The results showed that the binding constants of MBP with nonanal, hexanal, decanal, and hexanol are all above 10 4 M −1 .S −1 , with the number of binding sites ranging from 2.12 to 5.29. Thermodynamic parameters demonstrated that hydrogen bonding and hydrophobic interactions play a dominant role in the binding of MBP to beany flavor compounds. Structural changes in MBP during Lactobacillus fermentation were found to weaken its binding capacity with beany flavor compounds, as evidenced by a reduction in the amounts of 7S and 11S subunit proteins and a significant increase in -SH and -S-S- content. Moreover, there was a transition from α-helix and β-sheet to β-turn and irregular coil structures. Lactobacillus plantarum LP90 eliminated 92.57% of beany-flavor aldehydes and alcohols after 24 h of fermentation. This study provides a theoretical foundation for understanding the binding mechanism between MBP and beany flavor compounds. • MBP strongly interacts with beany flavor compounds: hexanal, nonanal, decanal, and hexanol. • Fermentation alters MBP structure and bonding, reducing its interaction with beany flavors. • Lactobacillus LP90 reduced beany flavor aldehydes and alcohols by 92.57% in 24 h.
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