Evaluation of the adsorption capacity and mechanism of soy protein isolate for volatile flavor compounds: Role of different oxygen-containing functional groups

被引:33
|
作者
Zhang, Bin [1 ]
Zhang, Jingwen [1 ]
Yu, Xiaobo [1 ,2 ]
Peng, Jing [1 ]
Pan, Leiqing [1 ]
Tu, Kang [1 ]
机构
[1] Nanjing Agr Univ, Coll Food Sci & Technol, 1 Weigang Rd, Nanjing 210095, Peoples R China
[2] Natl Ctr Meat Qual & Safety Control, Nanjing 210095, Peoples R China
关键词
Soy protein isolate; Volatile flavor compounds; Molecular interactions; Fluorescence quenching; Surface plasmon resonance; Molecular docking; AROMA COMPOUNDS; BINDING; PEA; VANILLIN; ABILITY; CANOLA;
D O I
10.1016/j.foodchem.2022.132745
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Mechanism of soy protein isolate (SPI) adsorbing isomers of volatile flavor compounds (VFCs: 2-octanone, 1-octen-3-ol and octanal) were investigated by exploring the interaction between different oxygen-containing functional groups (OCF groups: carbonyl, alcohol hydroxyl and aldehyde group) and SPI in this study. VFCs made SPI aggregate into larger particle size, and an increase in beta-sheet and beta-turn was observed. Octanal has strongest binding capacity to SPI, followed by 1-octen-3-ol and 2-octanone. Fluorescence analysis revealed that static quenching occurred between the VFCs and SPI, which suggested that SPI-VFCs complex were formed. Double logarithmic Stern-Volmer indicated the strongest interaction between aldehyde group and SPI, which was proved by surface plasmon resonance. Finally, molecular docking results showed more hydrogen bonds between octanal and SPI. The results showed that aldehyde groups were more likely to interact with SPI than others, probably due to their tendency to form more hydrogen bonds.
引用
收藏
页数:7
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