Analyzing changes in volatile flavor compounds of soy protein isolate during ultrasonic-thermal synergistic treatments using electronic nose and HS-SPME-GC-MS combined with chemometrics.

The beany flavor of soy protein isolate (SPI) creates barriers to their application in food processing. This study investigated the effect of ultrasonic-thermal synergistic treatments, combined with vacuum degassing, on the removal of volatile compounds from SPI. The results revealed that ultrasonic-thermal synergistic treatments altered protein secondary structure and increased fluorescence intensity and surface hydrophobicity, which affected the flavor-binding ability of protein, resulting in reduced electronic nose sensor response values. At synergistic treatment (350 W, 120 ℃ and 150 s), the content of hexanal, (E)-2-hexenal, and 1-octen-3-ol reduced by 70.60 %, 95.60 % and 61.23 %. (E)-2-nonenal and 2-pentylfuran were not detected. Chemometric analysis indicated significant flavor differences between control and treated SPI. Furthermore, α-helix, ß-sheet, ß-turn, and surface hydrophobicity highly correlated with volatile compounds through correlation analysis, indicating that altered protein structure affected interactions with volatile compounds. The study reduced beany flavor and further expanded the range of applications of plant protein in food industry.

Effects of ultrasonic treatment on the structural, functional properties and beany flavor of soy protein isolate: Comparison with traditional thermal treatment.

This research explored the influences of ultrasonic and thermal treatments on the structure, functional properties, and beany flavor of soy protein isolate (SPI). In comparison with traditional thermal treatment, ultrasonic treatment effectively induced protein structural unfolding and exposure of hydrophobic groups, which reduced relative content of α-helix, increased relative content of ß-turn, ß-sheet and random coil, and improved the solubility, emulsifying and foaming properties of SPI. Both treatments significantly decreased the species and contents of flavor compounds, such as hexanal, (E)-2-nonenal, (Z)-2-heptenal and (E)-2-hexenal in SPI. The relative content of hexanal in the major beany flavor compound decreased from 11.69% to 6.13% and 5.99% at 350 W ultrasonic power and 150 s thermal treatment procedure, respectively. After ultrasonic treatment, structural changes in SPI were significantly correlated with functional properties but showed a weak correlation with flavor. Conversely, the opposite trend was observed for thermal treatment. Thus, using ultrasonic treatment to induce and stabilise the denatured state of proteins is feasible to improve the functional properties and beany flavor of SPI.