Relationship between flexibility and interfacial functional properties of soy protein isolate: succinylation modification.

BACKGROUND

In this paper, the effects of different succinic anhydride (SA) additions on the flexibility of soy protein isolate (SPI) were investigated, and changes in protein conformation and interfacial functional properties were measured. The structure-effect relationship between conformation, flexibility, and interfacial functional properties was established.

RESULTS

SPI was bound to SA through disulfide bonds, and the zeta potential was reduced. The β-sheet content decreased, the disordered structure increased, and there were changes in tertiary structure and microstructure. The surface hydrophobicity, disulfide bond content, and solution turbidity were reduced to 5063, 1.0967 μmol g , and 0.0036 μmol g respectively. The best flexibility of SPI (0.3977) and interfacial functional properties were obtained when the mass ratio of SA/SPI was 15%. Correlation analysis showed a highly significant positive correlation (P < 0.01) between flexibility and emulsification and foaming properties, with correlation coefficients of 0.960 and 0.942 for flexibility with emulsifying activity and emulsion stability respectively, and 0.972 and 0.929 for flexibility with foaming capacity and foaming stability respectively.

CONCLUSION

The results suggest that succinylation-induced conformational changes of SPI improved its interfacial functional properties by changing its flexibility. These results provide theoretical guidelines for the development and application of highly emulsifiable and stable soy protein products utilizing succinylation. © 2022 Society of Chemical Industry.