Impact of rutin on the foaming properties of soybean protein: Formation and characterization of flavonoid-protein complexes.

The aims of present study were to determine the impact of rutin complexation on the ability of soybean protein isolates (SPI) to form and stabilize foams and its mechanism. At pH 7.0, the foaming capacity and foaming stability of the rutin-SPI complexes (28.33% and 14.22%) was appreciably changed when compared with that of SPI alone (19.64% and 32.95%). The improvement in foaming properties was mainly attributed to decrease gas bubble size and increase interfacial thickness as suggested by light microscopy analysis. UV-visible spectroscopy showed that the absorption peak of the SPI was increased and red shifted after complexation with rutin. ITC confirmed that there was an interaction between rutin and SPI. This interaction was hydrophobic interaction and the binding process was entropy driven. This study shows that the foaming properties of plant-based proteins can be improved by forming complexes with flavonoids, which may be useful for foaming agents in foods.