Quercetagetin loaded in soy protein isolate–κ-carrageenan complex: Fabrication mechanism and protective effect

•Quercetagetin exhibited high binding affinity with SPI–κ-CG complex.•Aggregate of SPI–quercetagetin–κ-CG was fabricated mainly through hydrophobic force.•SPI–κ-CG complex could obviously enhance the stability of quercetagetin.

In the present study, the potential of soy protein isolate (SPI)–κ-carrageenan (κ-CG) complex as a protective carrier for quercetagetin was investigated at different pH values (pH 2.3 and 6.5). The particle size of the ternary aggregates was slightly increased at pH 2.3, yet dramatically decreased at pH 6.5 with increasing quercetagetin concentration. Moreover, the negative ζ-potential of the ternary aggregates was increased significantly (p < 0.05) at pH 6.5. The addition of quercetagetin to the SPI–κ-CG complex could highly quench the intrinsic fluorescence of SPI. Circular dichroism spectra further suggested that the bound quercetagetin could induce the rise of β-sheet and β-turn contents at the cost of α-helix and unordered coil fractions of SPI. In addition, quercetagetin could increase the viscoelasticity of the ternary aggregates at both pH. Furthermore, the SPI–κ-CG complex was found to be superior to single SPI or κ-CG in terms of improving light stability and radical scavenging ability of quercetagetin.