Interaction characterization of preheated soy protein isolate with cyanidin-3-O-glucoside and their effects on the stability of black soybean seed coat anthocyanins extracts

The interactions of soy protein isolate with cyanidin-3-O-glucoside were investigated to study the protective effect of protein on anthocyanin’s stability by UV–Vis spectrophotometry, Fourier transform infrared spectroscopy, circular dichroism and fluorescence spectroscopy. Preheat treatment and binding of cyanidin-3-O-glucoside effectively changed the secondary structure of soy protein isolate, with a decrease in α-helix, random coil structure and an increase in β-sheet and β-turn. The soy protein isolate preheated at 121 °C exhibited a strong binding affinity towards cyanidin-3-O-glucoside with strong Ks of 147.40 × 104 M−1 and also effectively increased the thermal and oxidation stabilities of black soybean seed coat extract via decreasing the degradation rate by 67% and 23%, respectively. Soy protein isolate interacted with cyanidin-3-O-glucoside mainly through hydrophobic interactions and static quenching process. Altogether, the results suggested that preheated soy protein isolate-cyanidin-3-O-glucoside interaction could effectively protect anthocyanins’ stability through strong binding affinity influenced by the systematic alterations in the secondary structure.