Investigation on the interaction of heated soy proteins with anthocyanins from cornelian cherry fruits.

The interaction between preheated soy proteins and anthocyanins from cornelian cherries was evaluated using a spectroscopic approach and molecular modeling. Structural changes of glycinin, β-conglycinin and soy protein isolate were investigated based on spectra of native and heat treated proteins in the presence of anthocyanins rich extracts from fresh cornelian cherry fruits. The fluorescence maximum emission in the presence of anthocyanins showed significant red shifts when compared with individual proteins, indicating the change of polarity in the surroundings of Trp residues from soy proteins toward more hydrophilic, which were attributed to protein-polyphenols interactions. Soy proteins interacted with cornelian cherries anthocyanins mainly through a static quenching mechanism. Glycinin presented a better affinity toward anthocyanins as revealed by the binding constant. The in silico approach was further employed to provide single molecule level details on the interaction between the main soy proteins and anthocyanins prevailing in cornelian cherry extracts. The docking results are consistent with the fluorescence spectroscopy data indicating better affinity of glycinin for cyanidin 3-glucoside and cyanidin 3-rutinoside, compared to the β-conglycinin. These findings deliver important insights for efficient development of microencapsulated powders based on soy proteins and anthocyanins from cornelian cherries, from the perspectives of obtaining value-added ingredients.