Interaction of mulberry anthocyanins with soybean protein isolate: effect on the stability of anthocyanins and protein in vitro digestion characteristics

The interactions of anthocyanins and proteins might mutually influence each other on the physicochemical and functional properties. In this study, the interaction mechanism of soybean protein isolate (SPI) with mulberry anthocyanins (MA), and its effect on the thermal stability of anthocyanins and protein subunits' digestibility were investigated through multiple spectroscopies and in vitro gastrointestinal models. Results showed that cyanidin-3-O-glucoside (C3G), the main anthocyanin monomer in MA, could bind to SPI through hydrophobic interactions, resulting in static fluorescence quenching of SPI. The secondary structure of SPI changed by binding to C3G, with an increase of beta-sheet and a decrease of alpha-helix and random coil. The formation of the SPI-MA complexes improved the thermal stability of MA at 353 K, while, no significant protection occurred during heating at 368 K. Complexation with MA promoted the digestibility of SPI by pepsin, especially the alpha ' and alpha subunits of beta-conglycinin and the basic subunit of glycinin, and slightly delayed the digestibility of SPI under intestinal fluid. These results provide an in-depth understanding of the influence of the protein-anthocyanin interactions on the stability of anthocyanins and protein digestibility.

Automated summary

This study investigated the interaction mechanism between soybean protein isolate (SPI) and mulberry anthocyanins (MA) and found that it affects the thermal stability of anthocyanins and the digestibility of protein subunits.