Co-delivery mechanism of curcumin/catechin complex by modified soy protein isolate: Emphasizing structure, functionality, and intermolecular interaction

Modifying proteins to enhance their affinity for polyphenols is essential for developing a practical and efficient delivery system that promotes the synergistic effects of bioactive substances. The study investigated the nanoparticle complexation in both pure soy protein isolate (SPI) or SPI modified by ultrasonic combined heat treatment (UHSPI) with varying concentrations of curcumin/catechin (CU/CA) complex, and its effects on the functionality, structure and conformational changes of protein-polyphenol nanocomplexes. Additionally, the intermolecular interaction and co-delivery mechanisms of nanocomplexes were analyzed. Results showed that the physical modification process (28/40 kHz, 90 degrees C, 15 min) and a rational concentration of CU/CA (0.6 mg/ mL) improve the encapsulation efficiency of polyphenols by SPI (up to 77% for curcumin, and 93% for catechin), resulting in a higher DPPH and ABTS scavenging capacity, along with the highest emulsification activity index, as well as enhanced storage stability and thermal stability. The interaction between UHSPI and CU/CA disrupted the protein's secondary structure and exposed more hydrophobic residues to a hydrophilic environment, and exhibited stronger fluorescence quenching. Molecular docking analysis revealed that protein-polyphenol interactions primarily relied on hydrogen bonds and hydrophobic interactions, and 11S subunits exhibited higher affinity with CU/CA. FTIR, fluorescence spectra, and XRD further confirmed the enhanced interaction ability between UHSPI and CU/CA, resulting in the formation of a more stable nanocomplex. Overall, the modified SPI effectively facilitates the co-delivery of an appropriate concentration of curcumin/catechin complex.