Utilization of soybean protein isolate hydrolysates as carriers: Improved encapsulation efficiency and stability of curcumin.

This study aimed to explore the potential of soybean protein isolate hydrolysates (SPIH) prepared via Alcalase as delivery carriers and develop novel SPIH-Cur nanoparticles. Hydrolysis caused the varying degrees degradation in the 7S and 11S subunits, significantly enhancing SPI's antioxidant activity. The reduction in particle size and the exposure of hydrophobic groups in SPIH contributed to the formation of stable SPIH-Cur nanoparticles, due to their well binding capacity to curcumin (Cur). The 30 min SPIH-Cur sample exhibited the highest encapsulation efficiency (83.09 %), owing to its high binding affinity (Ka = 9.56 × 10 M). Encapsulation by SPIH also significantly improved Cur's thermal and light stability. Moreover, FTIR, fluorescence spectra, and molecular docking analyses revealed that the formation of SPIH-Cur were primarily driven by hydrophobic forces and hydrogen bonds. Above results provide a foundation for fabricating nanoparticles that deliver lipophilic bioactive compounds with high encapsulation efficiency and stability derived from SPIH.