Bioactivity and structural characterization of black sesame protein hydrolysate: Impact of enzymatic hydrolysis strategies

This study employed enzymatic hydrolysis to treat black sesame protein and investigated the relationship between the structure of the hydrolysates and their xanthine oxidase (XOD) inhibitory activity. The results indicated that the hydrolysate prepared with alkaline protease (A-BSPH) exhibited the highest XOD inhibitory activity, with an IC 50 value of 24.48 ± 0.22 mg/mL. This superior activity could be attributed to the broad specificity of alkaline protease, which produced hydrolysates with a lower molecular weight and a higher content of exposed aromatic amino acids, while maintaining favorable surface hydrophobicity. Furthermore, the hydrolysate retained its XOD inhibitory activity after simulated gastrointestinal digestion. In conclusion, this study provides a theoretical foundation for the use of black sesame protein hydrolysate as a potential XOD inhibitor.