Phenolics in sesame meal protein: Structural characterization, interaction mechanism, and impacts on protein functional properties.

This study characterized the phenolic profile of sesame meal protein (SMP) and investigated its binding interactions with proteins and the resulting effects on protein functional properties. Comprehensive phenolic profiling via UHPLC-HRMS/MS in both ESI+ and ESI- modes resulted in the identification of 145 compounds, comprising 61 phenolic acid derivatives, 43 flavonoids, 28 lignans, and 3 stilbenes. Notably, unlike other plant proteins, SMP retains unique sesame lignans. Molecular docking revealed that lignans (sesamin, sesaminol, sesamolin) exhibited the strongest affinity (-7.5 to -7.4 kcal/mol) with 11S globulin, primarily driven by hydrophobic and van der Waals interactions. Ultrasound-assisted ethanol dephenolization not only recovered valuable phenolics from sesame meal but also produced a modified protein (DPSMP) with improved purity, amino acid profile, color, solubility, emulsifying, and foaming properties. These results provide new insights into phenolic-protein interactions in sesame protein, offering potential strategies for targeted modification and high-value utilization of sesamin protein in food systems.