Moringa oleifera Lam. seed protein fibrils: Self-assembly and functional properties

This study aimed to identify the optimal preparation conditions for Moringa oleifera Lam. seed protein fibrils (MSPF) and comprehensively evaluate their structural characteristics and functional properties. MSPF were prepared under varied parameters, with fibrillization kinetics tracked via thioflavin (Th T) fluorescence (showing a typical 'S'-shaped curve) and structure characterized by transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FTIR), and UV-Vis spectroscopy. Optimal conditions were 4% (w/v) protein concentration, pH 1.5, and heating at 90 °C for 12 h, producing typical amyloid fibrils-short rod-like aggregates at 6 h and mature fibrillar structures at 12 h-with significantly increased β-sheet content. MSPF exhibited enhanced emulsifying activity (31.94 m²/g) and stability (95.45%), foaming capacity (93.67%), and ABTS⁺ free radical scavenging (63.15%), providing a solid theoretical basis for their application as sustainable functional ingredients in food processing.