Unraveling structure–function relationships and antioxidant stability of Ferula assafoetida seed protein hydrolysates with physicochemical and sensory characterization

Plant protein hydrolysates are increasingly explored as sustainable functional ingredients; however, limited information is available on the structure–function relationships and stability of hydrolysates derived from Ferula assafoetida seed protein as a safe and bioactive source. Thereby, this study aimed to elucidate the structural, functional, and antioxidant properties of its protein hydrolysates. Seed proteins were extracted using an alkaline method, yielding 38.0 ± 0.2 mg/g, and subsequently hydrolyzed enzymatically. Hydrolysis markedly reduced particle size (from 1663.1 to 274.6 nm) and dispersity, accompanied by a shift in ζ-potential from −19.1 to −2.0 mV, indicating altered surface charge and improved colloidal uniformity. Structural analyses (SEM, FT-IR, XRD, UV-Vis, and SDS-PAGE) confirmed extensive protein degradation into peptides