Enzymatic modification of millet prolamin by alcalase: structural characterization and functional enhancements

/g, 98.06 min) and foaming capacity and stability peaking at 30 min (147.50%) and 120 min (86.23%), respectively. Antioxidant activity was significantly elevated, with DPPH scavenging activity nearly doubled within 10 min, ABTS scavenging activity peaking at 76.43% at 60 min, and reducing power increased. Intrinsic fluorescence, UV-Vis, and FTIR spectroscopy confirmed protein conformational transitions through increased exposure of hydrophobic and aromatic residues and changes in amide bands. These findings demonstrate alcalase hydrolysis is an efficient strategy for producing bioactive peptides from MP, supporting its potential as a versatile, high-solubility functional ingredient in plant-based formulations, particularly in the development of food emulsions and antioxidant-rich dietary supplements.