Physicochemical, functional and antioxidant properties of mung bean protein enzymatic hydrolysates

This study aimed to investigate physicochemical, functional and antioxidant properties of mung bean protein (MBP) enzymatic hydrolysates (MBPEHs) by alcalase, neutrase, protamex, flavourzyme and papain. Physicochemical properties were evaluated by SDS-PAGE, particle size distribution, FTIR, ultraviolet visible and fluorescence spectrophotometries. ABTS, hydroxyl scavenging, Fe²⁺ chelating activity were used to evaluate antioxidant activity. Enzymolysis with five proteases decreased average particle size, α-helix, β-sheet, surface hydrophobicity of hydrolysates. Alcalase hydrolysate had the highest degree of hydrolysis (23.55%), absolute zeta potential (33.73 mV) and the lowest molecular weight (<10 kDa). Protamex and papain hydrolysates had higher foaming capacities, emulsification activity indexes, emulsion stability indexes (235.00%, 123.07 m²/g, 132.54 min; 200.10%, 105.39 m²/g, 190.67 min) than MBP (135.03%, 20.03 m²/g, 30.88 min). Alcalase hydrolysate demonstrated the lowest IC₅₀ (mg/mL) in ABTS (0.12), hydroxyl (2.98), Fe²⁺ chelating (0.22). These results provide support for application of MBPEHs as foaming agent, emulsifier and antioxidant in food industry.