Physico-chemical properties, antioxidant activities and angiotensin-I converting enzyme inhibitory of protein hydrolysates from Mung bean (Vigna radiate).

Mung bean Protein hydrolyses (MBPHs) have attracted a great deal of attention due to their variety of biological activities. In present study, MBPHs were fractionate according to the molecular mass into three fractions of MBPHs-I (<3 kDa), MBPHs-II (3-10 kDa) and MBPHs-III (>10 kDa). Their antioxidant activity and angiotensin-I converting enzyme (ACE) inhibitory of were investigated in vitro. Results showed that the alcalase-derived hydrolysate exhibited the highest degree of hydrolysis (DH) and trichloroacetic acid-nitrogen soluble index (TCA-NSI) versus those of other enzyme hydrolysates. MBPHs-I presented the best scavenge DPPH, hydroxyl radicals, superoxide radicals, Fe2+ chelating activities, and the best ACE inhibitory activity (IC50 = 4.66 μg/mL) than that of MBPHs and MBPHs-III. And MBPHs-I rich in hydrophobic and aromatic amino acids, and its secondary structure mainly contain α-helix, β-sheet and irregular coiled. Results indicated that MBPHs-I has a great potential as natural functional materials for supplement.