Quinoa husks protein was extracted by high concentration ethanol from quinoa husks, and the protein was hydrolyzed by four kinds of proteases (alkaline, neutral, compound and flavor protease) to produce polypeptides. The molecular weight distribution and amino acid composition of quinoa protein, the enzymatic hydrolysis ability of four proteases and the activities of the polypeptides were determined. The results showed that quinoa husks protein with molecular weight of 22.8 kDa, 39.1 kDa and 52.7 kDa contained 17 kinds of amino acids, and the ratios of essential amino acids and hydrophobic amino acids to total amino acids were 35.17% and 28.48%, respectively. The hydrolysis ability of alkaline protease for quinoa husks protein was the highest, with degree of hydrolysis reached 13% at 120 min, and the peptides yield was 88.88%. The peptides produced by flavor protease showed high α-glucosidase inhibitory activity and Fe2+ chelating ability, which were 81.67% and 89.03% respectively; the inhibition rate of alkaline protease produced peptides against tyrosinase was 73.17%, while neutral protease produced peptides had strong scavenging ability to DPPH free radicals, which was 84.91%. This study showed that quinoa peptides had good biological activities, which could provide a theoretical basis for further development and utilization of quinoa husks.
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