Abstract
The Perilla seed meal (PSM) protein was hydrolyzed with Flavourzyme; the hydrolysate was fractionated by an ultrafiltration and its physiological activity was measured. Peptides with low molecular weights exhibited higher antioxidant activity, except for the Fe<sup>2+</sup> chelating activity, compared to peptides with a high molecular weight. The IC<sub>50</sub> values of the α-amylase inhibitory activity ranged from 727.89 µg/ml to 757.18 µg/ml, the α-glucosidase inhibitory activity was highest in the &lt; 1 kDa fraction. The &lt; 1 kDa fraction exhibited the strongest angiotensin I-converting enzyme inhibitory activity. As a result, the peptides from PSM protein hydrolysates, particularly peptides &lt; 1 kDa, exhibited excellent antioxidant, antidiabetic, and antihypertensive activities and thus were highly likely to be developed as a functional food material.
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