Dininurilmi Putri Suleman, Harijono, Jue-Liang Hsu
Proteolytic enzymes are widely used to produce protein hydrolysates that contain bioactive peptides. Some of bioactive peptides are known inhibit the angiotensin-I-converting enzyme (ACE, EC 3.4.15.1) and act as human antihypertensive. Therefore, this study aims to produce protein hydrolysates via 16 hours of digestion process using Chenopodium formosanum (red quinoa) seed and the proteases, namely pepsin, trypsin, α-chymotrypsin, and thermolysin. The hydrolysates profiles and ACE-I inhibitory activity were analyzed using reversed phase-high performance liquid chromatography (RP-HPLC). The SDS-PAGE was also used to analyze the main storage protein in red quinoa seed, identified as being 11S seed storage globulin. Meanwhile, the ACE inhibitor activities of red quinoa seed protein (RQSP) produced by various proteases include the hydrolysate of pepsin 17.03% ± 3.88%, trypsin 42.67% ± 3.19%, α-chymotrypsin 72.71% ± 2.85% and thermolysin 77.67% ± 0.98%. These results show that red quinoa seed protein is a potential source of significant ACE inhibitor activity when hydrolyzed with α-chymotrypsin and thermolysin. © 2024, Bogor Agricultural University. All rights reserved.
Department of Agricultural Product Technology, Faculty of Agricultural Technology, University of Brawijaya, Malang, 65145, Indonesia; Department of Biological Science and Technology, National Pingtung University Science and Technology, Neipu, Pingtung, 91201, Taiwan; Research Center for Animal Biologics, National Pingtung University of Science and Technology, Neipu, Pingtung, 91201, Taiwan; International Master’s Degree Program in Food Science, National Pingtung University of Science and Technology, Neipu, Pingtung, 91201, Taiwan
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