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Open AccessArticle

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

1
Food Science Institute, Shanxi Normal University, Linfen 041004, China
2
Yunnan Institute of Food Safety, Kunming University of Science and Technology, Kunming, Yunnan 650500, China
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(24), 4562; https://doi.org/10.3390/molecules24244562
Received: 8 November 2019 / Revised: 5 December 2019 / Accepted: 10 December 2019 / Published: 12 December 2019
Albumin is the major fraction of quinoa protein that is characterized as having high nutritional value. However, until now, scant information is available on the bioactivity of quinoa albumin or its hydrolysates. To promote its usage, we extracted albumin in this study from quinoa bran assisted with cellulase and hemicellulose, and hydrolyzed it by alcalase and trypsin to produce bioactive peptides. The hydrolysates (QBAH) were purified by gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC), followed by identification using liquid chromatography–mass spectrometry (LC-MS/MS). Furthermore, based on in silico analysis, one angiotensin-I converting enzyme (ACE)-inhibitory and antioxidant peptide, RGQVIYVL (946.6 Da), and two antioxidant peptides, ASPKPSSA (743.8 Da), and QFLLAGR (803.5 Da), from QBAH were synthesized. RGQVIYVL showed a high ACE-inhibitory activity (IC50 = 38.16 μM) with competitive mode of inhibition, and showed significant antihypertensive effect in spontaneously hypertensive rats at a concentration of 100–150 mg/kg body weight (bw). Molecular docking simulation showed that it could interact with the active ACE site via hydrogen bonds with high binding power. Moreover, RGQVIYVL, ASPKPSSA, and QFLLAGR all demonstrated high ·OH scavenging activity (IC50 = 61.69–117.46 μM), ABTS+ scavenging activity (58.29–74.28%) and Fe2+ chelating ability (32.54–82.48% at 0.5 mg/mL). They could also retain activity after gastrointestinal enzyme digestion. These results indicate that quinoa albumin is a potential source of bioactive peptides possessing antioxidant and ACE-inhibitory activities. View Full-Text
Keywords: quinoa bran albumin; angiotensin-I converting enzyme; antioxidant peptides; inhibition kinetics; molecular docking; spontaneously hypertensive rats quinoa bran albumin; angiotensin-I converting enzyme; antioxidant peptides; inhibition kinetics; molecular docking; spontaneously hypertensive rats
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MDPI and ACS Style

Zheng, Y.; Wang, X.; Zhuang, Y.; Li, Y.; Tian, H.; Shi, P.; Li, G. Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking. Molecules 2019, 24, 4562.

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