Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization

文献类型: 外文期刊

第一作者: Guo, Huimin

作者: Guo, Huimin;Hao, Yuqiong;Chen, Yinhuan;Liu, Mengjie;Yang, Xiushi;Ren, Guixing;Guo, Huimin;Richel, Aurore;Everaert, Nadia

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关键词: Quinoa protein hydrolyzate; regulation of blood pressure; ACE inhibitory activity; peptide identification; molecular docking

期刊名称:JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE ( 影响因子:3.638; 五年影响因子:3.802 )

ISSN: 0022-5142

年卷期: 2020 年 100 卷 15 期

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收录情况: SCI

摘要: BACKGROUND Quinoa protein is a potential source of bioactive peptides. Although some studies have demonstrated its angiotensin converting enzyme (ACE) inhibitory properties, research into itsin vivoeffect on blood-pressure regulation and peptide characterization remains limited. RESULTS Quinoa protein hydrolyzate (QPH) was prepared by simulated gastrointestinal digestion. QPH lowered the systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive model rats (SHRs) from 2 h to10 h after oral administration, effectively controlling blood pressure in these SHRs. Anin vitrostudy showed that QPH is capable of inhibiting ACE activity. This was attributed to the activity of a number of low-molecular-weight peptides. With relatively high scores predicted by PeptideRanker, three promising bioactive peptides, FHPFPR, NWFPLPR, and NIFRPF, were further studied and their ACE-inhibition effects were confirmed with IC(50)values of 34.92, 16.77, and 32.40 mu M, respectively. A molecular docking study provided insights into the binding of ACE with peptides, and revealed that the presence of specific amino acids in the peptide sequence (Pro, Phe, and Arg at the C-terminal, and Asn at the N-terminal) could contribute to the interaction between ACE and peptides. CONCLUSION These results demonstrated the potential of QPH for the management of hypertension, which indicates that it could be a good candidate for inclusion in functional foods to control high blood pressure. (c) 2020 Society of Chemical Industry

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