دورية أكاديمية
Isolation, Structural Identification and in Vitro Activity Evaluation of Angiotensin-Converting Enzyme Inhibitory Peptides from Moringa oleifera Seeds
| العنوان: | Isolation, Structural Identification and in Vitro Activity Evaluation of Angiotensin-Converting Enzyme Inhibitory Peptides from Moringa oleifera Seeds |
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| المؤلفون: | ZHONG Yuwang, XU Wanli, FAN Yaozhu, LI Yiyan, WANG Xuefeng |
| المصدر: | Shipin Kexue, Vol 44, Iss 24, Pp 118-126 (2023) |
| بيانات النشر: | China Food Publishing Company, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Food processing and manufacture |
| مصطلحات موضوعية: | moringa oleifera seeds, angiotensin-converting enzyme inhibitory peptide, high performance liquid chromatography-tandem mass spectrometry, molecular docking, secondary structure, enzymatic inhibition kinetics, Food processing and manufacture, TP368-456 |
| الوصف: | In this study, angiotensin-converting enzyme (ACE) inhibitory peptides from an enzymatic hydrolysate of Moringa oleifera seeds were separated by sequential ultrafiltration and ion exchange chromatography. The peptide sequences were identified by high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) and potential ACE inhibitory peptides were selected by bioinformatics and molecular docking; their secondary structure was analyzed by Fourier transform infrared (FTIR) spectroscopy and their in vitro activity was evaluated by enzymatic inhibition kinetics and the methyl thiazolyl tetrazolium (MTT) method. The results showed that peptide fraction F-b had a good antihypertensive effect. A total of 11 peptide sequences were identified. Peptide QGPRPQ was identified as a potential ACE inhibitory peptide with a half-maximum inhibitory concentration (IC50 ) (1.15 ± 0.3) mmol/L. Molecular docking showed that QGPRPQ could better bind to ACE through hydrogen bond and hydrophobic interaction. Secondary structure analysis showed that QGPRPQ was composed of 22.8% α-helix, 33.3% β-fold and 43.9% β-turn. The mode of inhibition of QGPRPQ was mixed type, and it had no toxic effect on HepG2 cells at a concentration lower than 0.01 mg/mL. This study can provide an important theoretical basis for the development and utilization of hypotensive peptides derived from M. oleifera seed protein. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English Chinese |
| تدمد: | 1002-6630 |
| العلاقة: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-24-016.pdfTest; https://doaj.org/toc/1002-6630Test |
| DOI: | 10.7506/spkx1002-6630-20220926-284 |
| الوصول الحر: | https://doaj.org/article/68c3792aba9b4866b315e4f2c05521bfTest |
| رقم الانضمام: | edsdoj.68c3792aba9b4866b315e4f2c05521bf |
| قاعدة البيانات: | Directory of Open Access Journals |
| تدمد: | 10026630 |
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| DOI: | 10.7506/spkx1002-6630-20220926-284 |