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Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinali...

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Autores principales: Sun, Siqi, Xu, Xiaoting, Sun, Xue, Zhang, Xiaoqian, Chen, Xinping, Xu, Nianjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6471128/
https://www.ncbi.nlm.nih.gov/pubmed/30893907
http://dx.doi.org/10.3390/md17030179
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author Sun, Siqi
Xu, Xiaoting
Sun, Xue
Zhang, Xiaoqian
Chen, Xinping
Xu, Nianjun
author_facet Sun, Siqi
Xu, Xiaoting
Sun, Xue
Zhang, Xiaoqian
Chen, Xinping
Xu, Nianjun
author_sort Sun, Siqi
collection PubMed
description Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC(50) values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides.
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spelling pubmed-64711282019-04-27 Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis Sun, Siqi Xu, Xiaoting Sun, Xue Zhang, Xiaoqian Chen, Xinping Xu, Nianjun Mar Drugs Article Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC(50) values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides. MDPI 2019-03-19 /pmc/articles/PMC6471128/ /pubmed/30893907 http://dx.doi.org/10.3390/md17030179 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sun, Siqi
Xu, Xiaoting
Sun, Xue
Zhang, Xiaoqian
Chen, Xinping
Xu, Nianjun
Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title_full Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title_fullStr Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title_full_unstemmed Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title_short Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
title_sort preparation and identification of ace inhibitory peptides from the marine macroalga ulva intestinalis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6471128/
https://www.ncbi.nlm.nih.gov/pubmed/30893907
http://dx.doi.org/10.3390/md17030179
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