Cited by 140Protein Hydrolysis and Bioactive PeptidesSeaweed-derived Bioactive CompoundsPeptidase Inhibition and Analysis

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

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Sun, Siqi, Xu, Xiaoting, Sun, Xue, Zhang, Xiaoqian, Chen, Xinping, Xu, Nianjun·2019·Marine Drugs

DOI 10.3390/md17030179PMC PMC6471128

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Abstract

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 IC50 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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Figure 1 Angiotensin I-converting enzyme (ACE) inhibitory activities of U. intestinalis protein hydrolysates produced by different enzymes. Each point is the mean of three determinations (n = 3) ± SD. Different letters indicate significant differences. The concentration of each hydrolysate was 2.5 mg/mL; crude protein (2.5 mg/mL) was used as the positive control.CC BY · PubMed Central

Figure 2 Effects of hydrolysis pH (A), temperature (B), substrate concentration (C), E/S ratio (D), and reaction time (E) on ACE inhibitory activity of protein hydrolysates from U. intestinalis.CC BY · PubMed Central

Figure 3 Contour plots and response surface plots for pH (A), temperature (B), and substrate concentration (C) to ACE inhibition rate.CC BY · PubMed Central

Figure 4 Sephadex G-25 gel filtration chromatogram of <3 kDa fraction of trypsin hydrolysate from U. intestinalis. (A) The fraction was divided into five parts (A–E) by Sephadex G-25. (B) The ACE inhibitory activity (1.5 mg/mL) and percentage of A–E. (C) The fraction was divided into three parts (C1–C3) by Sephadex G-15. (D) The ACE inhibitory activity (1.5 mg/mL) and percentage of C1 to C3.CC BY · PubMed Central

Figure 5 ACE inhibitory activity of fraction C2 from RP-HPLC. (A) The fraction was divided into 9 parts (C2-1 to C2-9) by RP-HPLC. (B) ACE inhibitory activity (1.5 mg/mL) and percentages of C2-1 to C2-9. Means with different lower case letters are significantly different (p < 0.05).CC BY · PubMed Central

Figure 6 The primary mass spectrogram and corresponding secondary mass spectrogram of FGMPLDR and MELVLR. (A) MS/MS spectra of FGMPLDR. (B) The secondary mass spectrogram of FGMPLDR. (C) MS/MS spectra of MELVLR. (D) The secondary mass spectrogram of MELVLR.CC BY · PubMed Central

Figure 7 Molecular docking results for FGMPLDR and MELVLR with ACE (PDB: 1O8A). (A) 3-D details of ACE and FGMPLDR interactions. (B) 2-D interaction details for FGMPLDR. (C) 3-D details of ACE and MELVLR interactions. (D) 2D interaction details for MELVLR.CC BY · PubMed Central

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Authors: Sun, S., Xu, X., Sun, X., Zhang, X., Chen, X., & Xu, N.
Affiliations: Ningbo University (CN)
Vanderbilt University Medical Center (US)
Corresponding author: Xu, Nianjun
ORCID: Sun, Siqi
Sun, Xue
Zhang, Xiaoqian
Chen, Xinping
Xu, Nianjun
Venue: Marine Drugs
Publisher: MDPI AG
Published: 2019-03-19
Volume: 17
Issue: 3
Pages: 179
ISSN: 1660-3397 (ISSN-L)
DOI: 10.3390/md17030179
PMC: PMC6471128
OpenAlex: W2922600776
Cited by: 140
References: 50
Citations by year: 2026: 9 · 2025: 21 · 2024: 29 · 2023: 22 · 2022: 27 · 2021: 15 · 2020: 14 · 2019: 3
FWCI: 4.88
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Marine Drugs (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Discover Archive (Vanderbilt University) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: Natural Science Foundation of Zhejiang Province (LZ17D060001)
Ningbo International Cooperation Program (2017D10019)
Ningbo Municipal Bureau of Science and Technology (2016C10034)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Keywords: ACE inhibitory peptides, Ulva intestinalis, seaweed, protein hydrolysates, trypsin hydrolysis, enzymatic hydrolysis optimization, peptide purification, antihypertensive peptides, food-derived bioactive peptides, zinc binding
MeSH terms: Angiotensin-Converting Enzyme Inhibitors, Antihypertensive Agents, Drug Stability, Hydrolysis, Hypertension, Peptidyl-Dipeptidase A, Peptide Hydrolases, Peptides, Protein Hydrolysates, Seaweed, Inhibitory Concentration 50, Ulva, Enzyme Assays, Molecular Docking Simulation

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

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