Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein
Abstract
Hydrolysates containing angiotensin-I converting enzyme (ACE)-inhibitory peptide were prepared from Enteromorpha clathrata protein using alcalase. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10kDa) by ultrafiltration. The below-10kDa fraction showed higher ACE-inhibitory activity and was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of active peptide was identified as Pro-Ala-Phe-Gly by HPLC-Q-TOF-MS and its IC50 value was 35.9μM. The yield of this peptide from E. clathrata protein was 0.82%. Lineweaver-Burk plots demonstrated that the inhibitory kinetic mechanism of this peptide was non-competitive. Stability study revealed that the purified peptide showed resistance against gastrointestinal proteases. Thus, E. clathrata protein hydrolysate treated with alcalase is a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension and related diseases.
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Seaweed-derived peptides from Undaria pinnatifida, Neopyropia yezoensis, Ulva rigida, and Ulva clathrata have shown ACE inhibitory activity.
“Among seaweed-derived peptides, species such as Undaria pinnatifida (Phaeophyceae), Neopyropia yezoensis (formerly Porphyra yezoensis) (Rhodophyta), Ulva rigida, and Ulva clathrata (formerly Enteromorpha clathrata) have shown ACE inhibitory activity [53–57].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [57]
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References 46 · Cited by 110
- Authors
- Pan, S., Wang, S., Jing, L., & Yao, D.
- Affiliations
- Jiangsu Ocean University (CN)
- Institute of Botany, Jiangsu Province and Chinese Academy of Sciences (CN)
- Corresponding author
- Pan, Saikun
- Yao, Dongrui
- ORCID
- Wang, Shujun
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 211
- Pages
- 423-430
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W2392654232
- Cited by
- 110
- References
- 46
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 15 · 2023: 10 · 2022: 16 · 2021: 11 · 2020: 9 · 2019: 10 · 2018: 9 · 2017: 7 · 2016: 5
- FWCI
- 5.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Priority Academic Program Development of Jiangsu Higher Education Institutions (5511201401X-21)
- Science and Technology Project of Lianyungang (CXY1320)
- Open-end Funds of Jiangsu Key Laboratory of Marine Biotechnology
- Huaihai Institute of Technology (2009HS07)
- National Science and Technology Pillar Program of China (2012BAC07B00)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- angiotensin-converting enzyme inhibition, bioactive peptides, Enteromorpha clathrata, alcalase hydrolysis, peptide purification, non-competitive inhibition, hypertension, nutraceuticals
- MeSH terms
- Angiotensin-Converting Enzyme Inhibitors, Chromatography, Gel, Molecular Weight, Oligopeptides, Peptide Hydrolases, Plant Proteins, Protein Hydrolysates, Inhibitory Concentration 50, Ulva
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