Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste
Abstract
A hendeca-peptide with angiotensin I-converting enzyme (ACE) inhibitory activity was isolated from the pepsin hydrolysate of algae protein waste, a mass-produced industrial by-product of an algae essence from microalgae, Chlorella vulgaris. Edman degradation revealed its amino acid sequence to be Val-Glu-Cys-Tyr-Gly-Pro-Asn-Arg-Pro-Gln-Phe. Inhibitory kinetics revealed a non-competitive binding mode with IC₅₀ value against ACE of 29.6μM, suggesting a potent amount of ACE inhibitory activity compared with other peptides from the microalgae protein hydrolysates which have a reported range between 11.4 and 315.3μM. In addition, the purified hendeca-peptide completely retained its ACE inhibitory activity at a pH range of 2-10, temperatures of 40-100°C, as well as after treatments in vitro by a gastrointestinal enzyme, thus indicating its heat- and pH-stability. The combination of the biochemical properties of this isolated hendeca-peptide and a cheap algae protein resource make an attractive alternative for producing a high value product for blood pressure regulation as well as water and fluid balance.
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Blood pressure regulation primarily involves the renin-angiotensin system, where renin and ACE play central roles.
“Blood pressure regulation primarily involves the renin-angiotensin system (RAS), where the enzymes renin and angiotensin-converting enzyme ACE play central roles [44].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [44]
Peptides VECYGPNRPQF from Chlorella vulgaris and tripeptides Trp-Val and Val-Trp from Chlorella sorokiniana exhibit potent ACE inhibition.
“Peptides such as VECYGPNRPQF from Chlorella vulgaris [44] and tripeptides like Trp-Val and Val-Trp from Chlorella sorokiniana [62] exhibit potent ACE inhibition.”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [44]
Renin converts angiotensinogen into angiotensin I, which ACE transforms into angiotensin II, a potent vasoconstrictor that raises blood pressure.
“Renin converts angiotensinogen into angiotensin I, which is then transformed by ACE into angiotensin II, a potent vasoconstrictor that raises blood pressure.”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [44]
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- Authors
- Sheih, I.-C., Fang, T. J., & Wu, T.-K.
- Affiliations
- National Chung Hsing University (TW)
- National Yang Ming Chiao Tung University (TW)
- Corresponding author
- Wu, Tung-Kung
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 115
- Issue
- 1
- Pages
- 279-284
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W2075270505
- Cited by
- 280
- References
- 26
- Citations by year
- 2026: 4 · 2025: 17 · 2024: 11 · 2023: 16 · 2022: 17 · 2021: 17 · 2020: 19 · 2019: 24 · 2018: 15 · 2017: 19 · 2016: 20 · 2015: 17 · 2014: 17 · 2013: 23 · 2012: 12
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Food Chemistry (publishedVersion)
- Funders
- Ministry of Earth Sciences
- National Science Council
- Novo Nordisk
- Ministry of Education, India
- National Chiao Tung University
- 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 I-converting enzyme inhibitory peptides, Chlorella vulgaris, pepsin hydrolysate, non-competitive inhibition, peptide stability, blood pressure regulation, bioactive peptides
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