Identification of ACE inhibitory peptides from red alga Mazzaella japonica
Open accessAbstract
Angiotensin I converting enzyme (ACE) inhibition is one of the key factors for cardiovascular disease, and inhibition of ACE activity is related to the prevention of high blood pressure. Until now, some ACE inhibitory peptides have been found in the protein hydrolysates of red algae, and most of them were derived from phycobiliproteins and rubisco. In this study, we modified the preparation method to evaluate the potential of ACE inhibitory activity from protein hydrolysate of red alga Mazzaella japonica except for phycobiliproteins and rubisco. As a result, we identified 11 peptides (YRD, VSEGLD, TIMPHPR, GGPAT, SSNDYPI, SRIYNVKSNG, VDAHY, CPYDWV, YGDPDHY, NLGN and DFGVPGHEP) in the hydrolysate by the reversed phase-HPLC and MALDI-TOF/MS/MS. Among them, YRD would be derived from phycoerythrin α-subunit. However, the others would be from other proteins encoded in chloroplast or nuclear genomes. This study revealed that not only phycobiliproteins and rubisco but also the other proteins in red algae have the potential for the source of ACE inhibitory peptide.
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Peptides from Gracilariopsis lemaneiformis, Mazzaella japonica, and Ulva intestinalis contribute to ACE inhibition and cardiovascular health.
“Other promising peptides have been identified from Gracilariopsis lemaneiformis, Mazzaella japonica (Rhodophyta), and Ulva intestinalis (Chlorophyta), each contributing to ACE inhibition and cardiovascular health [58–60].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [58]
The Results (§6, page not available) report ACE-inhibitory activity in fractions of a Mazzaella japonica protein hydrolysate and identify peptides in those fractions. The Introduction links ACE inhibition to blood-pressure control, but the paper reports no human or animal studies, so a contribution to cardiovascular health is not established. This citation supports the Mazzaella japonica portion of the multi-source sentence, not claims about the other algae. (LLM, conf=0.86)
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- Authors
- Kumagai, Y., Kitade, Y., Kobayashi, M., Watanabe, K., Kurita, H., Takeda, H., Yasui, H., & Kishimura, H.
- Affiliations
- Hokkaido University (JP)
- Hokkaido Research Organization (JP)
- Corresponding author
- Kishimura, Hideki
- Venue
- European Food Research and Technology
- Published
- 2020-07-21
- Volume
- 246
- Issue
- 11
- Pages
- 2225-2231
- ISSN
- 0373-0174 (ISSN-L)
- 1438-2377
- 1438-2385
- OpenAlex
- W3045360608
- Cited by
- 37
- References
- 36
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 9 · 2023: 6 · 2022: 7 · 2021: 4
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Locations
- European Food Research and Technology (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Hokkaido University Collection of Scholarly and Academic Papers (Hokkaido University) (submittedVersion)
- Funders
- Science and Technology Research Promotion Program for Agriculture, Forestry, Fisheries and Food Industry
- 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
- ACE inhibitory peptides, red algae, protein hydrolysates, angiotensin-converting enzyme, phycobiliproteins, phycoerythrin, Rubisco, blood pressure, cardiovascular disease prevention, peptide identification
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