Angiotensin Converting Enzyme (ACE) Inhibitory Peptides: Production and Implementation of Functional Food
Abstract
In recent decades, the most successful strategy for controlling blood pressure has been inhibition of the angiotensin-converting enzyme (ACE). ACE inhibitors of chemical synthesis (captopril, enalapril, ramipril and trandolapril) have been widely used clinically to reduce mortality in patients with heart failure, and in patients with recent myocardial infarction and heart failure or marked left ventricular dysfunction. In addition to preventive and therapeutic drugs, increased attention has been paid to identifying dietary compounds that may contribute to cardiovascular treatment and prevention. ACE inhibitory peptides, derived from a multitude of plant and animal proteins such as milk, soy or fish, represent sources of health-enhancing components. These ACE inhibitory peptides can be enzymatically released from precursor proteins in vitro and in vivo, respectively during food processing and gastrointestinal digestion. They have shown the ability to lower blood pressure by limiting the vasoconstrictory effects of Angiotensin II and potentiating the vasodilatory effects of Bradykinin. By using specific procedures they may be generated in or incorporated into functional foods for the development of 'natural' beneficial health products. Several products containing peptides with ACE inhibitory properties are currently on the market or in development. This review focuses on the use, application and future perspective of bioactive peptides with properties relevant to cardiovascular…
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Several studies have shown that over and above basic nutrition, additional health benefits may be provided by specific amino acids and bioactive peptides.
“Several studies have also shown that over and above that of basic nutrition, additional health benefits may be provided by specific amino acids and bioactive peptides (7,68 -81) .”
From Protein quality evaluation twenty years after the introduction of the protein digestibility corrected amino acid score method (2012) · cites this paper as [72]
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References 193 · Cited by 149
- Authors
- De Leo, F., Panarese, S., Gallerani, R., & Ceci, L.
- Affiliations
- Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IT)
- ORCID
- Ceci, L.
- Venue
- Current Pharmaceutical Design
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2009-11-01
- Volume
- 15
- Issue
- 31
- Pages
- 3622-3643
- ISSN
- 1381-6128 (ISSN-L)
- OpenAlex
- W2147653965
- Cited by
- 149
- References
- 193
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 8 · 2023: 8 · 2022: 9 · 2021: 11 · 2020: 6 · 2019: 8 · 2018: 3 · 2017: 13 · 2016: 6 · 2015: 12 · 2014: 9 · 2013: 18 · 2012: 11
- FWCI
- 3.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Pharmaceutical Design (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- angiotensin I-converting enzyme inhibitory peptides, bioactive peptides, functional foods, blood pressure reduction, angiotensin II, bradykinin, cardiovascular health, dietary peptides, ACE inhibitors
- MeSH terms
- Angiotensin-Converting Enzyme Inhibitors, Animals, Blood Pressure, Cardiovascular Diseases, Dietary Proteins, Food, Humans, Peptides, Protein Precursors
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