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Antihypertensive Effect of the Peptides Derived from Casein by an Extracellular Proteinase from Lactobacillus helveticus CP790
Open accessAbstract
Peptides derived from alpha s1- and beta-caseins by the Lactobacillus helveticus CP790 proteinase were investigated for their inhibitory activities against angiotensin I-converting enzyme. The antihypertensive effect of casein hydrolysates in strain SHR spontaneously hypertensive rats was also investigated. Both alpha s1- and beta-casein hydrolysates inhibited this enzyme. Some of these peptides showed enzyme inhibitory activity, and one of them from beta-casein inhibited the enzyme greatly; the concentration of an angiotensin I-converting enzyme inhibitor needed to inhibit 50% of the enzyme activity was 4 microM. The hydrolysate of casein demonstrated antihypertensive activity in spontaneously hypertensive rats at an orally administered dosage of 15 mg/kg of body weight. MILK fermented with L. helveticus CP790, containing about .3% peptides, also showed antihypertensive activity in SHR rats with 5 ml/kg of body weight (15 mg of peptide/kg); however, the milk fermented with L. helveticus CP791, a variant defective for proteinase activity, did not show this activity. Results suggested that the peptides liberated from casein by the proteinase in the culture medium showed antihypertensive effect in SHR rats.
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“Some strains of L. helveticus such as CP790 (Yamamoto et al., 1994), CP53 (Ono et al., 1997), and PR4 (Di Cagno et al., 2006) are able to hydrolyze both αs1- and β-casein.”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Yamamoto et al., 1994
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Metadata
- Authors
- Yamamoto, N., Akino, A., & Takano, T.
- Affiliations
- Calpis Co., Ltd. (Japan) (JP)
- ORCID
- Yamamoto, Naoyuki
- Venue
- Journal of Dairy Science
- Publisher
- American Dairy Science Association
- Published
- 1994-04
- Volume
- 77
- Issue
- 4
- Pages
- 917-922
- ISSN
- 0022-0302 (ISSN-L)
- OpenAlex
- W2165457361
- Cited by
- 418
- References
- 25
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 10 · 2023: 17 · 2022: 12 · 2021: 6 · 2020: 22 · 2019: 16 · 2018: 13 · 2017: 16 · 2016: 20 · 2015: 22 · 2014: 15 · 2013: 12 · 2012: 22
- FWCI
- 2.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Dairy Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
- Keywords
- antihypertensive peptides, casein hydrolysate, Lactobacillus helveticus, extracellular protease, angiotensin-converting enzyme inhibition, αs1-casein, β-casein, spontaneously hypertensive rats, fermented milk, bioactive peptides
- MeSH terms
- Amino Acid Sequence, Animals, Caseins, Fermentation, Hydrolysis, Hypertension, Lactobacillus, Male, Milk, Molecular Sequence Data, Peptide Fragments, Endopeptidases, Rats, Inbred SHR, Rats, Inbred WKY, Rats
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