The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Citations
Cites
Church, F., Swaisgood, H. E., Porter, D. H., & Catignani, G. L. (1983) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(83)81926-2 · Cited by 1,579
Cushman, D. W., Cheung, H. S., Sabo, E. F., & Ondetti, M. A. (1977) · Biochemistry · doi:10.1021/bi00644a014 · Cited by 893
Angiotensin I converting enzyme.
Erdös, E. G. (1975) · Circulation Research · doi:10.1161/01.res.36.2.247 · Cited by 555
Ondetti, M. A., Williams, N. J., Sabo, E. F., PLUSCEC, J., Weaver, E. R., & Kocy, O. (1971) · Biochemistry · doi:10.1021/bi00798a004 · Cited by 521
Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom
Ferreira, S. H., Bartelt, D. C., & Greene, L. J. (1970) · Biochemistry · doi:10.1021/bi00815a005 · Cited by 515
Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom
J.P. (1971) · Toxicon · doi:10.1016/0041-0101(71)90098-5 · Cited by 480
Maruyama, S., Nakagomi, K., Tomizuka, N., & Suzuki, H. (1985) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1985.10866901 · Cited by 201
(1981) · Cited by 154
Antihypertensive effect of tryptic hydrolysate of milk casein in spontaneously hypertensive rats
Karaki, H., Kunio, D., SUGANO, S., Hideyo, U., Ryuji, S., Umeji, M., & Takemoto, S. (1990) · Comparative Biochemistry and Physiology Part C Comparative Pharmacology · doi:10.1016/0742-8413(90)90023-3 · Cited by 135
Maruyama, S., Mitachi, H., Tanaka, H., Tomizuka, N., & Suzuki, H. (1987) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.51.1581 · Cited by 126
Research works printed but not linked: 1
- Exterkate, 1975, An introductory study of the proteolytic system of Streptococcus cremoris strain HP, Neth. Milk Dairy J., 29, 303
Cited by
Sorted by citations
Items 401–414 of 414
Lecouvey, M., Frochot, C., Miclo, L., Orlewski, P., Marraud, M., Gaillard, J., Cung, M. T., & Vanderesse, R. (1997) · Letters in Peptide Science · doi:10.1023/a:1008813325683
Separación e identificación de péptidos bioactivos liberados por bacterias lácticas
González-Olivares, L. G. (2011) · doi:10.24275/uami.x059c754b
Shu, G., Yang, H., Chen, H., Zhang, Q., & Tian, Y. (2015) · Acta Scientiarum Polonorum Technologia Alimentaria · doi:10.17306/j.afs.2.12
Genetics of Lactic Acid Bacteria
McAuliffe, O. E. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-15956-5.00004-x
Savinova, О. S., Shabaev, A. V., & Fedorova, T. V. (2025) · Applied Biochemistry and Microbiology · doi:10.1134/s0003683825601209
Bioactive peptides from fermented non-bovine milks and their applications
Sharma, H., Rao, P. S., & Kumar, M. H. S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-23561-0.00011-6
Qi, D., Nie, X.-L., & Zhang, J. (2020) · Figshare · doi:10.6084/m9.figshare.12197319
Study of Alfalfa and Flaxseed Gums as Co-structurants in Probiotic Cryogel Scaffolds
Hellebois, T. (2023) · theses.fr (ABES) · doi:10.70675/7fc5548fz9c8fz4f0cza206z7f499edd9246
Oliveira, J. M. S., Silva, R., Pimentel, T. C., Arruda, H. S., Borsoi, F. T., Pastore, G. M., Morais, S. T. B., Bertolo, M. R. V., Martins, V. C. A., Bogusz, S., et al. (2026) · International Journal of Dairy Technology · doi:10.1111/1471-0307.70136
Gao, F., Deng, L., Cui, B., Zhang, F., Jiang, Y., Mu, G., & Tuo, Y. (2026) · Journal of Dairy Science · doi:10.3168/jds.2025-28065
Li, H., Du, Y., Zhang, Z., Zhao, Z., Li, S., Sun, Y., Wang, Z., & Zhang, X. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120197
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review