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Cited by 46Protein Hydrolysis and Bioactive PeptidesProbiotics and Fermented FoodsEnzyme Production and Characterization

The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.

Purification and characterization of an endopeptidase that has an important role in the carboxyl terminal processing of antihypertensive peptides in Lactobacillus helveticus CM4

Ueno, K., Mizuno, S., Yamamoto, N.·2004·Letters in Applied Microbiology
DOI 10.1111/j.1472-765x.2004.01560.x
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Abstract

AIMS: To purify and characterize a peptidase that can catalyse C-terminal processing of antihypertensive peptide from Lactobacillus helveticus CM4. METHODS AND RESULTS: An endopeptidase which seems to process the carboxyl terminal end of two antihypertensive peptides, Val-Pro-Pro and Ile-Pro-Pro, was purified from Lactobacillus helveticus CM4 by four stages of column chromatography, using synthetic pro-peptide as a substrate. The molecular weight of the purified enzyme was estimated to be 67,000 by SEPHACRYL S-200 and 70,000 by SDS-PAGE analysis. The purified enzyme generated: (i) Val-Pro-Pro from Val-Pro-Pro-Phe-Leu and Val-Pro-Pro-Phe-Leu-Gln-Pro, and (ii) Ile-Pro-Pro from Ile-Pro-Pro-Leu-Thr and Ile-Pro-Pro-Leu-Thr-Gln-Thr, but theses peptides could not be generated from Val-Pro-Pro-Phe, Val-Pro-Pro-Phe-Leu-Gln, Ile-Pro-Pro-Leu and Ile-Pro-Pro-Leu-Thr-Gln. Part of the amino terminal sequence of the purified enzyme had homology to a previously reported pepO gene product. CONCLUSION: These results suggest that the purified endopeptidase isolated in this study have an important role in the carboxyl terminal processing of two antihypertensive peptides in Lact. helveticus CM4.

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Crossref · 10.1111/j.1472-765x.2004.01560.x

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17 of 17 references verified0 citation errors · 0 not checkable

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  • The endopeptidase isolated from L. helveticus CM4 is a key player in the hydrolysis of the C-terminal during the production of Val-Pro-Pro and Ile-Pro-Pro in fermented milk.

    “Based on the results, it was suggested that the enzyme is a key player in the hydrolysis of the C-terminal during the production of Val-Pro-Pro and Ile-Pro-Pro in fermented milk.”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Ueno et al., 2004

  • An endopeptidase with the ability to hydrolyze peptides Val-Pro-Pro-Phe-Leu and Ile-Pro-Pro-Leu-Thr to produce Val-Pro-Pro and Ile-Pro-Pro, respectively, was isolated and characterized from L. helveticus CM4.

    “An endopeptidase with the ability to hydrolyze peptides Val-Pro-Pro-Phe-Leu and Ile-Pro-Pro-Leu-Thr to produce Val-Pro-Pro and Ile-Pro-Pro, respectively, was isolated and characterized from L. helveticus CM4 (Ueno et al., 2004).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Ueno et al., 2004

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  1. 10.1016/0378-1097(94)90389-1 · DOI

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Metadata

Authors
Ueno, K., Mizuno, S., & Yamamoto, N.
Affiliations
Calpis Co., Ltd. (Japan) (JP)
Corresponding author
Yamamoto, N.
ORCID
Venue
Letters in Applied Microbiology
Publisher
Oxford University Press (OUP)
Published
2004-10
Volume
39
Issue
4
Pages
313-318
ISSN
  • 0266-8254 (ISSN-L)
  • 1365-2673
DOI
10.1111/j.1472-765x.2004.01560.x
OpenAlex
W2063253668
Cited by
46
References
17
Citations by year
2026: 1 · 2025: 3 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 3 · 2013: 2 · 2012: 5
FWCI
0.83
Type
journal article
Language
en
Open access
closed
Licence
doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 3987 d)
Locations
  • Letters in Applied Microbiology (publishedVersion)
  • PubMed (publishedVersion)
  • Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
endopeptidase, antihypertensive peptides, C-terminal processing, Val-Pro-Pro, Ile-Pro-Pro, propeptide, enzyme purification, bioactive peptides, probiotics
MeSH terms
Antihypertensive Agents, Lactobacillus, Oligopeptides, Endopeptidases, Substrate Specificity

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