Cited by 17Probiotics and Fermented FoodsEnzyme Production and CharacterizationBacterial Genetics and Biotechnology

Classification of Lactobacillus helveticus Strains by Immunological Differences in Extracellular Proteinases

YAMAMOTO, Naoyuki, ONO, Hiroko, MAENO, Masafumi, UEDA, Yuudai, TAKANO, Toshiaki, MOMOSE, Haruo·1998·Bioscience, Biotechnology, and Biochemistry

Abstract

Polyclonal antibodies against an extracellular proteinase of Lactobacillus helveticus CP53 were raised. The antibodies reacted with a 170-kDa enzyme with activity and a 53-kDa protein that seemed to be a degradation product of the 170-kDa proteinase from results of immunoblotting. The antibodies reacted also with a 45-kDa extracellular proteinase of L. helveticus CP790. However, monoclonal antibodies to the CP790 proteinase did not react with the proteinase of L. helveticus CP53. Seventeen strains of L. helveticus were tested for immunological reactivity with the two kinds of antibodies. The strains all had the same reactivity as either strain CP53 or strain CP790. Eleven strains with the 45-kDa proteinase were identified as L. helveticus biovar jugurti because they did not ferment maltose, four other strains with the 170- and 53-kDa proteins were identified as L. helveticus biovar helveticus because they fermented maltose. The remaining two strains dit not fit this pattern; they had both the 170- and 53-kDa proteins, but classification by their sugar utilization showed them to be L. helveticus biovar jugurti.

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Crossref · 10.1271/bbb.62.1228

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  • The CEPs of L. helveticus are also able to hydrolyze κ-casein and αs2-casein, although to a lesser extent than for the other caseins.

    “The CEPs of L. helveticus are also able to hydrolyze κ-casein and αs2-casein; although to a lesser extent than for the other caseins (Ezzat et al., 1985; Yamamoto et al., 1998; Scolari et al., 2006; Jensen et al., 2009; Sadat-Mekmene et al., 2011a).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Yamamoto et al., 1998

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Authors
YAMAMOTO, N., ONO, H., MAENO, M., UEDA, Y., TAKANO, T., & MOMOSE, H.
Affiliations
  • Calpis Co., Ltd. (Japan) (JP)
  • Tokyo University of Science (JP)
Venue
Bioscience, Biotechnology, and Biochemistry
Published
1998-01
Volume
62
Issue
6
Pages
1228-1230
ISSN
  • 0916-8451 (ISSN-L)
  • 1347-6947
OpenAlex
W2074286463
Cited by
17
References
10
Citations by year
2024: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2014: 1 · 2013: 2 · 2012: 2
FWCI
0.75
Type
journal article
Language
en
Open access
closed
Locations
  • Bioscience Biotechnology and Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Lactobacillus helveticus, extracellular protease, strain classification, polyclonal antibodies, monoclonal antibodies, maltose fermentation, sugar utilization
MeSH terms
Animals, Antibody Specificity, Female, Lactobacillus, Serine Endopeptidases, Species Specificity, Immunoblotting, Mice

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