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Cited by 72Probiotics and Fermented FoodsProtein Hydrolysis and Bioactive PeptidesEnzyme Production and Characterization

Simultaneous Presence of PrtH and PrtH2 Proteinases in Lactobacillus helveticus Strains Improves Breakdown of the Pure α s1 -Casein

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Sadat-Mekmene, L., Jardin, J., Corre, C., Mollé, D., Richoux, R., Delage, M.-M., Lortal, S., Gagnaire, V.·2011·Applied and Environmental Microbiology
DOI 10.1128/aem.01466-10PMC PMC3019737
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Abstract

Lactobacillus helveticus can possess one or two cell envelope proteinases (CEPs), called PrtH2 and PrtH. The aim of this work was to explore the diversity of 15 strains of L. helveticus , isolated from various origins, in terms of their proteolytic activities and specificities on pure caseins or on milk casein micelles. CEP activity differed 14-fold when the strains were assayed on a synthetic substrate, but no significant differences were detected between strains possessing one or two CEPs. No correlation was observed between the proteolytic activities of the strains and their rates of acidification in milk. The kinetics of hydrolysis of purified α s1 - and β-casein by L. helveticus whole cells was monitored using Tris-Tricine sodium dodecyl sulfate (SDS) electrophoresis, and for four strains, the peptides released were identified using mass spectrometry. While rapid hydrolysis of pure β-casein was observed for all strains, the hydrolysis kinetics of α s1 -casein was the only criterion capable of distinguishing between the strains based on the number of CEPs. Fifty-four to 74 peptides were identified for each strain. When only PrtH2 was present, 22 to 30% of the peptides originated from α s1 -casein. The percentage increased to 41 to 49% for strains in which both CEPs were expressed. The peptide size ranged from 6 to 33 amino acids, revealing a broad range of cleavage specificities, involving all classes of amino acids (Leu, Val, Ala, Ile, Glu, Gln, Lys, Arg, Met, and Pro). Regions resistant to proteolysis were identified in both caseins. When strains were grown in milk, a drastic reduction in the number of peptides was observed, reflecting changes in accessibility and/or peptide assimilation during growth.

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Crossref · 10.1128/aem.01466-10

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  • The hydrolysis of αs1-casein by L. helveticus strains predominantly occurs at the N-terminal.

    “Two comprehensive studies have concluded that the hydrolysis of αs1-casein by L. helveticus strains predominantly occurs at the N-terminal (Jensen et al., 2009; Sadat-Mekmene et al., 2011a).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Sadat-Mekmene et al., 2011a

  • CEPs of L. helveticus are highly specific since the sites of cleavage on the caseins differ from one strain to another depending on the type of casein (α- or β-casein).

    “CEPs of L. helveticus are highly specific since the sites of cleavage on the caseins differ from one strain to another depending on the type of casein (α- or β-casein) (Zevaco and Gripon, 1988; Jensen et al., 2009; Sadat-Mekmene et al., 2011a).”

    From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Sadat-Mekmene et al., 2011a

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Authors
Sadat-Mekmene, L., Jardin, J., Corre, C., Mollé, D., Richoux, R., Delage, M.-M., Lortal, S., & Gagnaire, V.
Affiliations
  • Institut Agro Rennes-Angers (FR)
  • INRA, UMR1253, Science et Technologie du Lait et de l'Œuf, F-35042 Rennes
  • Actilait, BP 50915, F-35000 Rennes, France
ORCID
Venue
Applied and Environmental Microbiology
Publisher
American Society for Microbiology
Published
2011-01
Volume
77
Issue
1
Pages
179-186
ISSN
  • 0099-2240 (ISSN-L)
  • 1098-5336
DOI
10.1128/aem.01466-10
PMC
PMC3019737
OpenAlex
W2036422707
Cited by
72
References
47
Citations by year
2026: 1 · 2025: 1 · 2024: 6 · 2023: 3 · 2022: 8 · 2021: 5 · 2020: 2 · 2019: 7 · 2018: 7 · 2017: 4 · 2016: 5 · 2015: 4 · 2014: 6 · 2013: 6 · 2012: 3
FWCI
6.38
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Applied and Environmental Microbiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Funders
  • Institut National de la Recherche Agronomique
  • Région Bretagne
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
Lactobacillus helveticus, cell envelope proteinase, β-casein, casein micelles, proteolytic activity, protease specificity, proteolytic peptides, milk acidification, cheese ripening
MeSH terms
Bacterial Proteins, Caseins, Hydrolysis, Kinetics, Endopeptidases, Peptides, Phenotype, Mass Spectrometry, Lactobacillus helveticus

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