Cited by 138Protein Hydrolysis and Bioactive PeptidesProteins in Food SystemsProbiotics and Fermented Foods

Peptides identified during Emmental cheese ripening: origin and proteolytic systems involved.

Gagnaire, Valérie, Mollé,, Daniel, Herrouin, Maryse, Léonil, Joëlle·2001·Journal of Agricultural and Food Chemistry

Abstract

To determine the proteolytic changes occurring during Emmental cheese ripening, peptides released in cheese aqueous phase were analyzed by reversed-phase HPLC and identified by tandem mass spectrometry sequencing, for which different strategies were illustrated by some examples. Among the 91 peptides identified, most of them arose from alpha(s1)- (51) and beta-caseins (28), and a few arose from alpha(s2)- (9) and kappa-caseins (1). An attempt was made to correlate the released peptides with the proteolytic systems potentially involved during Emmental cheese manufacture. Besides the well-known action of plasmin on beta- and alpha(s2)-caseins, and in the absence of residual fungal coagulant from Endothia parasitica, two other proteinases seem to be involved in the hydrolysis of alpha(s1)-casein in Emmental cheese: cathepsin D originated from milk and cell-envelope proteinase from thermophilic starters. Moreover, peptidases from starters were also active throughout ripening, presumably like those from nonstarter lactic acid bacteria, in contrast to those from propionic acid bacteria.

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Crossref · 10.1021/jf000895z

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  • The N-terminal sequence of αs1-casein is proteolyzed into several peptides (including αs1-CN f24-30, αs1-CN f24-34, and αs1-CN f24-38).

    “As previously observed in other cheeses (e.g., Emmental) (Gagnaire et al., 2001), the N-terminal sequence of αs1–casein is proteolyzed into several peptides (in addition to the aforementioned ones, also αs1-CN f24–30, αs1-CN f24–34, and αs1-CN f24–38).”
  • The formation of the peptide β-CN f(1-6) can be ascribed to the action of cell-envelope proteinases from thermophilic Lactobacillus.

    “The formation of the peptide β-CN f(1–6) can be ascribed to the action of cell-envelope proteinases from thermophilic Lactobacillus (Gagnaire et al., 2001).”
  • The β-CN f 193-209 is generated by the cleavage of the peptide bond between Leu192-Tyr193, which can be hydrolyzed both by cathepsin D and cell-envelope proteinase of starter bacteria (Lactobacillus genus, mainly).

    “The β-CN f 193–209 is generated by the cleavage of the peptide bond between Leu192-Tyr193, which can be hydrolyzed both by cathepsin D and cell-envelope proteinase of starter bacteria (Lactobacillus genus, mainly) (Gagnaire et al., 2001).”

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Authors
Gagnaire, V., Mollé, Herrouin, M., & Léonil, J.
Affiliations
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR)
Corresponding author
Gagnaire, Valérie
Venue
Journal of Agricultural and Food Chemistry
Published
2001-08-25
Volume
49
Issue
9
Pages
4402-4413
ISSN
  • 0021-8561 (ISSN-L)
  • 1520-5118
OpenAlex
W1994885597
Cited by
138
References
31
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 8 · 2021: 5 · 2020: 12 · 2019: 4 · 2018: 8 · 2017: 7 · 2016: 7 · 2015: 3 · 2014: 8 · 2013: 7 · 2012: 5
FWCI
1.28
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Agricultural and Food Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Keywords
Emmental cheese, cheese ripening, peptides, proteolysis, casein, αs1-casein, β-casein, αs2-casein, kappa-casein, plasmin, Cryphonectria parasitica, cathepsin D, lactic acid bacteria, propionic acid bacteria
MeSH terms
Caseins, Cheese, Chromatography, High Pressure Liquid, Fibrinolysin, Food Handling, Peptide Hydrolases, Proteins, Mass Spectrometry, Time Factors

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