Original features of cell-envelope proteinases of Lactobacillus helveticus. A review
Abstract
Lactobacillus helveticus is a lactic acid bacterium very used in fermented milks and cheese. The rapid growth of L. helveticus in milk is supported by an efficient cell envelope proteinase (CEP) activity, due to subtilisin-like serine proteases. These enzymes play also crucial roles in texture and flavor formation in dairy products as well as in generating in situ bioactive peptides. In L. helveticus, several genes encoding putative CEPs were detected and characterized by a large intraspecific diversity; little is known about regulation of expression of CEP-encoding genes. Anchored at the bacterial surface, CEPs are large-sized enzymes (> 150 kDa) hydrolyzing β- and α(s1)-casein as well. Substrate cleavages occur after almost all types of amino acids residues, but mass spectrometry analysis revealed L. helveticus strains with specific profiles of substrate hydrolysis, which could explain identification of strains associated with interesting technological properties. In this review, the most recent data regarding CEP-encoding genes, CEP activities toward caseins and L. helveticus strain diversity are discussed.
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CEPs of L. helveticus can cleave αs1- or β-casein at different sites not specifically related to one type of amino acid.
“Different studies have agreed that CEPs of L. helveticus can cleave αs1- or β-casein at different sites not specifically related to one type of amino acid (Zevaco and Gripon, 1988; Broadbent et al., 2011; Sadat-Mekmene et al., 2011b).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Sadat-Mekmene et al., 2011b
Among all the tested strains there were no differences in the extent and time of hydrolysis of β-casein in strains with one CEP or more.
“Moreover, among all the tested strains there were no differences in the extent and time of hydrolysis of β-casein in strains with one CEP or more.”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Sadat-Mekmene et al., 2011b
The proteolytic system of fifteen strains of L. helveticus more efficiently hydrolyzed β-casein than αs1-casein.
“The proteolytic system of fifteen strains of L. helveticus more efficiently hydrolyzed β-casein than αs1-casein (Sadat-Mekmene et al., 2011b).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Sadat-Mekmene et al., 2011b
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References 133 · Cited by 119
- Authors
- Sadat-Mekmene, L., Genay, M., Atlan, D., Lortal, S., & Gagnaire, V.
- Affiliations
- Institut Agro Rennes-Angers (FR)
- Laboratoire Animal et Agroécosystèmes (FR)
- Lyon 1 Université (FR)
- Corresponding author
- Gagnaire, Valérie
- Venue
- International Journal of Food Microbiology
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 146
- Issue
- 1
- Pages
- 1-13
- ISSN
- 0168-1605 (ISSN-L)
- OpenAlex
- W1966232495
- Cited by
- 119
- References
- 133
- Citations by year
- 2026: 12 · 2025: 8 · 2024: 3 · 2023: 11 · 2022: 9 · 2021: 8 · 2020: 13 · 2019: 5 · 2018: 8 · 2017: 6 · 2016: 4 · 2015: 6 · 2014: 10 · 2013: 8 · 2012: 7
- FWCI
- 1.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Journal of Food Microbiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- 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 › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Keywords
- Lactobacillus helveticus, cell envelope proteinase, subtilisin-like protease, casein hydrolysis, β-casein, substrate specificity, intraspecific genetic diversity, fermented milk, cheese, bioactive peptides, gene expression regulation
- MeSH terms
- Bacterial Proteins, Caseins, Cell Membrane, Cheese, Genes, Bacterial, Hydrolysis, Peptide Hydrolases, Substrate Specificity, Lactobacillus helveticus, Protein Interaction Domains and Motifs
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