Modulation of the cell-surface proteinase activity of thermophilic lactobacilli by the peptide supply
Open accessAbstract
The proteolytic system of thermophilic lactobacilli is considered important for bacterial nutrition as well as for the formation of flavor and texture in fermented products. We investigated the influence of peptide content on the cell surface proteinase and intracellular aminopeptidase activities from seven thermophilic lactobacilli strains. The proteinase activities were remarkably reduced in cells grown in the peptide-rich medium MRS or in a chemically defined medium supplemented with Casitone compared with those found in a synthetic medium. The degree of inhibition observed was strain dependent. When proteinase activities were analyzed by their hydrolytic patterns of alpha- and beta-casein degradation, four types of P(III)-caseinolytic cleavage specificity were distinguished. Lactobacillus helveticus strains possessed aminopeptidase activities with broader specificity than those found in L. delbrueckii subsp. lactis strains. However, the aminopeptidase activities were not influenced by the peptide content of the medium.
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L. helveticus strains are among the most nutritionally fastidious LAB as they present multiple amino acid auxotrophies.
“L. helveticus strains are among the most nutritionally fastidious LAB as they present multiple amino acid auxothrophies (Hebert et al., 2002).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Hebert et al., 2002
The peptidase activity of the L. helveticus strains tested were not affected when grown in a peptide-rich medium.
“Conversely, the peptidase activity of the L. helveticus strains tested were not affected when grown in a peptide-rich medium.”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Hebert et al., 2002
The activity of L. helveticus CRL 1177 showed a 100-fold reduction in enzyme activity when cells were grown in MRS.
“Inparticular, the activity of L. helveticus CRL 1177 showed a 100-fold reduction in enzyme activity when cells were grown in MRS.”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Hebert et al., 2002
The proteinase activity of the LAB strains used in the study was reduced in cells grown in a peptide-rich medium, such as MRS.
“One of the few studies done on the modulation of CEPs by peptide supply (Hebert et al., 2002), concluded that the proteinase activity of the LAB strains used in this study was reduced in cells grown in a peptide-rich medium, such as MRS.”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Hebert et al., 2002
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References 20 · Cited by 27
- Authors
- Hébert, E. M., Raya, R. R., & de Giori, G. S.
- Venue
- Current Microbiology
- Published
- 2002-12-01
- Volume
- 45
- Issue
- 6
- Pages
- 385-389
- ISSN
- 0343-8651 (ISSN-L)
- 1432-0991
- OpenAlex
- W2058899563
- Cited by
- 27
- References
- 20
- Citations by year
- 2024: 1 · 2022: 1 · 2020: 2 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 3 · 2013: 3 · 2012: 2
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- cc-by-nc-sa
- www.springer.com/tdm (tdm)
- Locations
- Current Microbiology (publishedVersion)
- PubMed (publishedVersion)
- CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
- 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
- aminopeptidase, caseinolytic activity, casein degradation, Lactobacillus helveticus, Lactobacillus delbrueckii subsp. lactis, proteolytic system, fermented dairy products
- MeSH terms
- Aminopeptidases, Caseins, Culture Media, Hydrolysis, Lactobacillus, Endopeptidases, Peptides, Temperature
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