Classification of Lactococcus lactis cell envelope proteinase based on gene sequencing, peptides formed after hydrolysis of milk, and computer modeling.
Open accessAbstract
Lactococcus lactis strains depend on a proteolytic system for growth in milk to release essential AA from casein. The cleavage specificities of the cell envelope proteinase (CEP) can vary between strains and environments and whether the enzyme is released or bound to the cell wall. Thirty-eight Lc. lactis strains were grouped according to their CEP AA sequences and according to identified peptides after hydrolysis of milk. Finally, AA positions in the substrate binding region were suggested by the use of a new CEP template based on Streptococcus C5a CEP. Aligning the CEP AA sequences of 38 strains of Lc. lactis showed that 21 strains, which were previously classified as group d, could be subdivided into 3 groups. Independently, similar subgroupings were found based on comparison of the Lc. lactis CEP AA sequences and based on normalized quantity of identified peptides released from αS1-casein and β-casein. A model structure of Lc. lactis CEP based on the crystal structure of Streptococcus C5a CEP was used to investigate the AA positions in the substrate-binding region. New AA positions were suggested, which could be relevant for the cleavage specificity of CEP; however, these could only explain 2 out of 3 found subgroups. The third subgroup could be explained by 1 to 5 AA positions located opposite the substrate binding region.
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Some PrtP enzymes (PI type) prefer β-casein and all types cleave β-casein at multiple sites with no obvious specificity.
“Some PrtP enzymes (PI type) prefer β-casein and all types cleave β- casein at multiple sites with no obvious specificity (Visser et al., 1986; Exterkate et al., 1993; Børsting et al., 2015).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Børsting et al., 2015
The Introduction (page not provided) says type PI preferentially hydrolyzes β-casein, and the Distinction Between Subgroups of Group D table lists β-casein peptides from many regions. But that section also identifies cleavage preferences, so it does not support the claim that cleavage has no obvious specificity. (LLM, conf=0.87)
Experimental — accuracy not yet measuredThe CEP enzymes are rather unspecific and able to cleave at almost any position in β-casein.
“The CEP enzymes are rather unspecific and able to cleave at almost any position in β- casein (Visser et al., 1988, 1991, 1994; Juillard et al., 1995a; Børsting et al., 2015)”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Børsting et al., 2015
The peptide table in “Correlation Between Key AA Positions in the CEP and Identified Peptides” (page unavailable) shows β-casein peptides from many regions, supporting cleavage at varied sites. It does not establish cleavage at almost any position; “Distinction Between Subgroups of Group D” (page unavailable) reports cleavage preferences and no observed cleavage when proline occupied certain positions. (LLM, conf=0.83)
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References 28 · Cited by 20
Research works printed but not linked: 1
- Fox, P. F., and P. L. H. McSweeney. 1998. Milk proteins. Pages 146- 238 in Dairy Chemistry and Biochemistry. P. F. Fox and P. L. H. McSweeney, ed. Kluwer Academic/Plenum Publishers, New York, NY.
- Authors
- Børsting, M. W., Qvist, K. B., Brockmann, E., Vindeløv, J., Pedersen, T. L., Vogensen, F. K., & Ardö, Y.
- Affiliations
- University of Copenhagen (DK)
- Chr. Hansen (Denmark) (DK)
- Corresponding author
- Børsting, M.W.
- ORCID
- Vogensen, F.K.
- Venue
- Journal of Dairy Science
- Publisher
- American Dairy Science Association
- Published
- 2015-01
- Volume
- 98
- Issue
- 1
- Pages
- 68-77
- ISSN
- 0022-0302 (ISSN-L)
- OpenAlex
- W2064268030
- Cited by
- 20
- References
- 28
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 3 · 2021: 3 · 2020: 3 · 2017: 2 · 2016: 1
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Dairy Science (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- Danish Agency for Science, Technology and Innovation
- 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
- Lactococcus lactis, cell envelope proteinase, proteolytic system, casein hydrolysis, cleavage specificity, strain classification, αs1-casein, β-casein, substrate-binding region, protein structure modeling, amino acid sequence analysis
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Caseins, Cell Membrane, Cell Wall, Computer Simulation, Hydrolysis, Milk, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Endopeptidases, Peptides, Serine Endopeptidases, Streptococcus, Lactococcus lactis, Adhesins, Bacterial
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