Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification and properties of the enzyme
Abstract
Whole cells of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 were able to hydrolyse alpha- and beta-caseins. Irrespective of the growth medium used, milk or De Man-Rogosa-Sharpe (MRS) broth, identical patterns of alpha- and beta-casein hydrolytic products, respectively, were visualized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. A soluble proteinase present in cell-wall extracts was active on caseins and displayed the same hydrolytic patterns as whole cells. It was purified from cell-wall extract to homogeneity by ultrafiltration and ion exchange chromatography. The enzyme is a monomer with a molecular mass of 170 kDa, an optimum temperature of 42 degrees C and an optimum pH of 5.5. It was strongly activated by dithiothreitol and partially inhibited by E-64. These properties indicate that cysteine residues play an important role in the enzyme mechanism. The purified proteinase was not able to hydrolyse di- or tripeptides.
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PrtB of L. bulgaricus strongly differs from other CSPs in its specificity of cleavage and the structure of the long C-extension domains.
“The PrtB of L. bulgaricus strongly differs from other CSPs in its specificity of cleavage and the structure of the long C-extension domains (∼1,100 residues) (13, 23).”
The carboxy end of PrtB was previously shown to be different from the consensus anchoring region of other CSPs and exhibits an imperfect duplication of 59 amino acids with a high lysine content.
“The carboxy end of PrtB was previously shown to be different from the consensus anchoring region of other CSPs and exhibits an imperfect duplication of 59 amino acids with a high lysine content.”
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Self-citation
- Authors
- Laloi, P., Atlan, D., Blanc, B., Gilbert, C., & Portalier, R.
- Affiliations
- Lyon 1 Université (FR)
- Venue
- Applied Microbiology and Biotechnology
- Published
- 1991-11
- Volume
- 36
- Issue
- 2
- Pages
- 196-204
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- OpenAlex
- W2091372839
- Cited by
- 67
- References
- 26
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 3 · 2018: 3 · 2015: 3 · 2014: 2 · 2013: 5 · 2012: 3
- FWCI
- 6.24
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Applied Microbiology and Biotechnology (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 bulgaricus, casein hydrolysis, alpha-casein, β-casein, enzyme purification, cysteine protease, E-64 inhibition, dairy fermentation
- MeSH terms
- Amino Acid Sequence, Amino Acids, Bacterial Proteins, Caseins, Cell Wall, Chromogenic Compounds, Hydrolysis, Lactobacillus, Molecular Sequence Data, Endopeptidases, Substrate Specificity
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