Comparative analysis of β-casein proteolysis by PrtP proteinase from Lactobacillus paracasei subsp. paracasei BGHN14, PrtR proteinase from Lactobacillus rhamnosus BGT10 and PrtH proteinase from Lactobacillus helveticus BGRA43
Abstract
Lactic acid bacteria contain different cell-envelope proteinases responsible for hydrolysis of caseins. Isolates of Lactobacillus paracasei subsp. paracasei BGHN14 and Lactobacillus rhamnosus BGT10 harbour PrtP and PrtR proteinases, respectively, whereas the PrtH proteinase of Lactobacillus helveticus BGRA43 is similar to that of Lb. helveticus CNRZ32. Mass spectrometry analysis of the major peptides isolated by reversed phase-high performance liquid chromatography allowed the identification of 25, 22 and 17 peptides after β-casein hydrolysis by strains BGHN14, BGRA43 and BGT10, respectively. Regardless of the type of proteinase, β-casein was hydrolyzed preferentially after hydrophobic residues and glutamines (Q). PrtP and PrtR proteinases preferentially targeted the C-terminus of β-casein. In the case of PrtH proteinase, most of the peptides obtained were cleaved from N-terminus of this casein. Nine identical peptides were identified after hydrolysis with PrtP and PrtR, three after proteolysis with PrtR and PrtH, and two after hydrolysis with all three proteinases studied.
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L. helveticus BGRA43 isolated from human feces has strong proteolytic activity and is able to hydrolyze αs1-, β-, and κ-caseins completely.
“L. helveticus BGRA43 isolated from human feces has strong proteolytic activity and is able to hydrolyze αs1-, β-, and κ-caseins completely (Lozo et al., 2011).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Lozo et al., 2011
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Reconstruction of the proteolytic pathway for use of β‐casein by <i>Lactococcus lactis</i>
Kunji, E. R. S., Fang, G., Jeronimus‐Stratingh, C. M., Bruins, A. P., Poolman, B., & Konings, W. N. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00769.x · Cited by 66 · see citing works
Genay, M., Sadat, L., Gagnaire, V., & Lortal, S. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.02395-08 · Cited by 66 · see citing works
Scolari, G., Vescovo, M., Zacconi, C., & Vescovi, F. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72421-3 · Cited by 37 · see citing works
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Lactobacillus helveticus: the proteolytic system
Griffiths, M. W., & Tellez, A. M. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00030 · Cited by 241 · see citing works
“L. helveticus BGRA43 isolated from human feces has strong proteolytic activity and is able to hydrolyze αs1-, β-, and κ-caseins completely (Lozo et al., 2011).”
BackgroundMartini, S., Conte, A., & Tagliazucchi, D. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104668 · Cited by 61 · see citing works
- Authors
- Lozo, J., Strahinic, I., Dalgalarrondo, M., Chobert, J.-M., Haertlé, T., & Topisirovic, L.
- Affiliations
- University of Belgrade (RS)
- Biopolymères Interactions Assemblages (FR)
- Corresponding author
- Lozo, Jelena
- Venue
- International Dairy Journal
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 21
- Issue
- 11
- Pages
- 863-868
- ISSN
- 0958-6946 (ISSN-L)
- OpenAlex
- W2004702278
- Cited by
- 44
- References
- 3
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 3 · 2020: 4 · 2018: 4 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 1 · 2013: 3 · 2012: 2
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Dairy Journal (publishedVersion)
- HAL (submittedVersion)
- IMAGINE - Repository of the Institute of molecular genetics and genetic engineering (University of Belgrade) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- β-casein, casein hydrolysis, lactic acid bacteria, Lacticaseibacillus paracasei subsp. paracasei, Lactobacillus rhamnosus, Lactobacillus helveticus, cell envelope proteinase, proteolytic peptides, C-terminal cleavage, N-terminal cleavage
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