Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli
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1995
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Lactobacilli isolated from different natural sources were screened for the presence of cell envelope‐associated proteinases (Prt+ strains). Among them 17 of 75 tested isolates were Prt+. All Prt+ strains were producers of a serine‐type proteinase, since their proteolytic activity was inhibited by phenylmethylsulfonyl fluoride. Most of the natural isolates of mesophilic lactobacilli degraded only β‐casein such as Lactobacillus paracasei subsp. paracasei strains BGLI17 and BGLI18 and Lact. rhamnosus BGEN1. Only Lact. divergens BG742 cleaved all three, α‐, β‐ and κ‐caseins, even in the presence of Ca2+ ions. Total DNA isolated from Lact. paracasei subsp. paracasei strains BGLI17 and BGLI18 hybridized to the lactococcal proteinase gene probes originated from Lactococcus lactis subsp. cremoris Wg2. Hybridization could not be linked to the plasmid DNA, and pulse‐field gel electrophoresis analysis suggested that the proteinase genes of these two strains are most probably chromosomally located.... Copyright
Izvor:
Journal of Applied Bacteriology, 1995, 79, 1, 61-66
DOI: 10.1111/j.1365-2672.1995.tb03124.x
ISSN: 0021-8847
Scopus: 2-s2.0-0029054708
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https://imagine.imgge.bg.ac.rs/handle/123456789/89http://intor.torlakinstitut.com/handle/123456789/726
Institucija/grupa
TorlakTY - JOUR AU - Kojić, Milan AU - Fira, Đorđe AU - Bojović, B. AU - Banina, Ana AU - Topisirović, Ljubiša PY - 1995 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/89 UR - http://intor.torlakinstitut.com/handle/123456789/726 AB - Lactobacilli isolated from different natural sources were screened for the presence of cell envelope‐associated proteinases (Prt+ strains). Among them 17 of 75 tested isolates were Prt+. All Prt+ strains were producers of a serine‐type proteinase, since their proteolytic activity was inhibited by phenylmethylsulfonyl fluoride. Most of the natural isolates of mesophilic lactobacilli degraded only β‐casein such as Lactobacillus paracasei subsp. paracasei strains BGLI17 and BGLI18 and Lact. rhamnosus BGEN1. Only Lact. divergens BG742 cleaved all three, α‐, β‐ and κ‐caseins, even in the presence of Ca2+ ions. Total DNA isolated from Lact. paracasei subsp. paracasei strains BGLI17 and BGLI18 hybridized to the lactococcal proteinase gene probes originated from Lactococcus lactis subsp. cremoris Wg2. Hybridization could not be linked to the plasmid DNA, and pulse‐field gel electrophoresis analysis suggested that the proteinase genes of these two strains are most probably chromosomally located. Copyright T2 - Journal of Applied Bacteriology T1 - Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli EP - 66 IS - 1 SP - 61 VL - 79 DO - 10.1111/j.1365-2672.1995.tb03124.x ER -
@article{ author = "Kojić, Milan and Fira, Đorđe and Bojović, B. and Banina, Ana and Topisirović, Ljubiša", year = "1995", abstract = "Lactobacilli isolated from different natural sources were screened for the presence of cell envelope‐associated proteinases (Prt+ strains). Among them 17 of 75 tested isolates were Prt+. All Prt+ strains were producers of a serine‐type proteinase, since their proteolytic activity was inhibited by phenylmethylsulfonyl fluoride. Most of the natural isolates of mesophilic lactobacilli degraded only β‐casein such as Lactobacillus paracasei subsp. paracasei strains BGLI17 and BGLI18 and Lact. rhamnosus BGEN1. Only Lact. divergens BG742 cleaved all three, α‐, β‐ and κ‐caseins, even in the presence of Ca2+ ions. Total DNA isolated from Lact. paracasei subsp. paracasei strains BGLI17 and BGLI18 hybridized to the lactococcal proteinase gene probes originated from Lactococcus lactis subsp. cremoris Wg2. Hybridization could not be linked to the plasmid DNA, and pulse‐field gel electrophoresis analysis suggested that the proteinase genes of these two strains are most probably chromosomally located. Copyright", journal = "Journal of Applied Bacteriology", title = "Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli", pages = "66-61", number = "1", volume = "79", doi = "10.1111/j.1365-2672.1995.tb03124.x" }
Kojić, M., Fira, Đ., Bojović, B., Banina, A.,& Topisirović, L.. (1995). Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli. in Journal of Applied Bacteriology, 79(1), 61-66. https://doi.org/10.1111/j.1365-2672.1995.tb03124.x
Kojić M, Fira Đ, Bojović B, Banina A, Topisirović L. Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli. in Journal of Applied Bacteriology. 1995;79(1):61-66. doi:10.1111/j.1365-2672.1995.tb03124.x .
Kojić, Milan, Fira, Đorđe, Bojović, B., Banina, Ana, Topisirović, Ljubiša, "Comparative study on cell envelope‐associated proteinases in natural isolates of mesophilic lactobacilli" in Journal of Applied Bacteriology, 79, no. 1 (1995):61-66, https://doi.org/10.1111/j.1365-2672.1995.tb03124.x . .