Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli
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2016
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Lactocepins or CEPs are large cell wall bound extracellular proteinases of lactic acid bacteria, involved in protein breakdown and utilization. They are responsible for many health-promoting traits of food products fermented with these organisms, but also essential for probiotic effects of certain strains. Different mesophilic strains selected within the species Lactobacillus zeae, Lb. casei, Lb. rhamnosus, and Lb. plantarum were analyzed for their proteolytic activity towards main fractions of milk proteins-caseins and whey proteins. The strains showing excellent proteolytic features were further examined for presence of corresponding proteinase gene(s). It was found that Lb. zeae LMG17315 possessed catalytic domains of three distinct proteinase genes, unique feature in Lb. casei group, which are similar but not identical to previously characterized prtP and prtR genes. Lb. casei neotype strain ATCC393 was also analysed and based on obtained results its reclassification in taxon Lb. z...eae is supported. In addition, we report catalytic domain of prtR-type gene in Lb. plantarum LMG9208, which is first such report in this species, and it is first time that this gene is reported outside Lb. casei group.
Ključne reči:
prtR / prtP / proteinases / Lactobacillus / caseinIzvor:
Microbiology, 2016, 85, 1, 33-41Izdavač:
- Maik Nauka/Interperiodica/Springer, New York
Finansiranje / projekti:
- Izučavanje gena i molekularnih mehanizama u osnovi probiotičke aktivnosti bakterija mlečne kiseline izolovanih sa područja zapadnog Balkana (RS-MESTD-Basic Research (BR or ON)-173019)
- Molekularna karakterizacija bakterija iz rodova Bacillus i Pseudomonas kao potencijalnih agenasa za biološku kontrolu (RS-MESTD-Basic Research (BR or ON)-173026)
DOI: 10.1134/S002626171601015X
ISSN: 0026-2617
WoS: 000370791300003
Scopus: 2-s2.0-84958818530
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Vukotić, Goran AU - Strahinić, Ivana AU - Begović, Jelena AU - Lukić, Jovanka AU - Kojić, Milan AU - Fira, Đorđe PY - 2016 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/992 AB - Lactocepins or CEPs are large cell wall bound extracellular proteinases of lactic acid bacteria, involved in protein breakdown and utilization. They are responsible for many health-promoting traits of food products fermented with these organisms, but also essential for probiotic effects of certain strains. Different mesophilic strains selected within the species Lactobacillus zeae, Lb. casei, Lb. rhamnosus, and Lb. plantarum were analyzed for their proteolytic activity towards main fractions of milk proteins-caseins and whey proteins. The strains showing excellent proteolytic features were further examined for presence of corresponding proteinase gene(s). It was found that Lb. zeae LMG17315 possessed catalytic domains of three distinct proteinase genes, unique feature in Lb. casei group, which are similar but not identical to previously characterized prtP and prtR genes. Lb. casei neotype strain ATCC393 was also analysed and based on obtained results its reclassification in taxon Lb. zeae is supported. In addition, we report catalytic domain of prtR-type gene in Lb. plantarum LMG9208, which is first such report in this species, and it is first time that this gene is reported outside Lb. casei group. PB - Maik Nauka/Interperiodica/Springer, New York T2 - Microbiology T1 - Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli EP - 41 IS - 1 SP - 33 VL - 85 DO - 10.1134/S002626171601015X ER -
@article{ author = "Vukotić, Goran and Strahinić, Ivana and Begović, Jelena and Lukić, Jovanka and Kojić, Milan and Fira, Đorđe", year = "2016", abstract = "Lactocepins or CEPs are large cell wall bound extracellular proteinases of lactic acid bacteria, involved in protein breakdown and utilization. They are responsible for many health-promoting traits of food products fermented with these organisms, but also essential for probiotic effects of certain strains. Different mesophilic strains selected within the species Lactobacillus zeae, Lb. casei, Lb. rhamnosus, and Lb. plantarum were analyzed for their proteolytic activity towards main fractions of milk proteins-caseins and whey proteins. The strains showing excellent proteolytic features were further examined for presence of corresponding proteinase gene(s). It was found that Lb. zeae LMG17315 possessed catalytic domains of three distinct proteinase genes, unique feature in Lb. casei group, which are similar but not identical to previously characterized prtP and prtR genes. Lb. casei neotype strain ATCC393 was also analysed and based on obtained results its reclassification in taxon Lb. zeae is supported. In addition, we report catalytic domain of prtR-type gene in Lb. plantarum LMG9208, which is first such report in this species, and it is first time that this gene is reported outside Lb. casei group.", publisher = "Maik Nauka/Interperiodica/Springer, New York", journal = "Microbiology", title = "Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli", pages = "41-33", number = "1", volume = "85", doi = "10.1134/S002626171601015X" }
Vukotić, G., Strahinić, I., Begović, J., Lukić, J., Kojić, M.,& Fira, Đ.. (2016). Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli. in Microbiology Maik Nauka/Interperiodica/Springer, New York., 85(1), 33-41. https://doi.org/10.1134/S002626171601015X
Vukotić G, Strahinić I, Begović J, Lukić J, Kojić M, Fira Đ. Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli. in Microbiology. 2016;85(1):33-41. doi:10.1134/S002626171601015X .
Vukotić, Goran, Strahinić, Ivana, Begović, Jelena, Lukić, Jovanka, Kojić, Milan, Fira, Đorđe, "Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli" in Microbiology, 85, no. 1 (2016):33-41, https://doi.org/10.1134/S002626171601015X . .