TY  - JOUR
AU  - Vukotić, Goran
AU  - Obradović, Mina
AU  - Novović, Katarina
AU  - Di Luca, Mariagrazia
AU  - Jovčić, Branko
AU  - Fira, Đorđe
AU  - Neve, Horst
AU  - Kojić, Milan
AU  - McAuliffe, Olivia
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1355
AB  - Acinetobacter baumanniiis a leading cause of healthcare-associated infections worldwide. Its various intrinsic and acquired mechanisms of antibiotic resistance make the therapeutic challenge even more serious. One of the promising alternative treatments that is increasingly highlighted is phage therapy, the therapeutic use of bacteriophages to treat bacterial infections. Two phages active against nosocomial carbapenem-resistantA. baumanniistrain 6077/12, vB_AbaM_ISTD, and vB_AbaM_NOVI, were isolated from Belgrade wastewaters, purified, and concentrated using CsCl gradient ultracentrifugation. The phages were screened against 103 clinical isolates ofA. baumanniifrom a laboratory collection and characterized based on plaque and virion morphology, host range, adsorption rate, and one-step growth curve. Given that phage ISTD showed a broader host range, better adsorption rate, shorter latent period, and larger burst size, its ability to lyse planktonic and biofilm-embedded cells was tested in detail. Phage ISTD yielded a 3.5- and 2-log reduction in planktonic and biofilm-associated viable bacterial cell count, respectively, but the effect was time-dependent. Both phages produced growing turbid halos around plaques indicating the synthesis of depolymerases, enzymes capable of degrading bacterial exopolysaccharides. Halos tested positive for presence of phages in the proximity of the plaque, but not further from the plaque, which indicates that the observed halo enlargement is a consequence of enzyme diffusion through the agar, independently of the phages. This notion was also supported by the growing halos induced by phage preparations applied on pregrown bacterial lawns, indicating that depolymerizing effect was achieved also on non-dividing sensitive cells. Overall, good rates of growth, fast adsorption rate, broad host range, and high depolymerizing activity, as well as antibacterial effectiveness against planktonic and biofilm-associated bacteria, make these phages good candidates for potential application in combatingA. baumanniiinfections.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Medicine
T1  - Characterization, Antibiofilm, and Depolymerizing Activity of Two Phages Active on Carbapenem-ResistantAcinetobacter baumannii
VL  - 7
DO  - 10.3389/fmed.2020.00426
ER  - 

@article{
author = "Vukotić, Goran and Obradović, Mina and Novović, Katarina and Di Luca, Mariagrazia and Jovčić, Branko and Fira, Đorđe and Neve, Horst and Kojić, Milan and McAuliffe, Olivia",
year = "2020",
abstract = "Acinetobacter baumanniiis a leading cause of healthcare-associated infections worldwide. Its various intrinsic and acquired mechanisms of antibiotic resistance make the therapeutic challenge even more serious. One of the promising alternative treatments that is increasingly highlighted is phage therapy, the therapeutic use of bacteriophages to treat bacterial infections. Two phages active against nosocomial carbapenem-resistantA. baumanniistrain 6077/12, vB_AbaM_ISTD, and vB_AbaM_NOVI, were isolated from Belgrade wastewaters, purified, and concentrated using CsCl gradient ultracentrifugation. The phages were screened against 103 clinical isolates ofA. baumanniifrom a laboratory collection and characterized based on plaque and virion morphology, host range, adsorption rate, and one-step growth curve. Given that phage ISTD showed a broader host range, better adsorption rate, shorter latent period, and larger burst size, its ability to lyse planktonic and biofilm-embedded cells was tested in detail. Phage ISTD yielded a 3.5- and 2-log reduction in planktonic and biofilm-associated viable bacterial cell count, respectively, but the effect was time-dependent. Both phages produced growing turbid halos around plaques indicating the synthesis of depolymerases, enzymes capable of degrading bacterial exopolysaccharides. Halos tested positive for presence of phages in the proximity of the plaque, but not further from the plaque, which indicates that the observed halo enlargement is a consequence of enzyme diffusion through the agar, independently of the phages. This notion was also supported by the growing halos induced by phage preparations applied on pregrown bacterial lawns, indicating that depolymerizing effect was achieved also on non-dividing sensitive cells. Overall, good rates of growth, fast adsorption rate, broad host range, and high depolymerizing activity, as well as antibacterial effectiveness against planktonic and biofilm-associated bacteria, make these phages good candidates for potential application in combatingA. baumanniiinfections.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Medicine",
title = "Characterization, Antibiofilm, and Depolymerizing Activity of Two Phages Active on Carbapenem-ResistantAcinetobacter baumannii",
volume = "7",
doi = "10.3389/fmed.2020.00426"
}

Vukotić, G., Obradović, M., Novović, K., Di Luca, M., Jovčić, B., Fira, Đ., Neve, H., Kojić, M.,& McAuliffe, O.. (2020). Characterization, Antibiofilm, and Depolymerizing Activity of Two Phages Active on Carbapenem-ResistantAcinetobacter baumannii. in Frontiers in Medicine
Frontiers Media Sa, Lausanne., 7.
https://doi.org/10.3389/fmed.2020.00426

Vukotić G, Obradović M, Novović K, Di Luca M, Jovčić B, Fira Đ, Neve H, Kojić M, McAuliffe O. Characterization, Antibiofilm, and Depolymerizing Activity of Two Phages Active on Carbapenem-ResistantAcinetobacter baumannii. in Frontiers in Medicine. 2020;7.
doi:10.3389/fmed.2020.00426 .

Vukotić, Goran, Obradović, Mina, Novović, Katarina, Di Luca, Mariagrazia, Jovčić, Branko, Fira, Đorđe, Neve, Horst, Kojić, Milan, McAuliffe, Olivia, "Characterization, Antibiofilm, and Depolymerizing Activity of Two Phages Active on Carbapenem-ResistantAcinetobacter baumannii" in Frontiers in Medicine, 7 (2020),
https://doi.org/10.3389/fmed.2020.00426 . .

TY  - JOUR
AU  - Terzić-Vidojević, Amarela
AU  - Veljović, Katarina
AU  - Tolinački, Maja
AU  - Živković, Milica
AU  - Lukić, Jovanka
AU  - Lozo, Jelena
AU  - Fira, Đorđe
AU  - Jovčić, Branko
AU  - Strahinić, Ivana
AU  - Begović, Jelena
AU  - Popović, Nikola
AU  - Miljković, Marija
AU  - Kojić, Milan
AU  - Topisirović, Ljubiša
AU  - Golić, Nataša
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1353
AB  - The aim of this review was to summarize the data regarding diversity of non-starter lactic acid bacteria (NSLAB) isolated from various artisanal dairy products manufactured in Western Balkan Countries. The dairy products examined were manufactured from raw cow's, sheep's or goat's milk or mixed milk, in the traditional way without the addition of commercial starter cultures. Dairy products such as white brined cheese, fresh cheese, hard cheese, yogurt, sour cream and kajmak were sampled in the households of Serbia, Croatia, Slovenia, Bosnia and Herzegovina, Montenegro, and North Macedonia. It has been established that the diversity of lactic acid bacteria (LAB) from raw milk artisanal dairy products is extensive. In the reviewed literature, 28 LAB species and a large number of strains belonging to the Lactobacillus, Lactococcus, Enterococcus, Streptococcus, Pediococcus, Leuconostoc and Weissella genera were isolated from various dairy products. Over 3000 LAB strains were obtained and characterized for their technological and probiotic properties including: acidification and coagulation of milk, production of aromatic compounds, proteolytic activity, bacteriocins production and competitive exclusion of pathogens, production of exopolysaccharides, aggregation ability and immunomodulatory effect. Results show that many of the isolated NSLAB strains had one, two or more of the properties mentioned. The data presented emphasize the importance of artisanal products as a valuable source of NSLAB with unique technological and probiotic features important both as a base for scientific research as well as for designing novel starter cultures for functional dairy food.
PB  - Elsevier, Amsterdam
T2  - Food Research International
T1  - Diversity of non-starter lactic acid bacteria in autochthonous dairy products from Western Balkan Countries - Technological and probiotic properties
VL  - 136
DO  - 10.1016/j.foodres.2020.109494
ER  - 

@article{
author = "Terzić-Vidojević, Amarela and Veljović, Katarina and Tolinački, Maja and Živković, Milica and Lukić, Jovanka and Lozo, Jelena and Fira, Đorđe and Jovčić, Branko and Strahinić, Ivana and Begović, Jelena and Popović, Nikola and Miljković, Marija and Kojić, Milan and Topisirović, Ljubiša and Golić, Nataša",
year = "2020",
abstract = "The aim of this review was to summarize the data regarding diversity of non-starter lactic acid bacteria (NSLAB) isolated from various artisanal dairy products manufactured in Western Balkan Countries. The dairy products examined were manufactured from raw cow's, sheep's or goat's milk or mixed milk, in the traditional way without the addition of commercial starter cultures. Dairy products such as white brined cheese, fresh cheese, hard cheese, yogurt, sour cream and kajmak were sampled in the households of Serbia, Croatia, Slovenia, Bosnia and Herzegovina, Montenegro, and North Macedonia. It has been established that the diversity of lactic acid bacteria (LAB) from raw milk artisanal dairy products is extensive. In the reviewed literature, 28 LAB species and a large number of strains belonging to the Lactobacillus, Lactococcus, Enterococcus, Streptococcus, Pediococcus, Leuconostoc and Weissella genera were isolated from various dairy products. Over 3000 LAB strains were obtained and characterized for their technological and probiotic properties including: acidification and coagulation of milk, production of aromatic compounds, proteolytic activity, bacteriocins production and competitive exclusion of pathogens, production of exopolysaccharides, aggregation ability and immunomodulatory effect. Results show that many of the isolated NSLAB strains had one, two or more of the properties mentioned. The data presented emphasize the importance of artisanal products as a valuable source of NSLAB with unique technological and probiotic features important both as a base for scientific research as well as for designing novel starter cultures for functional dairy food.",
publisher = "Elsevier, Amsterdam",
journal = "Food Research International",
title = "Diversity of non-starter lactic acid bacteria in autochthonous dairy products from Western Balkan Countries - Technological and probiotic properties",
volume = "136",
doi = "10.1016/j.foodres.2020.109494"
}

Terzić-Vidojević, A., Veljović, K., Tolinački, M., Živković, M., Lukić, J., Lozo, J., Fira, Đ., Jovčić, B., Strahinić, I., Begović, J., Popović, N., Miljković, M., Kojić, M., Topisirović, L.,& Golić, N.. (2020). Diversity of non-starter lactic acid bacteria in autochthonous dairy products from Western Balkan Countries - Technological and probiotic properties. in Food Research International
Elsevier, Amsterdam., 136.
https://doi.org/10.1016/j.foodres.2020.109494

Terzić-Vidojević A, Veljović K, Tolinački M, Živković M, Lukić J, Lozo J, Fira Đ, Jovčić B, Strahinić I, Begović J, Popović N, Miljković M, Kojić M, Topisirović L, Golić N. Diversity of non-starter lactic acid bacteria in autochthonous dairy products from Western Balkan Countries - Technological and probiotic properties. in Food Research International. 2020;136.
doi:10.1016/j.foodres.2020.109494 .

Terzić-Vidojević, Amarela, Veljović, Katarina, Tolinački, Maja, Živković, Milica, Lukić, Jovanka, Lozo, Jelena, Fira, Đorđe, Jovčić, Branko, Strahinić, Ivana, Begović, Jelena, Popović, Nikola, Miljković, Marija, Kojić, Milan, Topisirović, Ljubiša, Golić, Nataša, "Diversity of non-starter lactic acid bacteria in autochthonous dairy products from Western Balkan Countries - Technological and probiotic properties" in Food Research International, 136 (2020),
https://doi.org/10.1016/j.foodres.2020.109494 . .

TY  - JOUR
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja
AU  - Fira, Đorđe
AU  - Kojić, Milan
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1251
AB  - In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501
VL  - 10
DO  - 10.3389/fmicb.2019.00874
ER  - 

@article{
author = "Vukotić, Goran and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja and Fira, Đorđe and Kojić, Milan",
year = "2019",
abstract = "In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501",
volume = "10",
doi = "10.3389/fmicb.2019.00874"
}

Vukotić, G., Polović, N., Mirković, N., Jovčić, B., Stanisavljević, N., Fira, Đ.,& Kojić, M.. (2019). Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 10.
https://doi.org/10.3389/fmicb.2019.00874

Vukotić G, Polović N, Mirković N, Jovčić B, Stanisavljević N, Fira Đ, Kojić M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501. in Frontiers in Microbiology. 2019;10.
doi:10.3389/fmicb.2019.00874 .

Vukotić, Goran, Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja, Fira, Đorđe, Kojić, Milan, "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501" in Frontiers in Microbiology, 10 (2019),
https://doi.org/10.3389/fmicb.2019.00874 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Jovanović, Sofija
AU  - O'Connor, Paula M.
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Filipić, Brankica
AU  - Dinić, Miroslav
AU  - Studholme, David John
AU  - Fira, Đorđe
AU  - Cotter, Paul D.
AU  - Kojić, Milan
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1264
AB  - Bacteria active against multi-drug resistant pathogens, isolated by direct selection of colonies from clover silage samples, produce zones of inhibition against two Gram-negative (Klebsiella pneumoniae Ni9 and Pseudomonas aeruginosa MMA83) and two Gram-positive (Staphylococcus aureus ATCC25923 and Listeria monocytogenes ATCC19111) pathogens. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 produced the largest zones of inhibition against all four pathogens when grown in LB broth with aeration at 37 degrees C. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 were identified as Brevibacillus laterosporus and pulsed field gel electrophoresis and extracellular protein profiles showed that three different strains (BGSP7, BGSP9 and BGSP11) were isolated. A semi-native SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) gel overlay assay showed that BGSP7 and BGSP9 produce small antimicrobial molecules of about 1.5 kDa, while BGSP11 produces antimicrobial molecules of 1.5 and 6 kDa active against S. aureus ATCC25923. Amino acid analysis of two antimicrobial molecules (1583.73 Da; from BGSP7 and 1556.31 Da; from BGSP11) revealed that they have a similar composition and differ only by virtue of the presence of a methionine which is present only in BGSP11 molecule. Genome sequencing of the three isolates revealed the presence of gene clusters associated with the production of non-ribosomally synthesized peptides (brevibacillin, bogorol, gramicidin S, plipastatin and tyrocin) and bacteriocins (laterosporulin, a lactococcin 972-like bacteriocin, as well as putative linocin M18, sactipeptide, UviB and lantipeptide-like molecules). Ultimately, the purification of a number of antimicrobial molecules from each isolate suggests that they can be considered as potent biocontrol strains that produce an arsenal of antimicrobial molecules active against Gram-positive and Gram-negative multi-resistant pathogens, fungi and insects.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials
IS  - 5
VL  - 14
DO  - 10.1371/journal.pone.0216773
ER  - 

@article{
author = "Miljković, Marija and Jovanović, Sofija and O'Connor, Paula M. and Mirković, Nemanja and Jovčić, Branko and Filipić, Brankica and Dinić, Miroslav and Studholme, David John and Fira, Đorđe and Cotter, Paul D. and Kojić, Milan",
year = "2019",
abstract = "Bacteria active against multi-drug resistant pathogens, isolated by direct selection of colonies from clover silage samples, produce zones of inhibition against two Gram-negative (Klebsiella pneumoniae Ni9 and Pseudomonas aeruginosa MMA83) and two Gram-positive (Staphylococcus aureus ATCC25923 and Listeria monocytogenes ATCC19111) pathogens. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 produced the largest zones of inhibition against all four pathogens when grown in LB broth with aeration at 37 degrees C. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 were identified as Brevibacillus laterosporus and pulsed field gel electrophoresis and extracellular protein profiles showed that three different strains (BGSP7, BGSP9 and BGSP11) were isolated. A semi-native SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) gel overlay assay showed that BGSP7 and BGSP9 produce small antimicrobial molecules of about 1.5 kDa, while BGSP11 produces antimicrobial molecules of 1.5 and 6 kDa active against S. aureus ATCC25923. Amino acid analysis of two antimicrobial molecules (1583.73 Da; from BGSP7 and 1556.31 Da; from BGSP11) revealed that they have a similar composition and differ only by virtue of the presence of a methionine which is present only in BGSP11 molecule. Genome sequencing of the three isolates revealed the presence of gene clusters associated with the production of non-ribosomally synthesized peptides (brevibacillin, bogorol, gramicidin S, plipastatin and tyrocin) and bacteriocins (laterosporulin, a lactococcin 972-like bacteriocin, as well as putative linocin M18, sactipeptide, UviB and lantipeptide-like molecules). Ultimately, the purification of a number of antimicrobial molecules from each isolate suggests that they can be considered as potent biocontrol strains that produce an arsenal of antimicrobial molecules active against Gram-positive and Gram-negative multi-resistant pathogens, fungi and insects.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials",
number = "5",
volume = "14",
doi = "10.1371/journal.pone.0216773"
}

Miljković, M., Jovanović, S., O'Connor, P. M., Mirković, N., Jovčić, B., Filipić, B., Dinić, M., Studholme, D. J., Fira, Đ., Cotter, P. D.,& Kojić, M.. (2019). Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials. in PLoS One
Public Library Science, San Francisco., 14(5).
https://doi.org/10.1371/journal.pone.0216773

Miljković M, Jovanović S, O'Connor PM, Mirković N, Jovčić B, Filipić B, Dinić M, Studholme DJ, Fira Đ, Cotter PD, Kojić M. Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials. in PLoS One. 2019;14(5).
doi:10.1371/journal.pone.0216773 .

Miljković, Marija, Jovanović, Sofija, O'Connor, Paula M., Mirković, Nemanja, Jovčić, Branko, Filipić, Brankica, Dinić, Miroslav, Studholme, David John, Fira, Đorđe, Cotter, Paul D., Kojić, Milan, "Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials" in PLoS One, 14, no. 5 (2019),
https://doi.org/10.1371/journal.pone.0216773 . .

TY  - 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 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Bertani, Iris
AU  - Fira, Đorđe
AU  - Jovčić, Branko
AU  - Novović, Katarina
AU  - Venturi, Vittorio
AU  - Kojić, Milan
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/924
AB  - AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation
EP  - 14
SP  - 1
VL  - 7
DO  - 10.3389/fmicb.2016.01422
ER  - 

@article{
author = "Miljković, Marija and Bertani, Iris and Fira, Đorđe and Jovčić, Branko and Novović, Katarina and Venturi, Vittorio and Kojić, Milan",
year = "2016",
abstract = "AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation",
pages = "14-1",
volume = "7",
doi = "10.3389/fmicb.2016.01422"
}

Miljković, M., Bertani, I., Fira, Đ., Jovčić, B., Novović, K., Venturi, V.,& Kojić, M.. (2016). Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 7, 1-14.
https://doi.org/10.3389/fmicb.2016.01422

Miljković M, Bertani I, Fira Đ, Jovčić B, Novović K, Venturi V, Kojić M. Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology. 2016;7:1-14.
doi:10.3389/fmicb.2016.01422 .

Miljković, Marija, Bertani, Iris, Fira, Đorđe, Jovčić, Branko, Novović, Katarina, Venturi, Vittorio, Kojić, Milan, "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation" in Frontiers in Microbiology, 7 (2016):1-14,
https://doi.org/10.3389/fmicb.2016.01422 . .

TY  - JOUR
AU  - Stanisavljević, Nemanja
AU  - Vukotić, Goran 
AU  - Pastor, Ferenc T.
AU  - Suznjević, Desanka
AU  - Jovanović, Živko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Radović, Svetlana S.
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/845
AB  - Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria
EP  - 1042
IS  - 3
SP  - 1033
VL  - 67
DO  - 10.2298/ABS150130066S
ER  - 

@article{
author = "Stanisavljević, Nemanja and Vukotić, Goran  and Pastor, Ferenc T. and Suznjević, Desanka and Jovanović, Živko and Strahinić, Ivana and Fira, Đorđe and Radović, Svetlana S.",
year = "2015",
abstract = "Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria",
pages = "1042-1033",
number = "3",
volume = "67",
doi = "10.2298/ABS150130066S"
}

Stanisavljević, N., Vukotić, G., Pastor, F. T., Suznjević, D., Jovanović, Ž., Strahinić, I., Fira, Đ.,& Radović, S. S.. (2015). Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 67(3), 1033-1042.
https://doi.org/10.2298/ABS150130066S

Stanisavljević N, Vukotić G, Pastor FT, Suznjević D, Jovanović Ž, Strahinić I, Fira Đ, Radović SS. Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria. in Archives of Biological Sciences. 2015;67(3):1033-1042.
doi:10.2298/ABS150130066S .

Stanisavljević, Nemanja, Vukotić, Goran , Pastor, Ferenc T., Suznjević, Desanka, Jovanović, Živko, Strahinić, Ivana, Fira, Đorđe, Radović, Svetlana S., "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria" in Archives of Biological Sciences, 67, no. 3 (2015):1033-1042,
https://doi.org/10.2298/ABS150130066S . .

TY  - JOUR
AU  - Vukotić, Goran
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Miljković, Marija
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Radulović, Zorica
AU  - Kojić, Milan
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/895
AB  - Proteinases and bacteriocins are of great importance to the dairy industry, but their interactions have not been studied so far. Lactococcus lactis subsp. lactis BGMN1-5 is a natural isolate from homemade semi-hard cheese which produces two bacteriocins (Lactococcin B and LsbB), as well as proteinase PrtP. A medium-dependent increase in the bacteriocin LcnB activity of L. lactis BGMN1-501, a derivate of L. lactis subsp. lactis BGMN1-5, was shown to be accompanied by a decrease in its promoter activity. A similar effect of media components on gene expression was reported for proteinase PrtP whose gene is co-localized on the same plasmid as the IcnB gene. Thus, the PrtP-LcnB interplay was investigated. Single gene knockout mutants were constructed with disrupted prtP or IcnB genes. PrtP mutants showed higher bacteriocin activity that had lost its growth medium dependence, which was in contrast to the original strain. When LcnB from this mutant was combined with proteinase from the LonB(-) mutant in vitro, its activity was rendered to the original level, suggesting that proteinase reduces bacteriocin activity. We propose a new model of medium dependent expression of these genes with regard to the effects of their interaction in vivo.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation
VL  - 6
DO  - 10.3389/fmicb.2015.00092
ER  - 

@article{
author = "Vukotić, Goran and Mirković, Nemanja and Jovčić, Branko and Miljković, Marija and Strahinić, Ivana and Fira, Đorđe and Radulović, Zorica and Kojić, Milan",
year = "2015",
abstract = "Proteinases and bacteriocins are of great importance to the dairy industry, but their interactions have not been studied so far. Lactococcus lactis subsp. lactis BGMN1-5 is a natural isolate from homemade semi-hard cheese which produces two bacteriocins (Lactococcin B and LsbB), as well as proteinase PrtP. A medium-dependent increase in the bacteriocin LcnB activity of L. lactis BGMN1-501, a derivate of L. lactis subsp. lactis BGMN1-5, was shown to be accompanied by a decrease in its promoter activity. A similar effect of media components on gene expression was reported for proteinase PrtP whose gene is co-localized on the same plasmid as the IcnB gene. Thus, the PrtP-LcnB interplay was investigated. Single gene knockout mutants were constructed with disrupted prtP or IcnB genes. PrtP mutants showed higher bacteriocin activity that had lost its growth medium dependence, which was in contrast to the original strain. When LcnB from this mutant was combined with proteinase from the LonB(-) mutant in vitro, its activity was rendered to the original level, suggesting that proteinase reduces bacteriocin activity. We propose a new model of medium dependent expression of these genes with regard to the effects of their interaction in vivo.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation",
volume = "6",
doi = "10.3389/fmicb.2015.00092"
}

Vukotić, G., Mirković, N., Jovčić, B., Miljković, M., Strahinić, I., Fira, Đ., Radulović, Z.,& Kojić, M.. (2015). Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 6.
https://doi.org/10.3389/fmicb.2015.00092

Vukotić G, Mirković N, Jovčić B, Miljković M, Strahinić I, Fira Đ, Radulović Z, Kojić M. Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation. in Frontiers in Microbiology. 2015;6.
doi:10.3389/fmicb.2015.00092 .

Vukotić, Goran, Mirković, Nemanja, Jovčić, Branko, Miljković, Marija, Strahinić, Ivana, Fira, Đorđe, Radulović, Zorica, Kojić, Milan, "Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation" in Frontiers in Microbiology, 6 (2015),
https://doi.org/10.3389/fmicb.2015.00092 . .

TY  - JOUR
AU  - Ivanović, Zarko
AU  - Popović, Tatjana
AU  - Janse, Jaap
AU  - Kojić, Milan
AU  - Stanković, Slaviša
AU  - Gavrilović, Veljko
AU  - Fira, Đorđe
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/854
AB  - The purpose of the present study was to investigate the genetic diversity of X. arboricola pv. juglandis strains in Serbia. This bacterium is the causal agent of walnut blight and is also associated with apical necrosis of immature walnut fruits. Although walnut blight is long known and widespread in Serbia, a systematic strain diversity study of Xanthomonas arboricola pv. juglandis strains from different regions in Serbia has not been performed. The objectives of this work were to examine the molecular diversity and its possible biological significance of 59 isolates of X. arboricola pv. juglandis collected from different geographic locations in Serbia. Genomic variability was assessed by using repetitive PCR, SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and partial sequencing of the gyrB gene. Molecular analyses showed substantial genetic diversity among strains and existence of diverse populations of X. arboricola pv. juglandis in Serbia.
PB  - Springer, Dordrecht
T2  - European Journal of Plant Pathology
T1  - Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques
EP  - 145
IS  - 1
SP  - 133
VL  - 141
DO  - 10.1007/s10658-014-0531-5
ER  - 

@article{
author = "Ivanović, Zarko and Popović, Tatjana and Janse, Jaap and Kojić, Milan and Stanković, Slaviša and Gavrilović, Veljko and Fira, Đorđe",
year = "2015",
abstract = "The purpose of the present study was to investigate the genetic diversity of X. arboricola pv. juglandis strains in Serbia. This bacterium is the causal agent of walnut blight and is also associated with apical necrosis of immature walnut fruits. Although walnut blight is long known and widespread in Serbia, a systematic strain diversity study of Xanthomonas arboricola pv. juglandis strains from different regions in Serbia has not been performed. The objectives of this work were to examine the molecular diversity and its possible biological significance of 59 isolates of X. arboricola pv. juglandis collected from different geographic locations in Serbia. Genomic variability was assessed by using repetitive PCR, SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and partial sequencing of the gyrB gene. Molecular analyses showed substantial genetic diversity among strains and existence of diverse populations of X. arboricola pv. juglandis in Serbia.",
publisher = "Springer, Dordrecht",
journal = "European Journal of Plant Pathology",
title = "Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques",
pages = "145-133",
number = "1",
volume = "141",
doi = "10.1007/s10658-014-0531-5"
}

Ivanović, Z., Popović, T., Janse, J., Kojić, M., Stanković, S., Gavrilović, V.,& Fira, Đ.. (2015). Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques. in European Journal of Plant Pathology
Springer, Dordrecht., 141(1), 133-145.
https://doi.org/10.1007/s10658-014-0531-5

Ivanović Z, Popović T, Janse J, Kojić M, Stanković S, Gavrilović V, Fira Đ. Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques. in European Journal of Plant Pathology. 2015;141(1):133-145.
doi:10.1007/s10658-014-0531-5 .

Ivanović, Zarko, Popović, Tatjana, Janse, Jaap, Kojić, Milan, Stanković, Slaviša, Gavrilović, Veljko, Fira, Đorđe, "Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques" in European Journal of Plant Pathology, 141, no. 1 (2015):133-145,
https://doi.org/10.1007/s10658-014-0531-5 . .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Berić, Tanja
AU  - Terzić-Vidojević, Amarela
AU  - Stanković, Slaviša
AU  - Fira, Đorđe
AU  - Stanisavljević, L.
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/817
AB  - Using cultivation-dependant method, we isolated 184 strains from fresh and old bee bread, pollen, larvae and adults of solitary bee Osmia cornuta. The 16S rDNA sequencing of 79 selected isolates gave the final species-specific identification of strains. Phylogenetic analysis indicated that microbiota isolated from five different sources were represented with 29 species within three different phyla, Firmicutes with 25 species, Actinobacteria with only one species and Proteobacteria with three species of Enterobacteriaceae. Bacterial biodiversity presented with Shannon-Wiener index (H') was highest in the alimentary tract of adults and old bee bread (H' = 2.43 and H' = 2.53, respectively) and in the same time no dominance of any species was scored. On the contrary, results obtained for Simpson index (D) showed that in pollen samples the dominant species was Pantoea agglomerans (D = 0.42) while in fresh bee bread that was Staphylococcus sp. (D = 0.27). We assume that microbial diversity detected in the tested samples of solitary bee O. cornuta probably come from environment.
PB  - Cambridge Univ Press, Cambridge
T2  - Bulletin of Entomological Research
T1  - Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)
EP  - 476
IS  - 4
SP  - 470
VL  - 105
DO  - 10.1017/S0007485315000292
ER  - 

@article{
author = "Lozo, Jelena and Berić, Tanja and Terzić-Vidojević, Amarela and Stanković, Slaviša and Fira, Đorđe and Stanisavljević, L.",
year = "2015",
abstract = "Using cultivation-dependant method, we isolated 184 strains from fresh and old bee bread, pollen, larvae and adults of solitary bee Osmia cornuta. The 16S rDNA sequencing of 79 selected isolates gave the final species-specific identification of strains. Phylogenetic analysis indicated that microbiota isolated from five different sources were represented with 29 species within three different phyla, Firmicutes with 25 species, Actinobacteria with only one species and Proteobacteria with three species of Enterobacteriaceae. Bacterial biodiversity presented with Shannon-Wiener index (H') was highest in the alimentary tract of adults and old bee bread (H' = 2.43 and H' = 2.53, respectively) and in the same time no dominance of any species was scored. On the contrary, results obtained for Simpson index (D) showed that in pollen samples the dominant species was Pantoea agglomerans (D = 0.42) while in fresh bee bread that was Staphylococcus sp. (D = 0.27). We assume that microbial diversity detected in the tested samples of solitary bee O. cornuta probably come from environment.",
publisher = "Cambridge Univ Press, Cambridge",
journal = "Bulletin of Entomological Research",
title = "Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)",
pages = "476-470",
number = "4",
volume = "105",
doi = "10.1017/S0007485315000292"
}

Lozo, J., Berić, T., Terzić-Vidojević, A., Stanković, S., Fira, Đ.,& Stanisavljević, L.. (2015). Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae). in Bulletin of Entomological Research
Cambridge Univ Press, Cambridge., 105(4), 470-476.
https://doi.org/10.1017/S0007485315000292

Lozo J, Berić T, Terzić-Vidojević A, Stanković S, Fira Đ, Stanisavljević L. Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae). in Bulletin of Entomological Research. 2015;105(4):470-476.
doi:10.1017/S0007485315000292 .

Lozo, Jelena, Berić, Tanja, Terzić-Vidojević, Amarela, Stanković, Slaviša, Fira, Đorđe, Stanisavljević, L., "Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)" in Bulletin of Entomological Research, 105, no. 4 (2015):470-476,
https://doi.org/10.1017/S0007485315000292 . .

TY  - JOUR
AU  - Berić, Tanja
AU  - Stanković, Slaviša
AU  - Draganić, V.
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Fira, Đorđe
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/792
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample
EP  - 510
IS  - 3
SP  - 502
VL  - 116
DO  - 10.1111/jam.12393
ER  - 

@article{
author = "Berić, Tanja and Stanković, Slaviša and Draganić, V. and Kojić, Milan and Lozo, Jelena and Fira, Đorđe",
year = "2014",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample",
pages = "510-502",
number = "3",
volume = "116",
doi = "10.1111/jam.12393"
}

Berić, T., Stanković, S., Draganić, V., Kojić, M., Lozo, J.,& Fira, Đ.. (2014). Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample. in Journal of Applied Microbiology
Wiley, Hoboken., 116(3), 502-510.
https://doi.org/10.1111/jam.12393

Berić T, Stanković S, Draganić V, Kojić M, Lozo J, Fira Đ. Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample. in Journal of Applied Microbiology. 2014;116(3):502-510.
doi:10.1111/jam.12393 .

Berić, Tanja, Stanković, Slaviša, Draganić, V., Kojić, Milan, Lozo, Jelena, Fira, Đorđe, "Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample" in Journal of Applied Microbiology, 116, no. 3 (2014):502-510,
https://doi.org/10.1111/jam.12393 . .

TY  - JOUR
AU  - Terzić-Vidojević, Amarela
AU  - Mihajlović, Sanja
AU  - Uzelac, Gordana
AU  - Golić, Nataša
AU  - Fira, Đorđe
AU  - Kojić, Milan
AU  - Topisirović, Ljubiša
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/770
AB  - The aim of this study was to identify and characterize the lactic acid bacteria (LAB) of artisanal Golija raw and cooked cows' milk cheeses traditionally manufactured without the addition of starter culture. A total of 188 Gram-positive and catalase-negative isolates of Golija cheeses were obtained from seven samples of different ripening time. Phenotype-based assays as well as rep-PCR and 16S rDNA sequence analysis were undertaken for all 188 LAB strains. The most diverse species were isolated from 20-day-old BGGO8 cheese (Lactobacillus fermentum, Lactobacillus plantarum, Lactobacillus casei/paracasei, Lactobacillus sucicola, Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis by. diacetylactis, Enterococcus faecium, Enterococcus durans and Leuconostoc mesenteroides). In other Golija cheeses Lactobacillus reuteri, Lactobacillus curvatus, Lactobacillus rhamnosus, Lactococcus lactis subsp. cremoris, Lactococcus garvieae, Streptococcus thermophilus and Leuconostoc pseudomesenteroides were found. Pronounced antimicrobial properties showed enterococci (13/42) and lactococci (12/31), while the good proteolytic activity demonstrated lactococci (13/31) and lactobacilli (10/29).
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses
EP  - 192
IS  - 1
SP  - 179
VL  - 66
DO  - 10.2298/ABS1401179T
ER  - 

@article{
author = "Terzić-Vidojević, Amarela and Mihajlović, Sanja and Uzelac, Gordana and Golić, Nataša and Fira, Đorđe and Kojić, Milan and Topisirović, Ljubiša",
year = "2014",
abstract = "The aim of this study was to identify and characterize the lactic acid bacteria (LAB) of artisanal Golija raw and cooked cows' milk cheeses traditionally manufactured without the addition of starter culture. A total of 188 Gram-positive and catalase-negative isolates of Golija cheeses were obtained from seven samples of different ripening time. Phenotype-based assays as well as rep-PCR and 16S rDNA sequence analysis were undertaken for all 188 LAB strains. The most diverse species were isolated from 20-day-old BGGO8 cheese (Lactobacillus fermentum, Lactobacillus plantarum, Lactobacillus casei/paracasei, Lactobacillus sucicola, Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis by. diacetylactis, Enterococcus faecium, Enterococcus durans and Leuconostoc mesenteroides). In other Golija cheeses Lactobacillus reuteri, Lactobacillus curvatus, Lactobacillus rhamnosus, Lactococcus lactis subsp. cremoris, Lactococcus garvieae, Streptococcus thermophilus and Leuconostoc pseudomesenteroides were found. Pronounced antimicrobial properties showed enterococci (13/42) and lactococci (12/31), while the good proteolytic activity demonstrated lactococci (13/31) and lactobacilli (10/29).",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses",
pages = "192-179",
number = "1",
volume = "66",
doi = "10.2298/ABS1401179T"
}

Terzić-Vidojević, A., Mihajlović, S., Uzelac, G., Golić, N., Fira, Đ., Kojić, M.,& Topisirović, L.. (2014). Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(1), 179-192.
https://doi.org/10.2298/ABS1401179T

Terzić-Vidojević A, Mihajlović S, Uzelac G, Golić N, Fira Đ, Kojić M, Topisirović L. Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses. in Archives of Biological Sciences. 2014;66(1):179-192.
doi:10.2298/ABS1401179T .

Terzić-Vidojević, Amarela, Mihajlović, Sanja, Uzelac, Gordana, Golić, Nataša, Fira, Đorđe, Kojić, Milan, Topisirović, Ljubiša, "Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses" in Archives of Biological Sciences, 66, no. 1 (2014):179-192,
https://doi.org/10.2298/ABS1401179T . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Lozo, Jelena
AU  - Terzić-Vidojević, Amarela
AU  - Fira, Đorđe
AU  - Kojić, Milan
AU  - Golić, Nataša
AU  - Begović, Jelena
AU  - Topisirović, Ljubiša
PY  - 2013
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/632
AB  - Lactobacillus helveticus BGRA43 is a human intestinal isolate showing antimicrobial activity, amongst others, against Yersinia enterocolitica, Shigella sonnei, Shigella flexneri, and Streptococcus pneumoniae. BGRA43 produces PrtH proteinase with proteolytic activity on both casein and beta-lactoglobulin (BLG). BGRA43 is able to reduce the allergenicity of BLG. Bioactive peptides released in BGRA43 fermented milk are potent modulators of innate immunity by modulating the production of proinflammatory cytokines IL-6 and TNF-alpha. BGRA43 is able to survive in simulated gastric and intestinal conditions. The growth of BGRA43 in milk results in a fast acidification lowering the milk pH to 4.53 generating mild, homogeneous, and viscous yogurt-like product. The strain BGRA43 grows suitably in pure cow or goat's milk as well as in milk containing inulin or nutrim even when they are used as the sole carbon source. It is suggested that strain BGRA43 could be used as a single-strain culture for the preparation of yogurt-like products from bovine or caprine milk. Overall, L. helveticus BGRA43 could be considered as a potential probiotic candidate with appropriate technological properties attractive for the dairy industry.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Technological and probiotic potential of BGRA43 a natural isolate of Lactobacillus helveticus
VL  - 4
DO  - 10.3389/fmicb.2013.00002
ER  - 

@article{
author = "Strahinić, Ivana and Lozo, Jelena and Terzić-Vidojević, Amarela and Fira, Đorđe and Kojić, Milan and Golić, Nataša and Begović, Jelena and Topisirović, Ljubiša",
year = "2013",
abstract = "Lactobacillus helveticus BGRA43 is a human intestinal isolate showing antimicrobial activity, amongst others, against Yersinia enterocolitica, Shigella sonnei, Shigella flexneri, and Streptococcus pneumoniae. BGRA43 produces PrtH proteinase with proteolytic activity on both casein and beta-lactoglobulin (BLG). BGRA43 is able to reduce the allergenicity of BLG. Bioactive peptides released in BGRA43 fermented milk are potent modulators of innate immunity by modulating the production of proinflammatory cytokines IL-6 and TNF-alpha. BGRA43 is able to survive in simulated gastric and intestinal conditions. The growth of BGRA43 in milk results in a fast acidification lowering the milk pH to 4.53 generating mild, homogeneous, and viscous yogurt-like product. The strain BGRA43 grows suitably in pure cow or goat's milk as well as in milk containing inulin or nutrim even when they are used as the sole carbon source. It is suggested that strain BGRA43 could be used as a single-strain culture for the preparation of yogurt-like products from bovine or caprine milk. Overall, L. helveticus BGRA43 could be considered as a potential probiotic candidate with appropriate technological properties attractive for the dairy industry.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Technological and probiotic potential of BGRA43 a natural isolate of Lactobacillus helveticus",
volume = "4",
doi = "10.3389/fmicb.2013.00002"
}

Strahinić, I., Lozo, J., Terzić-Vidojević, A., Fira, Đ., Kojić, M., Golić, N., Begović, J.,& Topisirović, L.. (2013). Technological and probiotic potential of BGRA43 a natural isolate of Lactobacillus helveticus. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 4.
https://doi.org/10.3389/fmicb.2013.00002

Strahinić I, Lozo J, Terzić-Vidojević A, Fira Đ, Kojić M, Golić N, Begović J, Topisirović L. Technological and probiotic potential of BGRA43 a natural isolate of Lactobacillus helveticus. in Frontiers in Microbiology. 2013;4.
doi:10.3389/fmicb.2013.00002 .

Strahinić, Ivana, Lozo, Jelena, Terzić-Vidojević, Amarela, Fira, Đorđe, Kojić, Milan, Golić, Nataša, Begović, Jelena, Topisirović, Ljubiša, "Technological and probiotic potential of BGRA43 a natural isolate of Lactobacillus helveticus" in Frontiers in Microbiology, 4 (2013),
https://doi.org/10.3389/fmicb.2013.00002 . .

TY  - JOUR
AU  - Ivanović, Zarko
AU  - Stanković, Slaviša
AU  - Zivković, Svetlana
AU  - Gavrilović, Veljko
AU  - Kojić, Milan
AU  - Fira, Đorđe
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/564
AB  - Infection of fruit trees by Pseudomonas syringae is a potentially serious problem that may limit the establishment and sustained productivity of pome and stone fruit orchards in Serbia. To estimate possible diversity of Pseudomonas syringae fruit trees strains, we collected a set of strains in several areas of Serbia. The samples were taken from infected orchards with raspberry, plum, cherry, sour cherry, peach, pear and apple trees. Genetic diversity of P. syringae strains isolated from fruit trees was determined by using SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and REP-PCR. Molecular analysis showed that most of isolates had unique profiles, with the exception of isolates from plum and cherry that displayed profiles identical to each other and similar to P. syringae pv. morsprunorum. The study presented here clearly demonstrates the discriminative power of molecular techniques in enabling a detailed analysis of the genetic variations between strains of P. syringae from different pome and stone fruit hosts in Serbia.
PB  - Springer, Dordrecht
T2  - European Journal of Plant Pathology
T1  - Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia
EP  - 203
IS  - 1
SP  - 191
VL  - 134
DO  - 10.1007/s10658-012-9978-4
ER  - 

@article{
author = "Ivanović, Zarko and Stanković, Slaviša and Zivković, Svetlana and Gavrilović, Veljko and Kojić, Milan and Fira, Đorđe",
year = "2012",
abstract = "Infection of fruit trees by Pseudomonas syringae is a potentially serious problem that may limit the establishment and sustained productivity of pome and stone fruit orchards in Serbia. To estimate possible diversity of Pseudomonas syringae fruit trees strains, we collected a set of strains in several areas of Serbia. The samples were taken from infected orchards with raspberry, plum, cherry, sour cherry, peach, pear and apple trees. Genetic diversity of P. syringae strains isolated from fruit trees was determined by using SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and REP-PCR. Molecular analysis showed that most of isolates had unique profiles, with the exception of isolates from plum and cherry that displayed profiles identical to each other and similar to P. syringae pv. morsprunorum. The study presented here clearly demonstrates the discriminative power of molecular techniques in enabling a detailed analysis of the genetic variations between strains of P. syringae from different pome and stone fruit hosts in Serbia.",
publisher = "Springer, Dordrecht",
journal = "European Journal of Plant Pathology",
title = "Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia",
pages = "203-191",
number = "1",
volume = "134",
doi = "10.1007/s10658-012-9978-4"
}

Ivanović, Z., Stanković, S., Zivković, S., Gavrilović, V., Kojić, M.,& Fira, Đ.. (2012). Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia. in European Journal of Plant Pathology
Springer, Dordrecht., 134(1), 191-203.
https://doi.org/10.1007/s10658-012-9978-4

Ivanović Z, Stanković S, Zivković S, Gavrilović V, Kojić M, Fira Đ. Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia. in European Journal of Plant Pathology. 2012;134(1):191-203.
doi:10.1007/s10658-012-9978-4 .

Ivanović, Zarko, Stanković, Slaviša, Zivković, Svetlana, Gavrilović, Veljko, Kojić, Milan, Fira, Đorđe, "Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia" in European Journal of Plant Pathology, 134, no. 1 (2012):191-203,
https://doi.org/10.1007/s10658-012-9978-4 . .

TY  - JOUR
AU  - Tolinački, Maja
AU  - Lozo, Jelena
AU  - Veljović, Katarina
AU  - Kojić, Milan
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/556
AB  - Cilj ove studije je izučavanje antimikrobnog potencijala 52 prirodna izolata vrste L. casei/paracasei. Učestalost gena koji kodiraju BacSJ (bacSJ2-8/bacSJ2-8i genski klaster), acidocin 8912 (acdT), ABC-transporter (abcT) i pomoćni protein (acc) su takođe izučavani. Genski klaster bacSJ2-8/bacSJ2-8i prisutan je kod 49 (94.23%), a acdT kod 41 (78.85%) od 52 testirana soja. Četrdeset sojeva (76.92%) poseduje oba analizirana gena. Interesantno je da samo 17 sojeva (32.69%) koji poseduju bacSJ2-8/bacSJ2-8i genski klaster i/ili acdT gen proizvode bakteriocine. Soj L. paracasei BGNK1-62 poseduje bacSJ2-8/bacSJ2-8i genski klaster, ali ne proizvodi bakteriocin BacSJ što je verovatno posledica nedostatka abcT i acc gena. Nakon transformacije soja BGNK1-62 konstruktom pA2A koji poseduje abcT i acc gene ostvarena je proizvodnja bakteriocina BacSJ. Osim toga, utvrđeno je da soj L. paracasei BGGR2-66 proizvodi nov bakteriocin označen kao BacGR, koji je biohemijski okarakterisan, a određena je i njegova N-terminalna sekvenca.
AB  - The aim of this study was to investigate the antimicrobial potential of 52 natural isolates of Lactobacillus casei/paracasei. The incidence of relevant genes encoding BacSJ (bacSJ2-8/bacSJ2-8i gene cluster), acidocin 8912 (acdT), ABC-transporter (abcT) and accessory protein (acc) was also studied. These genes were found to be widespread amongst the analyzed L. casei/paracasei strains. The bacSJ2-8/bacSJ2-8i gene cluster was present in 49 (94.23%) and acdT in 41 (78.85%) of the 52 tested strains. Forty of these strains (76.92%) harbored both analyzed genes. Interestingly, only 17 strains (32.69%) with the bacSJ2-8/bacSJ2-8i gene cluster and/or the acdT gene showed bacteriocin production. Strain L. paracasei BGNK1-62 contained the bacSJ2-8/bacSJ2-8i gene cluster, but did not produce bacteriocin BacSJ possibly due to absence of the abcT and acc genes. Hence, these genes were introduced into BGNK1-62 by transformation with constructed plasmid pA2A, after which BacSJ was produced. In addition, it was found that L. paracasei BGGR2-66 produced new bacteriocin designated as BacGR that was biochemically characterized and its N- terminal sequence was determined.
PB  - Društvo genetičara Srbije, Beograd
T2  - Genetika-Belgrade
T1  - Izučavanje antimikrobnog potencijala prirodnih izolata Lactobacillus casei/paracasei grupe
T1  - Examination of antimicrobial potential in natural isolates of lactobacillus casei/paracasei group
EP  - 677
IS  - 3
SP  - 661
VL  - 44
DO  - 10.2298/GENSR1203661T
ER  - 

@article{
author = "Tolinački, Maja and Lozo, Jelena and Veljović, Katarina and Kojić, Milan and Fira, Đorđe and Topisirović, Ljubiša",
year = "2012",
abstract = "Cilj ove studije je izučavanje antimikrobnog potencijala 52 prirodna izolata vrste L. casei/paracasei. Učestalost gena koji kodiraju BacSJ (bacSJ2-8/bacSJ2-8i genski klaster), acidocin 8912 (acdT), ABC-transporter (abcT) i pomoćni protein (acc) su takođe izučavani. Genski klaster bacSJ2-8/bacSJ2-8i prisutan je kod 49 (94.23%), a acdT kod 41 (78.85%) od 52 testirana soja. Četrdeset sojeva (76.92%) poseduje oba analizirana gena. Interesantno je da samo 17 sojeva (32.69%) koji poseduju bacSJ2-8/bacSJ2-8i genski klaster i/ili acdT gen proizvode bakteriocine. Soj L. paracasei BGNK1-62 poseduje bacSJ2-8/bacSJ2-8i genski klaster, ali ne proizvodi bakteriocin BacSJ što je verovatno posledica nedostatka abcT i acc gena. Nakon transformacije soja BGNK1-62 konstruktom pA2A koji poseduje abcT i acc gene ostvarena je proizvodnja bakteriocina BacSJ. Osim toga, utvrđeno je da soj L. paracasei BGGR2-66 proizvodi nov bakteriocin označen kao BacGR, koji je biohemijski okarakterisan, a određena je i njegova N-terminalna sekvenca., The aim of this study was to investigate the antimicrobial potential of 52 natural isolates of Lactobacillus casei/paracasei. The incidence of relevant genes encoding BacSJ (bacSJ2-8/bacSJ2-8i gene cluster), acidocin 8912 (acdT), ABC-transporter (abcT) and accessory protein (acc) was also studied. These genes were found to be widespread amongst the analyzed L. casei/paracasei strains. The bacSJ2-8/bacSJ2-8i gene cluster was present in 49 (94.23%) and acdT in 41 (78.85%) of the 52 tested strains. Forty of these strains (76.92%) harbored both analyzed genes. Interestingly, only 17 strains (32.69%) with the bacSJ2-8/bacSJ2-8i gene cluster and/or the acdT gene showed bacteriocin production. Strain L. paracasei BGNK1-62 contained the bacSJ2-8/bacSJ2-8i gene cluster, but did not produce bacteriocin BacSJ possibly due to absence of the abcT and acc genes. Hence, these genes were introduced into BGNK1-62 by transformation with constructed plasmid pA2A, after which BacSJ was produced. In addition, it was found that L. paracasei BGGR2-66 produced new bacteriocin designated as BacGR that was biochemically characterized and its N- terminal sequence was determined.",
publisher = "Društvo genetičara Srbije, Beograd",
journal = "Genetika-Belgrade",
title = "Izučavanje antimikrobnog potencijala prirodnih izolata Lactobacillus casei/paracasei grupe, Examination of antimicrobial potential in natural isolates of lactobacillus casei/paracasei group",
pages = "677-661",
number = "3",
volume = "44",
doi = "10.2298/GENSR1203661T"
}

Tolinački, M., Lozo, J., Veljović, K., Kojić, M., Fira, Đ.,& Topisirović, L.. (2012). Izučavanje antimikrobnog potencijala prirodnih izolata Lactobacillus casei/paracasei grupe. in Genetika-Belgrade
Društvo genetičara Srbije, Beograd., 44(3), 661-677.
https://doi.org/10.2298/GENSR1203661T

Tolinački M, Lozo J, Veljović K, Kojić M, Fira Đ, Topisirović L. Izučavanje antimikrobnog potencijala prirodnih izolata Lactobacillus casei/paracasei grupe. in Genetika-Belgrade. 2012;44(3):661-677.
doi:10.2298/GENSR1203661T .

Tolinački, Maja, Lozo, Jelena, Veljović, Katarina, Kojić, Milan, Fira, Đorđe, Topisirović, Ljubiša, "Izučavanje antimikrobnog potencijala prirodnih izolata Lactobacillus casei/paracasei grupe" in Genetika-Belgrade, 44, no. 3 (2012):661-677,
https://doi.org/10.2298/GENSR1203661T . .

TY  - JOUR
AU  - Berić, Tanja
AU  - Kojić, Milan
AU  - Stanković, Slaviša
AU  - Topisirović, Ljubiša
AU  - Degrassi, Giuliano
AU  - Myers, Michael
AU  - Venturi, Vittorio
AU  - Fira, Đorđe
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/574
AB  - Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria
EP  - 31
IS  - 1
SP  - 25
VL  - 50
UR  - https://hdl.handle.net/21.15107/rcub_imagine_574
ER  - 

@article{
author = "Berić, Tanja and Kojić, Milan and Stanković, Slaviša and Topisirović, Ljubiša and Degrassi, Giuliano and Myers, Michael and Venturi, Vittorio and Fira, Đorđe",
year = "2012",
abstract = "Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria",
pages = "31-25",
number = "1",
volume = "50",
url = "https://hdl.handle.net/21.15107/rcub_imagine_574"
}

Berić, T., Kojić, M., Stanković, S., Topisirović, L., Degrassi, G., Myers, M., Venturi, V.,& Fira, Đ.. (2012). Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology
University of Zagreb., 50(1), 25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574

Berić T, Kojić M, Stanković S, Topisirović L, Degrassi G, Myers M, Venturi V, Fira Đ. Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology. 2012;50(1):25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574 .

Berić, Tanja, Kojić, Milan, Stanković, Slaviša, Topisirović, Ljubiša, Degrassi, Giuliano, Myers, Michael, Venturi, Vittorio, Fira, Đorđe, "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria" in Food Technology and Biotechnology, 50, no. 1 (2012):25-31,
https://hdl.handle.net/21.15107/rcub_imagine_574 .

TY  - CHAP
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Golić, Nataša
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/519
PB  - CABI Publishing
T2  - Natural Antimicrobials in Food Safety and Quality
T1  - A survey of antimicrobial activity in lactic acid bacteria of different origin
EP  - 38
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_imagine_519
ER  - 

@inbook{
author = "Topisirović, Ljubiša and Kojić, Milan and Strahinić, Ivana and Fira, Đorđe and Golić, Nataša",
year = "2011",
publisher = "CABI Publishing",
journal = "Natural Antimicrobials in Food Safety and Quality",
booktitle = "A survey of antimicrobial activity in lactic acid bacteria of different origin",
pages = "38-27",
url = "https://hdl.handle.net/21.15107/rcub_imagine_519"
}

Topisirović, L., Kojić, M., Strahinić, I., Fira, Đ.,& Golić, N.. (2011). A survey of antimicrobial activity in lactic acid bacteria of different origin. in Natural Antimicrobials in Food Safety and Quality
CABI Publishing., 27-38.
https://hdl.handle.net/21.15107/rcub_imagine_519

Topisirović L, Kojić M, Strahinić I, Fira Đ, Golić N. A survey of antimicrobial activity in lactic acid bacteria of different origin. in Natural Antimicrobials in Food Safety and Quality. 2011;:27-38.
https://hdl.handle.net/21.15107/rcub_imagine_519 .

Topisirović, Ljubiša, Kojić, Milan, Strahinić, Ivana, Fira, Đorđe, Golić, Nataša, "A survey of antimicrobial activity in lactic acid bacteria of different origin" in Natural Antimicrobials in Food Safety and Quality (2011):27-38,
https://hdl.handle.net/21.15107/rcub_imagine_519 .

TY  - JOUR
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Jovčić, Branko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/421
AB  - The aim of this paper was to research the molecular cloning of genes encoding the novel bacteriocin BacSJ from Lactobacillus paracasei subsp. paracasei BGSJ2-8 by using a newly constructed shuttle cloning vector pA13. A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli, Lactobacillus and Lactococcus strains, showing a high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L. paracasei subsp. paracasei BGSJ2-8 was cloned in the pA13 using BamHI, obtaining the construct pB5. Sequencing and in silico analysis of the pB5 revealed 15 open reading frames (ORF). Plasmid pSJ2-8 harbors the genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. The combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled the determination of the primary structure of a bacteriocin BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirement for the production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to the class II bacteriocins. The shuttle cloning vector pA13 could be used as a tool for genetic manipulations in lactobacilli and lactococci.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912
EP  - 243
IS  - 2
SP  - 231
VL  - 62
DO  - 10.2298/ABS1002231K
ER  - 

@article{
author = "Kojić, Milan and Lozo, Jelena and Jovčić, Branko and Strahinić, Ivana and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "The aim of this paper was to research the molecular cloning of genes encoding the novel bacteriocin BacSJ from Lactobacillus paracasei subsp. paracasei BGSJ2-8 by using a newly constructed shuttle cloning vector pA13. A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli, Lactobacillus and Lactococcus strains, showing a high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L. paracasei subsp. paracasei BGSJ2-8 was cloned in the pA13 using BamHI, obtaining the construct pB5. Sequencing and in silico analysis of the pB5 revealed 15 open reading frames (ORF). Plasmid pSJ2-8 harbors the genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. The combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled the determination of the primary structure of a bacteriocin BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirement for the production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to the class II bacteriocins. The shuttle cloning vector pA13 could be used as a tool for genetic manipulations in lactobacilli and lactococci.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912",
pages = "243-231",
number = "2",
volume = "62",
doi = "10.2298/ABS1002231K"
}

Kojić, M., Lozo, J., Jovčić, B., Strahinić, I., Fira, Đ.,& Topisirović, L.. (2010). A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(2), 231-243.
https://doi.org/10.2298/ABS1002231K

Kojić M, Lozo J, Jovčić B, Strahinić I, Fira Đ, Topisirović L. A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912. in Archives of Biological Sciences. 2010;62(2):231-243.
doi:10.2298/ABS1002231K .

Kojić, Milan, Lozo, Jelena, Jovčić, Branko, Strahinić, Ivana, Fira, Đorđe, Topisirović, Ljubiša, "A successful use of a new shuttle cloning vector pA13 for the cloning of the bacteriocins BacSJ and acidocin 8912" in Archives of Biological Sciences, 62, no. 2 (2010):231-243,
https://doi.org/10.2298/ABS1002231K . .

TY  - JOUR
AU  - Tolinački, Maja
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Terzić-Vidojević, Amarela
AU  - Topisirović, Ljubiša
AU  - Fira, Đorđe
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/405
AB  - The strain Lactobacillus paracasei subsp. paracasei BGUB9 that was isolated from traditionally homemade hard cheese produces bacteriocin designated as BacUB9, with an approximate molecular mass of 4 kDa. Biochemical characterization and the antimicrobial activity test of BacUB9 were performed. The onset of BacUB9 biosynthesis was observed at the end of an exponential phase of growth. Bacteriocin UB9 retained the antimicrobial activity within the pH range from 1 to 10 and after treatment at 100oC for 30 min. The bacteriocin is susceptible to the activity of proteolytic enzymes. Bacteriocin BacUB9 has a very narrow antimicrobial spectrum, limited to several strains that belong to closely related species. The effect of BGUB9 on the growth of the strain Lactobacillus paracasei subsp. paracasei BGHN14 in a mixed culture was monitored. The mode of action of BacUB9 on the strain BGHN14 was identified as bacteriostatic. Plasmid curing results indicated that a plasmid, designated as pUB9, seemed to be responsible for both bacteriocin BacUB9 production and host immunity.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9
EP  - 899
IS  - 4
SP  - 889
VL  - 62
DO  - 10.2298/ABS1004889T
ER  - 

@article{
author = "Tolinački, Maja and Kojić, Milan and Lozo, Jelena and Terzić-Vidojević, Amarela and Topisirović, Ljubiša and Fira, Đorđe",
year = "2010",
abstract = "The strain Lactobacillus paracasei subsp. paracasei BGUB9 that was isolated from traditionally homemade hard cheese produces bacteriocin designated as BacUB9, with an approximate molecular mass of 4 kDa. Biochemical characterization and the antimicrobial activity test of BacUB9 were performed. The onset of BacUB9 biosynthesis was observed at the end of an exponential phase of growth. Bacteriocin UB9 retained the antimicrobial activity within the pH range from 1 to 10 and after treatment at 100oC for 30 min. The bacteriocin is susceptible to the activity of proteolytic enzymes. Bacteriocin BacUB9 has a very narrow antimicrobial spectrum, limited to several strains that belong to closely related species. The effect of BGUB9 on the growth of the strain Lactobacillus paracasei subsp. paracasei BGHN14 in a mixed culture was monitored. The mode of action of BacUB9 on the strain BGHN14 was identified as bacteriostatic. Plasmid curing results indicated that a plasmid, designated as pUB9, seemed to be responsible for both bacteriocin BacUB9 production and host immunity.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9",
pages = "899-889",
number = "4",
volume = "62",
doi = "10.2298/ABS1004889T"
}

Tolinački, M., Kojić, M., Lozo, J., Terzić-Vidojević, A., Topisirović, L.,& Fira, Đ.. (2010). Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(4), 889-899.
https://doi.org/10.2298/ABS1004889T

Tolinački M, Kojić M, Lozo J, Terzić-Vidojević A, Topisirović L, Fira Đ. Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9. in Archives of Biological Sciences. 2010;62(4):889-899.
doi:10.2298/ABS1004889T .

Tolinački, Maja, Kojić, Milan, Lozo, Jelena, Terzić-Vidojević, Amarela, Topisirović, Ljubiša, Fira, Đorđe, "Characterization of the bacteriocin-producing strain Lactobacillus paracasei subsp. paracasei BGUB9" in Archives of Biological Sciences, 62, no. 4 (2010):889-899,
https://doi.org/10.2298/ABS1004889T . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Jovčić, Branko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/432
AB  - A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli. Lactobacillus and Lactococcus strains. It showed high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L paracasei subsp. paracasei BGSJ2-8 was cloned into pA13 using BamHI to obtain the construct, pB5. Sequencing and in silico analysis of pB5 revealed fifteen open reading frames (ORF). Plasmid pSJ2-8 harbours genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. Combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled determination of the primary structure of bacteriocin BacSJ. The bacSJ2-8 gene encodes 68-amino-acid peptide with a double-glycine leader peptide consisting of 18 amino acids, followed by the orf2 (bacSJ2-8i) which encodes the immunity protein of BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirements for production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to class II bacteriocins.
PB  - Elsevier, Amsterdam
T2  - International Journal of Food Microbiology
T1  - Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8
EP  - 124
IS  - 2-3
SP  - 117
VL  - 140
DO  - 10.1016/j.ijfoodmicro.2010.04.010
ER  - 

@article{
author = "Kojić, Milan and Lozo, Jelena and Jovčić, Branko and Strahinić, Ivana and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "A new shuttle-cloning vector, pA13, was constructed and successfully introduced into Escherichia coli. Lactobacillus and Lactococcus strains. It showed high segregational and structural stability in all three hosts. The natural plasmid pSJ2-8 from L paracasei subsp. paracasei BGSJ2-8 was cloned into pA13 using BamHI to obtain the construct, pB5. Sequencing and in silico analysis of pB5 revealed fifteen open reading frames (ORF). Plasmid pSJ2-8 harbours genes encoding the production of two bacteriocins, BacSJ and acidocin 8912. Combined N-terminal amino acid sequencing of BacSJ in combination with DNA sequencing of the bacSJ2-8 gene enabled determination of the primary structure of bacteriocin BacSJ. The bacSJ2-8 gene encodes 68-amino-acid peptide with a double-glycine leader peptide consisting of 18 amino acids, followed by the orf2 (bacSJ2-8i) which encodes the immunity protein of BacSJ. The production and functional expression of BacSJ in homologous and heterologous hosts suggest that bacSJ2-8 and bacSJ2-8i together with the genes encoding the ABC transporter and accessory protein are the minimal requirements for production of BacSJ. Biochemical and genetic analyses showed that BacSJ belongs to class II bacteriocins.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Food Microbiology",
title = "Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8",
pages = "124-117",
number = "2-3",
volume = "140",
doi = "10.1016/j.ijfoodmicro.2010.04.010"
}

Kojić, M., Lozo, J., Jovčić, B., Strahinić, I., Fira, Đ.,& Topisirović, L.. (2010). Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8. in International Journal of Food Microbiology
Elsevier, Amsterdam., 140(2-3), 117-124.
https://doi.org/10.1016/j.ijfoodmicro.2010.04.010

Kojić M, Lozo J, Jovčić B, Strahinić I, Fira Đ, Topisirović L. Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8. in International Journal of Food Microbiology. 2010;140(2-3):117-124.
doi:10.1016/j.ijfoodmicro.2010.04.010 .

Kojić, Milan, Lozo, Jelena, Jovčić, Branko, Strahinić, Ivana, Fira, Đorđe, Topisirović, Ljubiša, "Construction of a new shuttle vector and its use for cloning and expression of two plasmid-encoded bacteriocins from Lactobacillus paracasei subsp paracasei BGSJ2-8" in International Journal of Food Microbiology, 140, no. 2-3 (2010):117-124,
https://doi.org/10.1016/j.ijfoodmicro.2010.04.010 . .

TY  - JOUR
AU  - Begović, Jelena
AU  - Fira, Đorđe
AU  - Terzić-Vidojević, Amarela
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/414
AB  - Lactobacilli represent normal commensals of the human body, particularly in the gut and vagina where they protect these environments from incoming pathogens via a variety of mechanisms. The influence of the carbohydrate source present in reconstituted MRS growth medium on the different cell properties of two Lactobacillus rhamnosus strains were examined. Two human vaginal isolates, BGHV719 and exopolysaccharide producer strain BGHV954 were analyzed. The results demonstrated that unlike in reconstituted MRS with glucose as a carbon source, the presence of fructose, mannose, or rhamnose, significantly reduced cell surface hydrophobicity of both strains. In addition, differences in cell wall protein composition of L. rhamnosus BGHV719 and alterations in colony mucoidity of L. rhamnosus BGHV954 were also demonstrated. Light and SEM microscopy revealed differences on the cellular level when BGHV719 was cultivated in the presence of different sugars. The results of this study point out the importance of complex relationships between growth medium composition and the different aspects of bacterial behavior, and call for more detailed analyses of versatile bacterial responses to the changes in the environment, including vaginal ecosystem. This is especially important since lactobacilli are amongst the most widely used of probiotics.
PB  - SCIENDO, Warsaw
T2  - Central European Journal of Biology
T1  - Influence of carbohydrates on cell properties of Lactobacillus rhamnosus
EP  - 110
IS  - 1
SP  - 103
VL  - 5
DO  - 10.2478/s11535-009-0078-1
ER  - 

@article{
author = "Begović, Jelena and Fira, Đorđe and Terzić-Vidojević, Amarela and Topisirović, Ljubiša",
year = "2010",
abstract = "Lactobacilli represent normal commensals of the human body, particularly in the gut and vagina where they protect these environments from incoming pathogens via a variety of mechanisms. The influence of the carbohydrate source present in reconstituted MRS growth medium on the different cell properties of two Lactobacillus rhamnosus strains were examined. Two human vaginal isolates, BGHV719 and exopolysaccharide producer strain BGHV954 were analyzed. The results demonstrated that unlike in reconstituted MRS with glucose as a carbon source, the presence of fructose, mannose, or rhamnose, significantly reduced cell surface hydrophobicity of both strains. In addition, differences in cell wall protein composition of L. rhamnosus BGHV719 and alterations in colony mucoidity of L. rhamnosus BGHV954 were also demonstrated. Light and SEM microscopy revealed differences on the cellular level when BGHV719 was cultivated in the presence of different sugars. The results of this study point out the importance of complex relationships between growth medium composition and the different aspects of bacterial behavior, and call for more detailed analyses of versatile bacterial responses to the changes in the environment, including vaginal ecosystem. This is especially important since lactobacilli are amongst the most widely used of probiotics.",
publisher = "SCIENDO, Warsaw",
journal = "Central European Journal of Biology",
title = "Influence of carbohydrates on cell properties of Lactobacillus rhamnosus",
pages = "110-103",
number = "1",
volume = "5",
doi = "10.2478/s11535-009-0078-1"
}

Begović, J., Fira, Đ., Terzić-Vidojević, A.,& Topisirović, L.. (2010). Influence of carbohydrates on cell properties of Lactobacillus rhamnosus. in Central European Journal of Biology
SCIENDO, Warsaw., 5(1), 103-110.
https://doi.org/10.2478/s11535-009-0078-1

Begović J, Fira Đ, Terzić-Vidojević A, Topisirović L. Influence of carbohydrates on cell properties of Lactobacillus rhamnosus. in Central European Journal of Biology. 2010;5(1):103-110.
doi:10.2478/s11535-009-0078-1 .

Begović, Jelena, Fira, Đorđe, Terzić-Vidojević, Amarela, Topisirović, Ljubiša, "Influence of carbohydrates on cell properties of Lactobacillus rhamnosus" in Central European Journal of Biology, 5, no. 1 (2010):103-110,
https://doi.org/10.2478/s11535-009-0078-1 . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Kojić, Milan
AU  - Tolinački, Maja
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/465
AB  - Aims: The study of proteolytic activity and examination of proteinase gene region organization in proteolytically active Lactobacillus plantarum strains from different natural sources. Methods and Results: A set of 37 lactobacilli was distinguished by using multiplex PCR assay. Results showed that 34 strains were Lact. plantarum and three of them were Lact. paraplantarum. The examination of proteolytic activity revealed that 28 Lact. plantarum and two Lact. paraplantarum hydrolyse beta-casein. Further analyses of all proteolytically active Lact. plantarum with primers specific for different types of CEPs demonstrated that strain BGSJ3-18 has prtP catalytic domain as well as prtP-prtM intergenic region showing more than 95% sequence identity with the same regions present in Lact. paracasei, Lact. casei and L. lactis. No presence of prtB, prtH or prtR proteinase genes was detected in any of tested Lact. plantarum strains. Conclusions: One out of 28 analysed Lact. plantarum strains harbours the prtP-like gene. The other proteolytically active Lact. plantarum probably possesses a different type of extracellular proteinase(s). Significance and Impact of the Study: It is the first report about the presence of the prtP-like gene in Lact. plantarum, which illustrates the mobility of this gene and its presence in different species.
PB  - Wiley, Hoboken
T2  - Letters in Applied Microbiology
T1  - The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18
EP  - 49
IS  - 1
SP  - 43
VL  - 50
DO  - 10.1111/j.1472-765X.2009.02748.x
ER  - 

@article{
author = "Strahinić, Ivana and Kojić, Milan and Tolinački, Maja and Fira, Đorđe and Topisirović, Ljubiša",
year = "2010",
abstract = "Aims: The study of proteolytic activity and examination of proteinase gene region organization in proteolytically active Lactobacillus plantarum strains from different natural sources. Methods and Results: A set of 37 lactobacilli was distinguished by using multiplex PCR assay. Results showed that 34 strains were Lact. plantarum and three of them were Lact. paraplantarum. The examination of proteolytic activity revealed that 28 Lact. plantarum and two Lact. paraplantarum hydrolyse beta-casein. Further analyses of all proteolytically active Lact. plantarum with primers specific for different types of CEPs demonstrated that strain BGSJ3-18 has prtP catalytic domain as well as prtP-prtM intergenic region showing more than 95% sequence identity with the same regions present in Lact. paracasei, Lact. casei and L. lactis. No presence of prtB, prtH or prtR proteinase genes was detected in any of tested Lact. plantarum strains. Conclusions: One out of 28 analysed Lact. plantarum strains harbours the prtP-like gene. The other proteolytically active Lact. plantarum probably possesses a different type of extracellular proteinase(s). Significance and Impact of the Study: It is the first report about the presence of the prtP-like gene in Lact. plantarum, which illustrates the mobility of this gene and its presence in different species.",
publisher = "Wiley, Hoboken",
journal = "Letters in Applied Microbiology",
title = "The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18",
pages = "49-43",
number = "1",
volume = "50",
doi = "10.1111/j.1472-765X.2009.02748.x"
}

Strahinić, I., Kojić, M., Tolinački, M., Fira, Đ.,& Topisirović, L.. (2010). The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18. in Letters in Applied Microbiology
Wiley, Hoboken., 50(1), 43-49.
https://doi.org/10.1111/j.1472-765X.2009.02748.x

Strahinić I, Kojić M, Tolinački M, Fira Đ, Topisirović L. The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18. in Letters in Applied Microbiology. 2010;50(1):43-49.
doi:10.1111/j.1472-765X.2009.02748.x .

Strahinić, Ivana, Kojić, Milan, Tolinački, Maja, Fira, Đorđe, Topisirović, Ljubiša, "The presence of prtP proteinase gene in natural isolate Lactobacillus plantarum BGSJ3-18" in Letters in Applied Microbiology, 50, no. 1 (2010):43-49,
https://doi.org/10.1111/j.1472-765X.2009.02748.x . .

TY  - JOUR
AU  - Strahinić, Ivana
AU  - Kojić, Milan
AU  - Tolinački, Maja
AU  - Fira, Đorđe
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/366
AB  - Strain Lactococcus lactis subsp. lactis bv. diacetylactis S50 harbours five theta-replicating plasmids (pS6, pS7a, pS7b, pS80 and pS140). The aim of this study was to characterize domains involved in the replication and conjugative mobilization of the small plasmids pS7a and pS7b, which are structurally very similar. Complete nucleotide sequences of pS7a and pS7b were determined by cloning DNA fragments of different sizes into Escherichia coli vectors. Linearized plasmids and four EcoRI fragments of the pS7a and pS7b were cloned into an origin probe vector. Constructed plasmids (pSEV10, pSK10, pISE1a and pISE1b) were able to replicate in the strain L. lactis subsp. cremoris MG1363. In addition, experiments showed that plasmids pS7a and pS7b contained oriT sequences and their conjugative transfer directly depended on the presence of pS80 in donor cells. Plasmids pS7a and pS7b contained typical lactococcal theta replication origin and repB gene that enable them to replicate in the strain L. lactis subsp. cremoris MG1363. Plasmid pS80 plays a key role in the conjugative transfer of small plasmids. Plasmids pS7a and pS7b-based derivatives could be valuable tools for genetic manipulation, studying processes of plasmid maintenance and horizontal gene transfer in lactococci.
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors
EP  - 88
IS  - 1
SP  - 78
VL  - 106
DO  - 10.1111/j.1365-2672.2008.03977.x
ER  - 

@article{
author = "Strahinić, Ivana and Kojić, Milan and Tolinački, Maja and Fira, Đorđe and Topisirović, Ljubiša",
year = "2009",
abstract = "Strain Lactococcus lactis subsp. lactis bv. diacetylactis S50 harbours five theta-replicating plasmids (pS6, pS7a, pS7b, pS80 and pS140). The aim of this study was to characterize domains involved in the replication and conjugative mobilization of the small plasmids pS7a and pS7b, which are structurally very similar. Complete nucleotide sequences of pS7a and pS7b were determined by cloning DNA fragments of different sizes into Escherichia coli vectors. Linearized plasmids and four EcoRI fragments of the pS7a and pS7b were cloned into an origin probe vector. Constructed plasmids (pSEV10, pSK10, pISE1a and pISE1b) were able to replicate in the strain L. lactis subsp. cremoris MG1363. In addition, experiments showed that plasmids pS7a and pS7b contained oriT sequences and their conjugative transfer directly depended on the presence of pS80 in donor cells. Plasmids pS7a and pS7b contained typical lactococcal theta replication origin and repB gene that enable them to replicate in the strain L. lactis subsp. cremoris MG1363. Plasmid pS80 plays a key role in the conjugative transfer of small plasmids. Plasmids pS7a and pS7b-based derivatives could be valuable tools for genetic manipulation, studying processes of plasmid maintenance and horizontal gene transfer in lactococci.",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors",
pages = "88-78",
number = "1",
volume = "106",
doi = "10.1111/j.1365-2672.2008.03977.x"
}

Strahinić, I., Kojić, M., Tolinački, M., Fira, Đ.,& Topisirović, L.. (2009). Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors. in Journal of Applied Microbiology
Wiley, Hoboken., 106(1), 78-88.
https://doi.org/10.1111/j.1365-2672.2008.03977.x

Strahinić I, Kojić M, Tolinački M, Fira Đ, Topisirović L. Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors. in Journal of Applied Microbiology. 2009;106(1):78-88.
doi:10.1111/j.1365-2672.2008.03977.x .

Strahinić, Ivana, Kojić, Milan, Tolinački, Maja, Fira, Đorđe, Topisirović, Ljubiša, "Molecular characterization of plasmids pS7a and pS7b from Lactococcus lactis subsp lactis bv. diacetylactis S50 as a base for the construction of mobilizable cloning vectors" in Journal of Applied Microbiology, 106, no. 1 (2009):78-88,
https://doi.org/10.1111/j.1365-2672.2008.03977.x . .

TY  - JOUR
AU  - Veljović, Katarina
AU  - Fira, Đorđe
AU  - Terzić-Vidojević, Amarela
AU  - Abriouel, Hikmate
AU  - Galvez, Antonio
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/378
AB  - A collection of 26 enterococci isolated from dairy and meat products were tested for antimicrobial and proteolytic activity. Enterococcus faecium and E. faecalis were the most frequent species among tested enterococci, and 11 isolates produced antimicrobial compounds. Results revealed that 10 out of 11 enterococci synthesized enterocins showing antimicrobial activity against food-born pathogen such as Listeria monocytogenes and Staphylococcus aureus. The broadest spectrum of antimicrobial activity was detected in E. faecalis BGPT1-10P and BGPT1-78. E. faecalis BG221 showed antimicrobial activity that was not related to production of enterocin, H2O2 or organic acid. Twenty-five enterococci showed strong or moderate proteolytic activity towards beta-casein. Two isolates, BGPT1-10P and BGPT1-78, showed the most intense hydrolysis of alpha(s1)-, beta-, kappa-casein fractions, total casein as well as gelatin. Extracellular BGPT1-10P and BGPT1-78 proteinases have a molecular mass of about 29 kDa. Bacteriocin production and proteinase activity of natural isolates of enterococci may be of technological interest in dairy and meat-fermented products.
PB  - Springer, New York
T2  - European Food Research and Technology
T1  - Evaluation of antimicrobial and proteolytic activity of enterococci isolated from fermented products
EP  - 70
IS  - 1
SP  - 63
VL  - 230
DO  - 10.1007/s00217-009-1137-6
ER  - 

@article{
author = "Veljović, Katarina and Fira, Đorđe and Terzić-Vidojević, Amarela and Abriouel, Hikmate and Galvez, Antonio and Topisirović, Ljubiša",
year = "2009",
abstract = "A collection of 26 enterococci isolated from dairy and meat products were tested for antimicrobial and proteolytic activity. Enterococcus faecium and E. faecalis were the most frequent species among tested enterococci, and 11 isolates produced antimicrobial compounds. Results revealed that 10 out of 11 enterococci synthesized enterocins showing antimicrobial activity against food-born pathogen such as Listeria monocytogenes and Staphylococcus aureus. The broadest spectrum of antimicrobial activity was detected in E. faecalis BGPT1-10P and BGPT1-78. E. faecalis BG221 showed antimicrobial activity that was not related to production of enterocin, H2O2 or organic acid. Twenty-five enterococci showed strong or moderate proteolytic activity towards beta-casein. Two isolates, BGPT1-10P and BGPT1-78, showed the most intense hydrolysis of alpha(s1)-, beta-, kappa-casein fractions, total casein as well as gelatin. Extracellular BGPT1-10P and BGPT1-78 proteinases have a molecular mass of about 29 kDa. Bacteriocin production and proteinase activity of natural isolates of enterococci may be of technological interest in dairy and meat-fermented products.",
publisher = "Springer, New York",
journal = "European Food Research and Technology",
title = "Evaluation of antimicrobial and proteolytic activity of enterococci isolated from fermented products",
pages = "70-63",
number = "1",
volume = "230",
doi = "10.1007/s00217-009-1137-6"
}

Veljović, K., Fira, Đ., Terzić-Vidojević, A., Abriouel, H., Galvez, A.,& Topisirović, L.. (2009). Evaluation of antimicrobial and proteolytic activity of enterococci isolated from fermented products. in European Food Research and Technology
Springer, New York., 230(1), 63-70.
https://doi.org/10.1007/s00217-009-1137-6

Veljović K, Fira Đ, Terzić-Vidojević A, Abriouel H, Galvez A, Topisirović L. Evaluation of antimicrobial and proteolytic activity of enterococci isolated from fermented products. in European Food Research and Technology. 2009;230(1):63-70.
doi:10.1007/s00217-009-1137-6 .

Veljović, Katarina, Fira, Đorđe, Terzić-Vidojević, Amarela, Abriouel, Hikmate, Galvez, Antonio, Topisirović, Ljubiša, "Evaluation of antimicrobial and proteolytic activity of enterococci isolated from fermented products" in European Food Research and Technology, 230, no. 1 (2009):63-70,
https://doi.org/10.1007/s00217-009-1137-6 . .

TY  - JOUR
AU  - Živković, Milica
AU  - Tolinački, Maja
AU  - Fira, Đorđe
AU  - Golić, Nataša
AU  - Topisirović, Ljubiša
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/346
AB  - Comparison of cell-wall-bound extracellular proteinases (CEPs) from Lactobacillus paracasei (LBP) ssp. paracasei natural isolates BGHN14, BGAR75 and BGAR76 with Lactococcus lactis (LCL) ssp. cremoris Wg2, in their action on alpha(S1)-, beta- and kappa-casein was done. The CEPs of LBP strains were able to degrade alpha(S1)- and beta-caseins and their caseinolytic specificity depended on the type of buffer used. These CEPs, compared with LCL Wg2, differ in four amino acid residues in small segments predicted to be involved in substrate binding. The most striking features of this comparison are the presence of Ala instead of Ser(329) and the presence of Thr instead of Asn(256) and Ala(299), in the subtilisin-like region of the CEP in LBP natural isolates. Additional conservative amino acid substitution Leu to Ile(364) was found.
PB  - Springer, Dordrecht
T2  - Folia Microbiologica
T1  - Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp paracasei
EP  - 194
IS  - 3
SP  - 188
VL  - 54
DO  - 10.1007/s12223-009-0029-2
ER  - 

@article{
author = "Živković, Milica and Tolinački, Maja and Fira, Đorđe and Golić, Nataša and Topisirović, Ljubiša",
year = "2009",
abstract = "Comparison of cell-wall-bound extracellular proteinases (CEPs) from Lactobacillus paracasei (LBP) ssp. paracasei natural isolates BGHN14, BGAR75 and BGAR76 with Lactococcus lactis (LCL) ssp. cremoris Wg2, in their action on alpha(S1)-, beta- and kappa-casein was done. The CEPs of LBP strains were able to degrade alpha(S1)- and beta-caseins and their caseinolytic specificity depended on the type of buffer used. These CEPs, compared with LCL Wg2, differ in four amino acid residues in small segments predicted to be involved in substrate binding. The most striking features of this comparison are the presence of Ala instead of Ser(329) and the presence of Thr instead of Asn(256) and Ala(299), in the subtilisin-like region of the CEP in LBP natural isolates. Additional conservative amino acid substitution Leu to Ile(364) was found.",
publisher = "Springer, Dordrecht",
journal = "Folia Microbiologica",
title = "Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp paracasei",
pages = "194-188",
number = "3",
volume = "54",
doi = "10.1007/s12223-009-0029-2"
}

Živković, M., Tolinački, M., Fira, Đ., Golić, N.,& Topisirović, L.. (2009). Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp paracasei. in Folia Microbiologica
Springer, Dordrecht., 54(3), 188-194.
https://doi.org/10.1007/s12223-009-0029-2

Živković M, Tolinački M, Fira Đ, Golić N, Topisirović L. Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp paracasei. in Folia Microbiologica. 2009;54(3):188-194.
doi:10.1007/s12223-009-0029-2 .

Živković, Milica, Tolinački, Maja, Fira, Đorđe, Golić, Nataša, Topisirović, Ljubiša, "Variation in specificity of the PrtP extracellular proteinases in Lactococcus lactis and Lactobacillus paracasei subsp paracasei" in Folia Microbiologica, 54, no. 3 (2009):188-194,
https://doi.org/10.1007/s12223-009-0029-2 . .