TY  - JOUR
AU  - Mirković, Nemanja
AU  - Obradović, Mina
AU  - O’Connor, Paula M.
AU  - Filipić, Brankica
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan
PY  - 2021
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5908
AB  - Screening for producers of potent antimicrobial peptides, resulted in the isolation of Bacillus cereus BGNM1 with strong antimicrobial activity against Listeria monocytogenes. Genome sequence analysis revealed that BGNM1 contains the gene cluster associated with the production of the lantibiotic, thusin, previously identified in B. thuringiensis. Purification of the antimicrobial activity confirmed that strain BGMN1 produces thusin. Both thusin sensitive and resistant strains were detected among clinical isolates of Streptococcus agalactiae. Random mutagenesis of a thusin sensitive strain, S. agalactiae B782, was performed in an attempt to identify the receptor protein for thusin. Three independent thusin resistant mutants were selected and their complete genomes sequenced. Comparative sequence analysis of these mutants with the WT strain revealed that duplication of a region encoding a 79 amino acids repeat in a C-protein α-antigen was a common difference, suggesting it to be responsible for increased resistance to thusin. Since induced thusin resistant mutants showed higher level of resistance than the naturally resistant B761 strain, complete genome sequencing of strain B761 was performed to check the integrity of the C-protein α-antigen-encoding gene. This analysis revealed that this gene is deleted in B761, providing further evidence that this protein promotes interaction of the thusin with receptor.
PB  - Springer Science and Business Media Deutschland GmbH
T2  - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
T1  - C-protein α-antigen modulates the lantibiotic thusin resistance in Streptococcus agalactiae
EP  - 1607
IS  - 10
SP  - 1595
VL  - 114
DO  - 10.1007/s10482-021-01626-3
ER  - 

@article{
author = "Mirković, Nemanja and Obradović, Mina and O’Connor, Paula M. and Filipić, Brankica and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan",
year = "2021",
abstract = "Screening for producers of potent antimicrobial peptides, resulted in the isolation of Bacillus cereus BGNM1 with strong antimicrobial activity against Listeria monocytogenes. Genome sequence analysis revealed that BGNM1 contains the gene cluster associated with the production of the lantibiotic, thusin, previously identified in B. thuringiensis. Purification of the antimicrobial activity confirmed that strain BGMN1 produces thusin. Both thusin sensitive and resistant strains were detected among clinical isolates of Streptococcus agalactiae. Random mutagenesis of a thusin sensitive strain, S. agalactiae B782, was performed in an attempt to identify the receptor protein for thusin. Three independent thusin resistant mutants were selected and their complete genomes sequenced. Comparative sequence analysis of these mutants with the WT strain revealed that duplication of a region encoding a 79 amino acids repeat in a C-protein α-antigen was a common difference, suggesting it to be responsible for increased resistance to thusin. Since induced thusin resistant mutants showed higher level of resistance than the naturally resistant B761 strain, complete genome sequencing of strain B761 was performed to check the integrity of the C-protein α-antigen-encoding gene. This analysis revealed that this gene is deleted in B761, providing further evidence that this protein promotes interaction of the thusin with receptor.",
publisher = "Springer Science and Business Media Deutschland GmbH",
journal = "Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology",
title = "C-protein α-antigen modulates the lantibiotic thusin resistance in Streptococcus agalactiae",
pages = "1607-1595",
number = "10",
volume = "114",
doi = "10.1007/s10482-021-01626-3"
}

Mirković, N., Obradović, M., O’Connor, P. M., Filipić, B., Jovčić, B., Cotter, P. D.,& Kojić, M.. (2021). C-protein α-antigen modulates the lantibiotic thusin resistance in Streptococcus agalactiae. in Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
Springer Science and Business Media Deutschland GmbH., 114(10), 1595-1607.
https://doi.org/10.1007/s10482-021-01626-3

Mirković N, Obradović M, O’Connor PM, Filipić B, Jovčić B, Cotter PD, Kojić M. C-protein α-antigen modulates the lantibiotic thusin resistance in Streptococcus agalactiae. in Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology. 2021;114(10):1595-1607.
doi:10.1007/s10482-021-01626-3 .

Mirković, Nemanja, Obradović, Mina, O’Connor, Paula M., Filipić, Brankica, Jovčić, Branko, Cotter, Paul D., Kojić, Milan, "C-protein α-antigen modulates the lantibiotic thusin resistance in Streptococcus agalactiae" in Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology, 114, no. 10 (2021):1595-1607,
https://doi.org/10.1007/s10482-021-01626-3 . .

TY  - JOUR
AU  - Milincić, Danijel D.
AU  - Vojinović, Uroš
AU  - Kostić, Aleksandar
AU  - Pešić, Mirjana
AU  - Špirović-Trifunović, Bojana
AU  - Brkić, Dragica
AU  - Stević, Milan
AU  - Kojić, Milan
AU  - Stanisavljević, Nemanja S.
PY  - 2020
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5371
AB  - The aim of this study was to investigate the bioaccessibility of pesticide residues in blueberries (com-mercial and sample from controlled field trial) from Serbia, involving the presence of a complex food matrix and to assess the potential risk to human health. The presence of nine active substances (azox-ystrobin, boscalid, fludioxonil, cyprodinil, pyrimethanil, pyridaben, pyriproxyfen, acetamiprid and thia-metoxam) in initial blueberry samples was determined in concentration range from 5.15 mu g/kg for thiametoxam to 187 mu g/kg for azoxystrobin. Clothianidin, metabolite of thiametoxam, was not detected in any blueberry sample. However, after in vitro digestion, the content of initially detected pesticides residues was significantly decreased or it was below limit of quantification resulting in the total bio-accessibility of about 15%. Azoxystrobin, pyrimethanil and fludioxonil was quantified in digestive juice at concentrations which were about 81%, 37% and 10% less than the inital concentration, respectively. The presence of food matrix during digestion of blueberries even more severely reduced concentration of pesticide residues (total bioaccessibility was about 7%) compared to digestion without the food matrix. Only azoxystrobin was quantified after digestion with food matrix in concentration of 27 mu g/kg in sample from controlled field trial and detected in two commercial samples but below the limit of quantification. Furthermore, chronic risk assessment indicated that risk is acceptable for the health of different human subpopulation groups. The current study on pesticides residues, most commonly applied on blueberries, provides for the first time an insight into their bioaccessibility under conditions that mimic physiological environment of human digestive tract.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Chemosphere
T1  - In vitro assessment of pesticide residues bioaccessibility in conventionally grown blueberries as affected by complex food matrix
VL  - 252
DO  - 10.1016/j.chemosphere.2020.126568
ER  - 

@article{
author = "Milincić, Danijel D. and Vojinović, Uroš and Kostić, Aleksandar and Pešić, Mirjana and Špirović-Trifunović, Bojana and Brkić, Dragica and Stević, Milan and Kojić, Milan and Stanisavljević, Nemanja S.",
year = "2020",
abstract = "The aim of this study was to investigate the bioaccessibility of pesticide residues in blueberries (com-mercial and sample from controlled field trial) from Serbia, involving the presence of a complex food matrix and to assess the potential risk to human health. The presence of nine active substances (azox-ystrobin, boscalid, fludioxonil, cyprodinil, pyrimethanil, pyridaben, pyriproxyfen, acetamiprid and thia-metoxam) in initial blueberry samples was determined in concentration range from 5.15 mu g/kg for thiametoxam to 187 mu g/kg for azoxystrobin. Clothianidin, metabolite of thiametoxam, was not detected in any blueberry sample. However, after in vitro digestion, the content of initially detected pesticides residues was significantly decreased or it was below limit of quantification resulting in the total bio-accessibility of about 15%. Azoxystrobin, pyrimethanil and fludioxonil was quantified in digestive juice at concentrations which were about 81%, 37% and 10% less than the inital concentration, respectively. The presence of food matrix during digestion of blueberries even more severely reduced concentration of pesticide residues (total bioaccessibility was about 7%) compared to digestion without the food matrix. Only azoxystrobin was quantified after digestion with food matrix in concentration of 27 mu g/kg in sample from controlled field trial and detected in two commercial samples but below the limit of quantification. Furthermore, chronic risk assessment indicated that risk is acceptable for the health of different human subpopulation groups. The current study on pesticides residues, most commonly applied on blueberries, provides for the first time an insight into their bioaccessibility under conditions that mimic physiological environment of human digestive tract.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Chemosphere",
title = "In vitro assessment of pesticide residues bioaccessibility in conventionally grown blueberries as affected by complex food matrix",
volume = "252",
doi = "10.1016/j.chemosphere.2020.126568"
}

Milincić, D. D., Vojinović, U., Kostić, A., Pešić, M., Špirović-Trifunović, B., Brkić, D., Stević, M., Kojić, M.,& Stanisavljević, N. S.. (2020). In vitro assessment of pesticide residues bioaccessibility in conventionally grown blueberries as affected by complex food matrix. in Chemosphere
Pergamon-Elsevier Science Ltd, Oxford., 252.
https://doi.org/10.1016/j.chemosphere.2020.126568

Milincić DD, Vojinović U, Kostić A, Pešić M, Špirović-Trifunović B, Brkić D, Stević M, Kojić M, Stanisavljević NS. In vitro assessment of pesticide residues bioaccessibility in conventionally grown blueberries as affected by complex food matrix. in Chemosphere. 2020;252.
doi:10.1016/j.chemosphere.2020.126568 .

Milincić, Danijel D., Vojinović, Uroš, Kostić, Aleksandar, Pešić, Mirjana, Špirović-Trifunović, Bojana, Brkić, Dragica, Stević, Milan, Kojić, Milan, Stanisavljević, Nemanja S., "In vitro assessment of pesticide residues bioaccessibility in conventionally grown blueberries as affected by complex food matrix" in Chemosphere, 252 (2020),
https://doi.org/10.1016/j.chemosphere.2020.126568 . .

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Kulas, Jelena
AU  - Miloradović, Zorana
AU  - Miljković, Marija
AU  - Tucović, Dina
AU  - Miočinović, Jelena
AU  - Jovcić, Branko
AU  - Mirkov, Ivana
AU  - Kojić, Milan
PY  - 2020
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5345
AB  - In last two decades, there has been a strong trend in the application of lactic acid bacteria as adjunctive cultures to control growth of spoilage and pathogenic bacteria in food. One of the most important properties that contribute to the application of these bacteria is the production of antimicrobial molecules. Lactococcus lactis subsp. lactis BGBU1-4, isolated from traditional brined cheese, produces thermostable bacteriocin named lactolisterin BU, with broad spectrum of activity against spoilage bacteria and foodborne pathogens. In this study, effect of strain BGBU1-4, as adjunct culture, on the numbers of Listeria monocytogenes ATCC19111 and Staphylococcus aureus LMM322 in artificially contaminated Quark-type, soft acid coagulated cheese, was examined. In addition, we analyzed influence of BGBU1-4 on chemical and sensory properties of the cheese, as well as immunological response of Albino oxford rats fed with Quark-type of cheese made using BGBU1-4 as adjunct culture. Results of this study revealed antibacterial potential of strain BGBU1-4 against L. monocytogenes ATCC19111 and S. aureus LMM322 in Quark-type cheese during 21 days of storage at 4 degrees C. Also, it was noticed the ability of BGBU1-4 to control the spontaneously grown yeasts and molds. Chemical composition and pH values of cheese containing BGBU1-4 were unchanged in comparison to control. The sensory quality scores showed that there was difference between cheese with and without adjunct culture in terms of flavor and oral texture, while for the odor and appearance no differences between two cheese variants were scored. Results of the immunological response of Albino rats fed with Quark-type cheese containing BGBU1-4 indicate absence of systematic inflammation. However, increased pro-inflammatory cytokines content (IL-1 beta, IL-6, IL-17) in intestine of rats fed with cheese containing BGBU1-4, concomitantly with unchanged anti-inflammatory cytokines suggests disruption of gut homeostasis and inflammation in this tissue. The changes caused by BGBU1-4 are reversible, system returns into homeostasis seven days after cessation of feeding with cheese containing BGBU1-4.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Control
T1  - Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats
VL  - 111
DO  - 10.1016/j.foodcont.2019.107076
ER  - 

@article{
author = "Mirković, Nemanja and Kulas, Jelena and Miloradović, Zorana and Miljković, Marija and Tucović, Dina and Miočinović, Jelena and Jovcić, Branko and Mirkov, Ivana and Kojić, Milan",
year = "2020",
abstract = "In last two decades, there has been a strong trend in the application of lactic acid bacteria as adjunctive cultures to control growth of spoilage and pathogenic bacteria in food. One of the most important properties that contribute to the application of these bacteria is the production of antimicrobial molecules. Lactococcus lactis subsp. lactis BGBU1-4, isolated from traditional brined cheese, produces thermostable bacteriocin named lactolisterin BU, with broad spectrum of activity against spoilage bacteria and foodborne pathogens. In this study, effect of strain BGBU1-4, as adjunct culture, on the numbers of Listeria monocytogenes ATCC19111 and Staphylococcus aureus LMM322 in artificially contaminated Quark-type, soft acid coagulated cheese, was examined. In addition, we analyzed influence of BGBU1-4 on chemical and sensory properties of the cheese, as well as immunological response of Albino oxford rats fed with Quark-type of cheese made using BGBU1-4 as adjunct culture. Results of this study revealed antibacterial potential of strain BGBU1-4 against L. monocytogenes ATCC19111 and S. aureus LMM322 in Quark-type cheese during 21 days of storage at 4 degrees C. Also, it was noticed the ability of BGBU1-4 to control the spontaneously grown yeasts and molds. Chemical composition and pH values of cheese containing BGBU1-4 were unchanged in comparison to control. The sensory quality scores showed that there was difference between cheese with and without adjunct culture in terms of flavor and oral texture, while for the odor and appearance no differences between two cheese variants were scored. Results of the immunological response of Albino rats fed with Quark-type cheese containing BGBU1-4 indicate absence of systematic inflammation. However, increased pro-inflammatory cytokines content (IL-1 beta, IL-6, IL-17) in intestine of rats fed with cheese containing BGBU1-4, concomitantly with unchanged anti-inflammatory cytokines suggests disruption of gut homeostasis and inflammation in this tissue. The changes caused by BGBU1-4 are reversible, system returns into homeostasis seven days after cessation of feeding with cheese containing BGBU1-4.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Control",
title = "Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats",
volume = "111",
doi = "10.1016/j.foodcont.2019.107076"
}

Mirković, N., Kulas, J., Miloradović, Z., Miljković, M., Tucović, D., Miočinović, J., Jovcić, B., Mirkov, I.,& Kojić, M.. (2020). Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats. in Food Control
Elsevier Sci Ltd, Oxford., 111.
https://doi.org/10.1016/j.foodcont.2019.107076

Mirković N, Kulas J, Miloradović Z, Miljković M, Tucović D, Miočinović J, Jovcić B, Mirkov I, Kojić M. Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats. in Food Control. 2020;111.
doi:10.1016/j.foodcont.2019.107076 .

Mirković, Nemanja, Kulas, Jelena, Miloradović, Zorana, Miljković, Marija, Tucović, Dina, Miočinović, Jelena, Jovcić, Branko, Mirkov, Ivana, Kojić, Milan, "Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats" in Food Control, 111 (2020),
https://doi.org/10.1016/j.foodcont.2019.107076 . .

TY  - JOUR
AU  - Klisurić, Olivera
AU  - Armaković, Sanja J.
AU  - Armaković, Stevan
AU  - Marković, Sanja
AU  - Todorović, Tamara R.
AU  - Portalone, Gustavo
AU  - Novović, Katarina
AU  - Lozo, Jelena
AU  - Filipović, Nenad
PY  - 2020
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5361
AB  - In this work pharmaceutical application of focused library of six quinoline-based chalcogensemicarbazones (QBCs) was tested through determination of their antimicrobial activity against twenty-eight Gram-negative and Gram-positive strains from different origin. Pharmacokinetic properties have been assessed by the analysis of frequently employed drug likeness parameters. Computational study has been complemented with calculation of their global and local reactive properties, within the framework of density functional theory (DFT). Among other information, DFT calculations helped us to locate the most reactive sites of investigated QBCs and to identify their sensitivity towards the oxidation.
PB  - Elsevier, Amsterdam
T2  - Journal of Molecular Structure
T1  - Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones
VL  - 1203
DO  - 10.1016/j.molstruc.2019.127482
ER  - 

@article{
author = "Klisurić, Olivera and Armaković, Sanja J. and Armaković, Stevan and Marković, Sanja and Todorović, Tamara R. and Portalone, Gustavo and Novović, Katarina and Lozo, Jelena and Filipović, Nenad",
year = "2020",
abstract = "In this work pharmaceutical application of focused library of six quinoline-based chalcogensemicarbazones (QBCs) was tested through determination of their antimicrobial activity against twenty-eight Gram-negative and Gram-positive strains from different origin. Pharmacokinetic properties have been assessed by the analysis of frequently employed drug likeness parameters. Computational study has been complemented with calculation of their global and local reactive properties, within the framework of density functional theory (DFT). Among other information, DFT calculations helped us to locate the most reactive sites of investigated QBCs and to identify their sensitivity towards the oxidation.",
publisher = "Elsevier, Amsterdam",
journal = "Journal of Molecular Structure",
title = "Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones",
volume = "1203",
doi = "10.1016/j.molstruc.2019.127482"
}

Klisurić, O., Armaković, S. J., Armaković, S., Marković, S., Todorović, T. R., Portalone, G., Novović, K., Lozo, J.,& Filipović, N.. (2020). Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones. in Journal of Molecular Structure
Elsevier, Amsterdam., 1203.
https://doi.org/10.1016/j.molstruc.2019.127482

Klisurić O, Armaković SJ, Armaković S, Marković S, Todorović TR, Portalone G, Novović K, Lozo J, Filipović N. Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones. in Journal of Molecular Structure. 2020;1203.
doi:10.1016/j.molstruc.2019.127482 .

Klisurić, Olivera, Armaković, Sanja J., Armaković, Stevan, Marković, Sanja, Todorović, Tamara R., Portalone, Gustavo, Novović, Katarina, Lozo, Jelena, Filipović, Nenad, "Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones" in Journal of Molecular Structure, 1203 (2020),
https://doi.org/10.1016/j.molstruc.2019.127482 . .

TY  - JOUR
AU  - Pešić, Mirjana
AU  - Milincić, Danijel D.
AU  - Kostić, Aleksandar
AU  - Stanisavljević, Nemanja S.
AU  - Vukotić, Goran
AU  - Kojić, Milan
AU  - Gašić, Uroš M.
AU  - Barać, Miroljub
AU  - Stanojević, Sladjana
AU  - Popović, Dušanka A.
AU  - Banjac, Nebojša
AU  - Tešić, Živoslav
PY  - 2019
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5034
AB  - The aim of this study was to evaluate the effect of enriching a complex food matrix (FM) with grape extracts on polyphenol content, composition, bioaccessibility and antioxidant activity during digestion. The grape extracts and FM were separately tested under the same conditions as controls. The FM by itself contains a significant amount of phenolic acids and flavonols, influencing the final recovery of polyphenols from grape extracts. The FM significantly increased the total recovery of polyphenols after digestion of grape seed extracts compared to those digested without the FM; however, a low recovery of proantocyanidins and total flavonoids was observed. Digestive fluids and FM compounds significantly increased the total polyphenol content of grape digests and significantly contributed to their ABTS(center dot+) scavenging activity and ferrous-ion-chelating capacity. The present study suggested that enrichment of meat-and cereal-based products with grape polyphenol extracts could be a good strategy to formulate a healthier diet.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?
EP  - 44
SP  - 28
VL  - 284
DO  - 10.1016/j.foodchem.2019.01.107
ER  - 

@article{
author = "Pešić, Mirjana and Milincić, Danijel D. and Kostić, Aleksandar and Stanisavljević, Nemanja S. and Vukotić, Goran and Kojić, Milan and Gašić, Uroš M. and Barać, Miroljub and Stanojević, Sladjana and Popović, Dušanka A. and Banjac, Nebojša and Tešić, Živoslav",
year = "2019",
abstract = "The aim of this study was to evaluate the effect of enriching a complex food matrix (FM) with grape extracts on polyphenol content, composition, bioaccessibility and antioxidant activity during digestion. The grape extracts and FM were separately tested under the same conditions as controls. The FM by itself contains a significant amount of phenolic acids and flavonols, influencing the final recovery of polyphenols from grape extracts. The FM significantly increased the total recovery of polyphenols after digestion of grape seed extracts compared to those digested without the FM; however, a low recovery of proantocyanidins and total flavonoids was observed. Digestive fluids and FM compounds significantly increased the total polyphenol content of grape digests and significantly contributed to their ABTS(center dot+) scavenging activity and ferrous-ion-chelating capacity. The present study suggested that enrichment of meat-and cereal-based products with grape polyphenol extracts could be a good strategy to formulate a healthier diet.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?",
pages = "44-28",
volume = "284",
doi = "10.1016/j.foodchem.2019.01.107"
}

Pešić, M., Milincić, D. D., Kostić, A., Stanisavljević, N. S., Vukotić, G., Kojić, M., Gašić, U. M., Barać, M., Stanojević, S., Popović, D. A., Banjac, N.,& Tešić, Ž.. (2019). In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?. in Food Chemistry
Elsevier Sci Ltd, Oxford., 284, 28-44.
https://doi.org/10.1016/j.foodchem.2019.01.107

Pešić M, Milincić DD, Kostić A, Stanisavljević NS, Vukotić G, Kojić M, Gašić UM, Barać M, Stanojević S, Popović DA, Banjac N, Tešić Ž. In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?. in Food Chemistry. 2019;284:28-44.
doi:10.1016/j.foodchem.2019.01.107 .

Pešić, Mirjana, Milincić, Danijel D., Kostić, Aleksandar, Stanisavljević, Nemanja S., Vukotić, Goran, Kojić, Milan, Gašić, Uroš M., Barać, Miroljub, Stanojević, Sladjana, Popović, Dušanka A., Banjac, Nebojša, Tešić, Živoslav, "In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?" in Food Chemistry, 284 (2019):28-44,
https://doi.org/10.1016/j.foodchem.2019.01.107 . .

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Polović, Natalija
AU  - Vukotić, Goran
AU  - Jovcić, Branko
AU  - Miljković, Marija
AU  - Radulović, Zorica
AU  - Diep, Dzung B.
AU  - Kojić, Milan
PY  - 2016
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4208
AB  - Bacteriocin producers normally possess dedicated immunity systems to protect themselves from their own bacteriocins. Lactococcus lactis strains LMG2081 and BGBM50 are known as lactococcin G producers. However, BGBM50 was sensitive to LMG2081, which indicated that LMG2081 might produce additional bacteriocins that are not present in BGBM50. Therefore, whole-genome sequencing of the two strains was performed, and a lantibiotic operon (called lctLMG) was identified in LMG2081 but not in BGBM50. The lctLMG operon contains six open reading frames; the first three genes, lmgA, lmgM, and lmgT, are involved in the biosynthesis and export of bacteriocin, while the other three genes, lmgF, lmgE, and lmgG, are involved in lantibiotic immunity. Mutational analysis confirmed that the lctLMG operon is responsible for the additional antimicrobial activity. Specifically, site-directed mutation within this operon rendered LMG2081 inactive toward BGBM50. Subsequent purification and electrospray ionization-time of flight mass spectrometric analysis confirmed that the lantibiotic bacteriocin called lacticin LMG is exported as a 25-amino-acid peptide. Lacticin LMG is highly similar to the lacticin 481 group. It is interesting that a bacteriocin producer produces two different classes of bacteriocins, whose operons are located in the chromosome and a plasmid.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic
EP  - 2562
IS  - 8
SP  - 2555
VL  - 82
DO  - 10.1128/AEM.03988-15
ER  - 

@article{
author = "Mirković, Nemanja and Polović, Natalija and Vukotić, Goran and Jovcić, Branko and Miljković, Marija and Radulović, Zorica and Diep, Dzung B. and Kojić, Milan",
year = "2016",
abstract = "Bacteriocin producers normally possess dedicated immunity systems to protect themselves from their own bacteriocins. Lactococcus lactis strains LMG2081 and BGBM50 are known as lactococcin G producers. However, BGBM50 was sensitive to LMG2081, which indicated that LMG2081 might produce additional bacteriocins that are not present in BGBM50. Therefore, whole-genome sequencing of the two strains was performed, and a lantibiotic operon (called lctLMG) was identified in LMG2081 but not in BGBM50. The lctLMG operon contains six open reading frames; the first three genes, lmgA, lmgM, and lmgT, are involved in the biosynthesis and export of bacteriocin, while the other three genes, lmgF, lmgE, and lmgG, are involved in lantibiotic immunity. Mutational analysis confirmed that the lctLMG operon is responsible for the additional antimicrobial activity. Specifically, site-directed mutation within this operon rendered LMG2081 inactive toward BGBM50. Subsequent purification and electrospray ionization-time of flight mass spectrometric analysis confirmed that the lantibiotic bacteriocin called lacticin LMG is exported as a 25-amino-acid peptide. Lacticin LMG is highly similar to the lacticin 481 group. It is interesting that a bacteriocin producer produces two different classes of bacteriocins, whose operons are located in the chromosome and a plasmid.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic",
pages = "2562-2555",
number = "8",
volume = "82",
doi = "10.1128/AEM.03988-15"
}

Mirković, N., Polović, N., Vukotić, G., Jovcić, B., Miljković, M., Radulović, Z., Diep, D. B.,& Kojić, M.. (2016). Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 82(8), 2555-2562.
https://doi.org/10.1128/AEM.03988-15

Mirković N, Polović N, Vukotić G, Jovcić B, Miljković M, Radulović Z, Diep DB, Kojić M. Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic. in Applied and Environmental Microbiology. 2016;82(8):2555-2562.
doi:10.1128/AEM.03988-15 .

Mirković, Nemanja, Polović, Natalija, Vukotić, Goran, Jovcić, Branko, Miljković, Marija, Radulović, Zorica, Diep, Dzung B., Kojić, Milan, "Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic" in Applied and Environmental Microbiology, 82, no. 8 (2016):2555-2562,
https://doi.org/10.1128/AEM.03988-15 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Uzelac, Gordana
AU  - Mirković, Nemanja
AU  - Devescovi, Giulia
AU  - Diep, Dzung B.
AU  - Venturi, Vittorio
AU  - Kojić, Milan
PY  - 2016
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4029
AB  - The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor
EP  - 5374
IS  - 17
SP  - 5364
VL  - 82
DO  - 10.1128/AEM.01293-16
ER  - 

@article{
author = "Miljković, Marija and Uzelac, Gordana and Mirković, Nemanja and Devescovi, Giulia and Diep, Dzung B. and Venturi, Vittorio and Kojić, Milan",
year = "2016",
abstract = "The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor",
pages = "5374-5364",
number = "17",
volume = "82",
doi = "10.1128/AEM.01293-16"
}

Miljković, M., Uzelac, G., Mirković, N., Devescovi, G., Diep, D. B., Venturi, V.,& Kojić, M.. (2016). LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 82(17), 5364-5374.
https://doi.org/10.1128/AEM.01293-16

Miljković M, Uzelac G, Mirković N, Devescovi G, Diep DB, Venturi V, Kojić M. LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology. 2016;82(17):5364-5374.
doi:10.1128/AEM.01293-16 .

Miljković, Marija, Uzelac, Gordana, Mirković, Nemanja, Devescovi, Giulia, Diep, Dzung B., Venturi, Vittorio, Kojić, Milan, "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor" in Applied and Environmental Microbiology, 82, no. 17 (2016):5364-5374,
https://doi.org/10.1128/AEM.01293-16 . .

TY  - JOUR
AU  - Uzelac, Gordana
AU  - Miljković, Marija
AU  - Lozo, Jelena
AU  - Radulović, Zorica
AU  - Tosić, Nataša
AU  - Kojić, Milan
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3689
AB  - The production of LsbB, leaderless class II bacteriocin, is encoded by genes (lsbB and lmrB) located on plasmid pMN5 in Lactococcus lactis BGMN1-5. Heterologous expression of the lsbB gene using the pAZIL vector (pAZIL-lsbB) in L. lactis subsp. cremoris MG7284 resulted in a significant reduction (more than 30 times) of bacteriocin LsbB expression. Subcloning and deletion experiments with plasmid pMN5 revealed that full expression of LsbB requires the presence of a complete transcription terminator located downstream of the lsbB gene. RNA stability analysis revealed that the presence of a transcription terminator increased the RNA stability by three times and the expression of LsbB by 30 times. The study of the influence of transcription terminator on the expression of other bacteriocin genes (lcnB, for lactococcin B production) indicated that this translational terminator likely functions in a lsbB-specific manner rather than in a general manner.
PB  - Elsevier Gmbh, Urban & Fischer Verlag, Jena
T2  - Microbiological Research
T1  - Expression of bacteriocin LsbB is dependent on a transcription terminator
EP  - 53
SP  - 45
VL  - 179
DO  - 10.1016/j.micres.2015.06.011
ER  - 

@article{
author = "Uzelac, Gordana and Miljković, Marija and Lozo, Jelena and Radulović, Zorica and Tosić, Nataša and Kojić, Milan",
year = "2015",
abstract = "The production of LsbB, leaderless class II bacteriocin, is encoded by genes (lsbB and lmrB) located on plasmid pMN5 in Lactococcus lactis BGMN1-5. Heterologous expression of the lsbB gene using the pAZIL vector (pAZIL-lsbB) in L. lactis subsp. cremoris MG7284 resulted in a significant reduction (more than 30 times) of bacteriocin LsbB expression. Subcloning and deletion experiments with plasmid pMN5 revealed that full expression of LsbB requires the presence of a complete transcription terminator located downstream of the lsbB gene. RNA stability analysis revealed that the presence of a transcription terminator increased the RNA stability by three times and the expression of LsbB by 30 times. The study of the influence of transcription terminator on the expression of other bacteriocin genes (lcnB, for lactococcin B production) indicated that this translational terminator likely functions in a lsbB-specific manner rather than in a general manner.",
publisher = "Elsevier Gmbh, Urban & Fischer Verlag, Jena",
journal = "Microbiological Research",
title = "Expression of bacteriocin LsbB is dependent on a transcription terminator",
pages = "53-45",
volume = "179",
doi = "10.1016/j.micres.2015.06.011"
}

Uzelac, G., Miljković, M., Lozo, J., Radulović, Z., Tosić, N.,& Kojić, M.. (2015). Expression of bacteriocin LsbB is dependent on a transcription terminator. in Microbiological Research
Elsevier Gmbh, Urban & Fischer Verlag, Jena., 179, 45-53.
https://doi.org/10.1016/j.micres.2015.06.011

Uzelac G, Miljković M, Lozo J, Radulović Z, Tosić N, Kojić M. Expression of bacteriocin LsbB is dependent on a transcription terminator. in Microbiological Research. 2015;179:45-53.
doi:10.1016/j.micres.2015.06.011 .

Uzelac, Gordana, Miljković, Marija, Lozo, Jelena, Radulović, Zorica, Tosić, Nataša, Kojić, Milan, "Expression of bacteriocin LsbB is dependent on a transcription terminator" in Microbiological Research, 179 (2015):45-53,
https://doi.org/10.1016/j.micres.2015.06.011 . .

TY  - JOUR
AU  - Vukotić, Goran
AU  - Mirković, Nemanja
AU  - Jovcić, Branko
AU  - Miljković, Marija
AU  - Strahinić, Ivana
AU  - Fira, Djordje
AU  - Radulović, Zorica
AU  - Kojić, Milan
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3817
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 Jovcić, Branko and Miljković, Marija and Strahinić, Ivana and Fira, Djordje 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., Jovcić, B., Miljković, M., Strahinić, I., Fira, D., 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, Jovcić B, Miljković M, Strahinić I, Fira D, 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, Jovcić, Branko, Miljković, Marija, Strahinić, Ivana, Fira, Djordje, 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  - Mirković, Nemanja
AU  - Radulović, Zorica
AU  - Uzelac, Gordana
AU  - Lozo, Jelena
AU  - Obradović, Dragojlo
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3845
AB  - Lactococcus locus ssp. lactis BGBM50, a producer of lactococcin G and aggregation-promoting factor, was isolated from selected lactic acid bacteria taken from semi-hard cheese traditionally produced in the village Zanjic, Montenegro. Strain BGBM50 harbours a number of plasmids of different sizes. Plasmid curing experiments showed that genes for bacteriocin production are located on pBM140, a plasmid 140 kb in length. PCR analysis with primers specific for lactococcin Q and G genes gave fragment of the expected size. In addition, after plasmid curing of strain BGBM50, different derivatives with altered phenotypes were obtained, among them BGBM50-34 strain, which retained bacteriocin synthesis but had enhanced aggregation ability.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain
EP  - 242
IS  - 2
SP  - 237
VL  - 53
DO  - 10.17113/ftb.53.02.15.3846
ER  - 

@article{
author = "Mirković, Nemanja and Radulović, Zorica and Uzelac, Gordana and Lozo, Jelena and Obradović, Dragojlo and Topisirović, Ljubiša and Kojić, Milan",
year = "2015",
abstract = "Lactococcus locus ssp. lactis BGBM50, a producer of lactococcin G and aggregation-promoting factor, was isolated from selected lactic acid bacteria taken from semi-hard cheese traditionally produced in the village Zanjic, Montenegro. Strain BGBM50 harbours a number of plasmids of different sizes. Plasmid curing experiments showed that genes for bacteriocin production are located on pBM140, a plasmid 140 kb in length. PCR analysis with primers specific for lactococcin Q and G genes gave fragment of the expected size. In addition, after plasmid curing of strain BGBM50, different derivatives with altered phenotypes were obtained, among them BGBM50-34 strain, which retained bacteriocin synthesis but had enhanced aggregation ability.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain",
pages = "242-237",
number = "2",
volume = "53",
doi = "10.17113/ftb.53.02.15.3846"
}

Mirković, N., Radulović, Z., Uzelac, G., Lozo, J., Obradović, D., Topisirović, L.,& Kojić, M.. (2015). Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain. in Food Technology and Biotechnology
University of Zagreb., 53(2), 237-242.
https://doi.org/10.17113/ftb.53.02.15.3846

Mirković N, Radulović Z, Uzelac G, Lozo J, Obradović D, Topisirović L, Kojić M. Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain. in Food Technology and Biotechnology. 2015;53(2):237-242.
doi:10.17113/ftb.53.02.15.3846 .

Mirković, Nemanja, Radulović, Zorica, Uzelac, Gordana, Lozo, Jelena, Obradović, Dragojlo, Topisirović, Ljubiša, Kojić, Milan, "Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain" in Food Technology and Biotechnology, 53, no. 2 (2015):237-242,
https://doi.org/10.17113/ftb.53.02.15.3846 . .

TY  - JOUR
AU  - Novović, Katarina
AU  - Filipić, B.
AU  - Veljović, Katarina
AU  - Begović, J.
AU  - Mirković, Nemanja
AU  - Jovcić, B.
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3798
AB  - New Delhi metallo-beta-lactamase-1 (NDM-1) will soon become the most commonly isolated and distributed metallo-beta-lactamase worldwide due to its rapid international dissemination and its ability to be expressed by numerous Gram-negative pathogens. NDM-positive bacteria pose a significant public health threat in the Indian subcontinent and the Balkans, which have been designated as endemic regions. Our study was focused on urban rivers, a lake and springheads as a potential source of NDM-1-producing strains in Serbia, but also as a source of other metallo-beta-lactamases and extended-spectrum beta-lactamase (ESBL) producing bacteria. A total of 69 beta-lactam resistant isolates, belonging to 12 bacterial genera, were collected from 8 out of 10 different locations in Belgrade, of which the most were from a popular recreational site, Ada Ciganlija Lake. Phenotypic tests revealed 7 (10.14%) ESBL-producing isolates and 39 (56.52%) isolates resistant to imipenem, of which 32 were positive for metallo-beta-lactamase (MBL) production. PCR and sequencing revealed the presence of genetic determinants for SHV (3 isolates), DHA-1 (1 isolate) and CMY-2 (1 isolate) beta-lactamases. However, we did not detect any NDM-1-producing strains (previously described cases of NDM-1 from Serbia were limited to Belgrade), so we propose that Serbian NDM-1 is in fact a transplant and a nosocomial, rather than an environmental, issue and that Serbia is not an endemic region for NDM-1.
PB  - Elsevier, Amsterdam
T2  - Science of the Total Environment
T1  - Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned
EP  - 398
SP  - 393
VL  - 511
DO  - 10.1016/j.scitotenv.2014.12.072
ER  - 

@article{
author = "Novović, Katarina and Filipić, B. and Veljović, Katarina and Begović, J. and Mirković, Nemanja and Jovcić, B.",
year = "2015",
abstract = "New Delhi metallo-beta-lactamase-1 (NDM-1) will soon become the most commonly isolated and distributed metallo-beta-lactamase worldwide due to its rapid international dissemination and its ability to be expressed by numerous Gram-negative pathogens. NDM-positive bacteria pose a significant public health threat in the Indian subcontinent and the Balkans, which have been designated as endemic regions. Our study was focused on urban rivers, a lake and springheads as a potential source of NDM-1-producing strains in Serbia, but also as a source of other metallo-beta-lactamases and extended-spectrum beta-lactamase (ESBL) producing bacteria. A total of 69 beta-lactam resistant isolates, belonging to 12 bacterial genera, were collected from 8 out of 10 different locations in Belgrade, of which the most were from a popular recreational site, Ada Ciganlija Lake. Phenotypic tests revealed 7 (10.14%) ESBL-producing isolates and 39 (56.52%) isolates resistant to imipenem, of which 32 were positive for metallo-beta-lactamase (MBL) production. PCR and sequencing revealed the presence of genetic determinants for SHV (3 isolates), DHA-1 (1 isolate) and CMY-2 (1 isolate) beta-lactamases. However, we did not detect any NDM-1-producing strains (previously described cases of NDM-1 from Serbia were limited to Belgrade), so we propose that Serbian NDM-1 is in fact a transplant and a nosocomial, rather than an environmental, issue and that Serbia is not an endemic region for NDM-1.",
publisher = "Elsevier, Amsterdam",
journal = "Science of the Total Environment",
title = "Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned",
pages = "398-393",
volume = "511",
doi = "10.1016/j.scitotenv.2014.12.072"
}

Novović, K., Filipić, B., Veljović, K., Begović, J., Mirković, N.,& Jovcić, B.. (2015). Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned. in Science of the Total Environment
Elsevier, Amsterdam., 511, 393-398.
https://doi.org/10.1016/j.scitotenv.2014.12.072

Novović K, Filipić B, Veljović K, Begović J, Mirković N, Jovcić B. Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned. in Science of the Total Environment. 2015;511:393-398.
doi:10.1016/j.scitotenv.2014.12.072 .

Novović, Katarina, Filipić, B., Veljović, Katarina, Begović, J., Mirković, Nemanja, Jovcić, B., "Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned" in Science of the Total Environment, 511 (2015):393-398,
https://doi.org/10.1016/j.scitotenv.2014.12.072 . .

TY  - JOUR
AU  - Terzić-Vidojević, Amarela
AU  - Tolinacki, Maja
AU  - Nikolić, Milica
AU  - Veljović, Katarina
AU  - Jovanović, Snežana
AU  - Maćej, Ognjen
AU  - Topisirović, Ljubiša
PY  - 2013
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3131
AB  - The aim of this study is the isolation, characterization and identification of autochthonous lactic acid bacteria (LAB) from artisanal Vlasina raw goat's milk cheese for the selection of potential starter cultures. Soft white Vlasina cheese was manufactured at a household on the Stara Planina Mountain using traditional techniques without starter cultures. One hundred and forty nine LAB isolates were collected from two samples of Vlasina cheese, designated as BGVL2 (5 days old) and BGVL2a (15 days old). The population of LAB in the cheese samples was characterized by phenotype-based assays and presumptively identified using repetitive element palindromic polymerase chain reaction (rep-PCR) with the primer (GTG)(5). Results were confirmed by 16S rDNA sequencing. Among the BGVL2 isolates (56), the most numerous LAB species were Leuconostoc pseudomesenteroides (27) and Lactococcus lactis (26). In 15-day-old BGVL2a (93 isolates), Lactobacillus plantarum (33), Enterococcus durans (26) and Pediococcus pentosaceus (14) were predominant. Lc. lactis ssp. lactis BGVL2-8 showed good acidification ability and the ability to produce antimicrobial compounds, Lb. plantarum BGVL2a-18 had good proteolytic ability and produced exo-polysaccharides, while BGVL2-29 and BGVL2-63, which belonged to the species Ln. pseudomesenteroides, utilized citrate and produced diacetyl and acetoin. They appeared to be suitable candidates for inclusion in the starter culture. This study contributed to the understanding of the role of autochthonous LAB in the quality of artisanal cheese and the possibility of using the selected LAB as potential starter cultures for cheese making under controlled conditions.
PB  - Faculty Food Technology Biotechnology, Zagreb
T2  - Food Technology and Biotechnology
T1  - Artisanal Vlasina Raw Goat's Milk Cheese: Evaluation and Selection of Autochthonous Lactic Acid Bacteria as Starter Cultures
EP  - 563
IS  - 4
SP  - 554
VL  - 51
UR  - https://hdl.handle.net/21.15107/rcub_agrospace_3131
ER  - 

@article{
author = "Terzić-Vidojević, Amarela and Tolinacki, Maja and Nikolić, Milica and Veljović, Katarina and Jovanović, Snežana and Maćej, Ognjen and Topisirović, Ljubiša",
year = "2013",
abstract = "The aim of this study is the isolation, characterization and identification of autochthonous lactic acid bacteria (LAB) from artisanal Vlasina raw goat's milk cheese for the selection of potential starter cultures. Soft white Vlasina cheese was manufactured at a household on the Stara Planina Mountain using traditional techniques without starter cultures. One hundred and forty nine LAB isolates were collected from two samples of Vlasina cheese, designated as BGVL2 (5 days old) and BGVL2a (15 days old). The population of LAB in the cheese samples was characterized by phenotype-based assays and presumptively identified using repetitive element palindromic polymerase chain reaction (rep-PCR) with the primer (GTG)(5). Results were confirmed by 16S rDNA sequencing. Among the BGVL2 isolates (56), the most numerous LAB species were Leuconostoc pseudomesenteroides (27) and Lactococcus lactis (26). In 15-day-old BGVL2a (93 isolates), Lactobacillus plantarum (33), Enterococcus durans (26) and Pediococcus pentosaceus (14) were predominant. Lc. lactis ssp. lactis BGVL2-8 showed good acidification ability and the ability to produce antimicrobial compounds, Lb. plantarum BGVL2a-18 had good proteolytic ability and produced exo-polysaccharides, while BGVL2-29 and BGVL2-63, which belonged to the species Ln. pseudomesenteroides, utilized citrate and produced diacetyl and acetoin. They appeared to be suitable candidates for inclusion in the starter culture. This study contributed to the understanding of the role of autochthonous LAB in the quality of artisanal cheese and the possibility of using the selected LAB as potential starter cultures for cheese making under controlled conditions.",
publisher = "Faculty Food Technology Biotechnology, Zagreb",
journal = "Food Technology and Biotechnology",
title = "Artisanal Vlasina Raw Goat's Milk Cheese: Evaluation and Selection of Autochthonous Lactic Acid Bacteria as Starter Cultures",
pages = "563-554",
number = "4",
volume = "51",
url = "https://hdl.handle.net/21.15107/rcub_agrospace_3131"
}

Terzić-Vidojević, A., Tolinacki, M., Nikolić, M., Veljović, K., Jovanović, S., Maćej, O.,& Topisirović, L.. (2013). Artisanal Vlasina Raw Goat's Milk Cheese: Evaluation and Selection of Autochthonous Lactic Acid Bacteria as Starter Cultures. in Food Technology and Biotechnology
Faculty Food Technology Biotechnology, Zagreb., 51(4), 554-563.
https://hdl.handle.net/21.15107/rcub_agrospace_3131

Terzić-Vidojević A, Tolinacki M, Nikolić M, Veljović K, Jovanović S, Maćej O, Topisirović L. Artisanal Vlasina Raw Goat's Milk Cheese: Evaluation and Selection of Autochthonous Lactic Acid Bacteria as Starter Cultures. in Food Technology and Biotechnology. 2013;51(4):554-563.
https://hdl.handle.net/21.15107/rcub_agrospace_3131 .

Terzić-Vidojević, Amarela, Tolinacki, Maja, Nikolić, Milica, Veljović, Katarina, Jovanović, Snežana, Maćej, Ognjen, Topisirović, Ljubiša, "Artisanal Vlasina Raw Goat's Milk Cheese: Evaluation and Selection of Autochthonous Lactic Acid Bacteria as Starter Cultures" in Food Technology and Biotechnology, 51, no. 4 (2013):554-563,
https://hdl.handle.net/21.15107/rcub_agrospace_3131 .