TY  - JOUR
AU  - Paunović, Dušanka D.
AU  - Mirković, Milica M.
AU  - Mirković, Nemanja
AU  - Tešević, Vele
AU  - Stanković Jeremić, Jovana M.
AU  - Todosijević, Marina
AU  - Radulović, Zorica T.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6379
AB  - The use of truffles in food is based mainly on the addition of artificial flavors, aiming to achieve an intense aroma in the products. As truffle is a natural product with nutritional and functional properties, it is important to find an optimal method for truffle storage. As the microbiota contribute to truffle aroma, the bacterial and yeast compositions in the rhizosphere and fruiting body of the truffle and the impact of different freezing methods on the volatile profile of the truffle Tuber aestivum during 90 days of the storage were determined. Bacteria and yeasts isolates were identified using 16s rRNA and 18s rRNA. The effect of freezing truffles at -20°C and -80°C with and without previous dipping in liquid N2 on the volatile compounds was observed using GC/MS. The results demonstrated that the isolated bacteria belonged to the phylum Proteobacteria, Firmicutes and Actinobacteria, and the identified species mainly belonged to Firmicutes, genus Bacillus sp. Isolated yeasts were identified as Cryptococcus sp., Debaromyces hanseinii, Candida fermentati and Rhodotorula mucilaginosa. The GC/MS analysis revealed that frozen truffle samples were richer in the compounds 2-butanone, 2-methyl-butanal, methanethiol and 2-butanol after freezing or during storage. The content of DMS, acetaldehyde, 3-octanone, ethanol, and 2-methyl-1-propanol significantly decreased immediately after freezing. Overall, the gained results indicated that freezing of truffles as a preservation method had profound effects on the volatile compounds, while previous dipping in liquid N2 showed no significant impact on the volatile profile of truffle Tuber aestivum. © 2023 University of Belgrade - Faculty of Agriculture. All Rights Reserved.
T2  - Journal of Agricultural Sciences
T1  - Serbian Black Truffle Tuber Aestivum: Microbiota and Effects of Different Freezing Regimes on Volatile Aroma Compounds during Storage
VL  - 68
IS  - 3
SP  - 329
EP  - 346
DO  - 10.2298/JAS2303329P
ER  - 

@article{
author = "Paunović, Dušanka D. and Mirković, Milica M. and Mirković, Nemanja and Tešević, Vele and Stanković Jeremić, Jovana M. and Todosijević, Marina and Radulović, Zorica T.",
year = "2023",
abstract = "The use of truffles in food is based mainly on the addition of artificial flavors, aiming to achieve an intense aroma in the products. As truffle is a natural product with nutritional and functional properties, it is important to find an optimal method for truffle storage. As the microbiota contribute to truffle aroma, the bacterial and yeast compositions in the rhizosphere and fruiting body of the truffle and the impact of different freezing methods on the volatile profile of the truffle Tuber aestivum during 90 days of the storage were determined. Bacteria and yeasts isolates were identified using 16s rRNA and 18s rRNA. The effect of freezing truffles at -20°C and -80°C with and without previous dipping in liquid N2 on the volatile compounds was observed using GC/MS. The results demonstrated that the isolated bacteria belonged to the phylum Proteobacteria, Firmicutes and Actinobacteria, and the identified species mainly belonged to Firmicutes, genus Bacillus sp. Isolated yeasts were identified as Cryptococcus sp., Debaromyces hanseinii, Candida fermentati and Rhodotorula mucilaginosa. The GC/MS analysis revealed that frozen truffle samples were richer in the compounds 2-butanone, 2-methyl-butanal, methanethiol and 2-butanol after freezing or during storage. The content of DMS, acetaldehyde, 3-octanone, ethanol, and 2-methyl-1-propanol significantly decreased immediately after freezing. Overall, the gained results indicated that freezing of truffles as a preservation method had profound effects on the volatile compounds, while previous dipping in liquid N2 showed no significant impact on the volatile profile of truffle Tuber aestivum. © 2023 University of Belgrade - Faculty of Agriculture. All Rights Reserved.",
journal = "Journal of Agricultural Sciences",
title = "Serbian Black Truffle Tuber Aestivum: Microbiota and Effects of Different Freezing Regimes on Volatile Aroma Compounds during Storage",
volume = "68",
number = "3",
pages = "329-346",
doi = "10.2298/JAS2303329P"
}

Paunović, D. D., Mirković, M. M., Mirković, N., Tešević, V., Stanković Jeremić, J. M., Todosijević, M.,& Radulović, Z. T.. (2023). Serbian Black Truffle Tuber Aestivum: Microbiota and Effects of Different Freezing Regimes on Volatile Aroma Compounds during Storage. in Journal of Agricultural Sciences, 68(3), 329-346.
https://doi.org/10.2298/JAS2303329P

Paunović DD, Mirković MM, Mirković N, Tešević V, Stanković Jeremić JM, Todosijević M, Radulović ZT. Serbian Black Truffle Tuber Aestivum: Microbiota and Effects of Different Freezing Regimes on Volatile Aroma Compounds during Storage. in Journal of Agricultural Sciences. 2023;68(3):329-346.
doi:10.2298/JAS2303329P .

Paunović, Dušanka D., Mirković, Milica M., Mirković, Nemanja, Tešević, Vele, Stanković Jeremić, Jovana M., Todosijević, Marina, Radulović, Zorica T., "Serbian Black Truffle Tuber Aestivum: Microbiota and Effects of Different Freezing Regimes on Volatile Aroma Compounds during Storage" in Journal of Agricultural Sciences, 68, no. 3 (2023):329-346,
https://doi.org/10.2298/JAS2303329P . .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1389172320303996
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4779
AB  - Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.
PB  - Elsevier
T2  - Journal of Bioscience and Bioengineering
T1  - Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants
VL  - 131
IS  - 3
SP  - 234
EP  - 240
DO  - 10.1016/j.jbiosc.2020.10.010
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2021",
abstract = "Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.",
publisher = "Elsevier",
journal = "Journal of Bioscience and Bioengineering",
title = "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants",
volume = "131",
number = "3",
pages = "234-240",
doi = "10.1016/j.jbiosc.2020.10.010"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2021). Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering
Elsevier., 131(3), 234-240.
https://doi.org/10.1016/j.jbiosc.2020.10.010

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering. 2021;131(3):234-240.
doi:10.1016/j.jbiosc.2020.10.010 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants" in Journal of Bioscience and Bioengineering, 131, no. 3 (2021):234-240,
https://doi.org/10.1016/j.jbiosc.2020.10.010 . .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4090
AB  - Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes
VL  - 334
SP  - 108851
DO  - 10.1016/j.ijfoodmicro.2020.108851
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
abstract = "Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes",
volume = "334",
pages = "108851",
doi = "10.1016/j.ijfoodmicro.2020.108851"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology
Elsevier., 334, 108851.
https://doi.org/10.1016/j.ijfoodmicro.2020.108851

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology. 2020;334:108851.
doi:10.1016/j.ijfoodmicro.2020.108851 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes" in International Journal of Food Microbiology, 334 (2020):108851,
https://doi.org/10.1016/j.ijfoodmicro.2020.108851 . .

TY  - DATA
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4091
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4091
ER  - 

@misc{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4091"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4091

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851" in International Journal of Food Microbiology (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

TY  - JOUR
AU  - Vukotić, Goran N.
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3298
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 in Microbiology
T2  - Frontiers in Microbiology
T1  - Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501
VL  - 10
IS  - APR
DO  - 10.3389/fmicb.2019.00874
ER  - 

@article{
author = "Vukotić, Goran N. and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
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 in Microbiology",
journal = "Frontiers in Microbiology",
title = "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501",
volume = "10",
number = "APR",
doi = "10.3389/fmicb.2019.00874"
}

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

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

Vukotić, Goran N., Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja S., Fira, Đorđe, Kojić, Milan O., "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501" in Frontiers in Microbiology, 10, no. APR (2019),
https://doi.org/10.3389/fmicb.2019.00874 . .

TY  - DATA
AU  - Vukotić, Goran N.
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3299
PB  - Frontiers in Microbiology
T2  - Frontiers in Microbiology
T1  - Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3299
ER  - 

@misc{
author = "Vukotić, Goran N. and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
year = "2019",
publisher = "Frontiers in Microbiology",
journal = "Frontiers in Microbiology",
title = "Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3299"
}

Vukotić, G. N., Polović, N., Mirković, N., Jovčić, B., Stanisavljević, N. S., Fira, Đ.,& Kojić, M. O.. (2019). Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874. in Frontiers in Microbiology
Frontiers in Microbiology..
https://hdl.handle.net/21.15107/rcub_cherry_3299

Vukotić GN, Polović N, Mirković N, Jovčić B, Stanisavljević NS, Fira Đ, Kojić MO. Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874. in Frontiers in Microbiology. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3299 .

Vukotić, Goran N., Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja S., Fira, Đorđe, Kojić, Milan O., "Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874" in Frontiers in Microbiology (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3299 .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2541
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
VL  - 83
IS  - 21
DO  - 10.1128/AEM.01519-17
ER  - 

@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
volume = "83",
number = "21",
doi = "10.1128/AEM.01519-17"
}

Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17

Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17 .

Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 . .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2998
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
VL  - 83
IS  - 21
DO  - 10.1128/AEM.01519-17
ER  - 

@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
volume = "83",
number = "21",
doi = "10.1128/AEM.01519-17"
}

Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17

Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17 .

Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 . .

TY  - DATA
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2999
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2999
ER  - 

@misc{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2999"
}

Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington..
https://hdl.handle.net/21.15107/rcub_cherry_2999

Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17. in Applied and Environmental Microbiology. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_2999 .

Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17" in Applied and Environmental Microbiology (2017),
https://hdl.handle.net/21.15107/rcub_cherry_2999 .

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Polović, Natalija
AU  - Vukotić, Goran N.
AU  - Jovčić, Branko
AU  - Miljković, Marija
AU  - Radulovic, Zorica
AU  - Diep, Dzung B.
AU  - Kojić, Milan O.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1908
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
VL  - 82
IS  - 8
SP  - 2555
EP  - 2562
DO  - 10.1128/AEM.03988-15
ER  - 

@article{
author = "Mirković, Nemanja and Polović, Natalija and Vukotić, Goran N. and Jovčić, Branko and Miljković, Marija and Radulovic, Zorica and Diep, Dzung B. and Kojić, Milan O.",
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",
volume = "82",
number = "8",
pages = "2555-2562",
doi = "10.1128/AEM.03988-15"
}

Mirković, N., Polović, N., Vukotić, G. N., Jovčić, B., Miljković, M., Radulovic, Z., Diep, D. B.,& Kojić, M. O.. (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 GN, Jovčić B, Miljković M, Radulovic Z, Diep DB, Kojić MO. 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 N., Jovčić, Branko, Miljković, Marija, Radulovic, Zorica, Diep, Dzung B., Kojić, Milan O., "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 . .