Vukotić, Goran N.

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32f2eaa2-3029-43d2-8f9a-3d8a86cc632e
  • Vukotić, Goran N. (5)
  • Vukotić, Goran (2)
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Author's Bibliography

Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501

Vukotić, Goran; Polović, Natalija; Mirković, Nemanja; Jovčić, Branko; Stanisavljević, Nemanja S.; Fira, Đorđe; Kojić, Milan O.

(Frontiers in Microbiology, 2019)

TY  - JOUR
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - http://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 and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3298",
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., 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.
Frontiers in Microbiology
Frontiers in Microbiology., 10(APR).
https://doi.org/10.3389/fmicb.2019.00874
Vukotić G, 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. Frontiers in Microbiology. 2019;10(APR)
Vukotić Goran, 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" Frontiers in Microbiology, 10, no. APR (2019),
https://doi.org/10.3389/fmicb.2019.00874 .
2
2
2

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

Vukotić, Goran; Polović, Natalija; Mirković, Nemanja; Jovčić, Branko; Stanisavljević, Nemanja S.; Fira, Đorđe; Kojić, Milan O.

(Frontiers in Microbiology, 2019)

TY  - BOOK
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - http://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
ER  - 
@book{
author = "Vukotić, Goran and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3299",
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"
}
Vukotić, G., 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.
Frontiers in Microbiology
Frontiers in Microbiology..
Vukotić G, 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. Frontiers in Microbiology. 2019;
Vukotić Goran, 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" Frontiers in Microbiology (2019)

In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?

Pešić, Mirjana B.; Milinčić, Danijel D.; Kostić, Aleksandar Ž.; Stanisavljević, Nemanja S.; Vukotić, Goran N.; Kojić, Milan O.; Gašić, Uroš M.; Barać, Miroljub B.; Stanojević, Slađana P.; Popović, Dušanka A.; Banjac, Nebojša R.; Tešić, Živoslav Lj.

(Elsevier, 2019)

TY  - JOUR
AU  - Pešić, Mirjana B.
AU  - Milinčić, Danijel D.
AU  - Kostić, Aleksandar Ž.
AU  - Stanisavljević, Nemanja S.
AU  - Vukotić, Goran N.
AU  - Kojić, Milan O.
AU  - Gašić, Uroš M.
AU  - Barać, Miroljub B.
AU  - Stanojević, Slađana P.
AU  - Popović, Dušanka A.
AU  - Banjac, Nebojša R.
AU  - Tešić, Živoslav Lj.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2843
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 [rad]+ 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
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?
VL  - 284
SP  - 28
EP  - 44
DO  - 10.1016/j.foodchem.2019.01.107
ER  - 
@article{
author = "Pešić, Mirjana B. and Milinčić, Danijel D. and Kostić, Aleksandar Ž. and Stanisavljević, Nemanja S. and Vukotić, Goran N. and Kojić, Milan O. and Gašić, Uroš M. and Barać, Miroljub B. and Stanojević, Slađana P. and Popović, Dušanka A. and Banjac, Nebojša R. and Tešić, Živoslav Lj.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2843",
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 [rad]+ 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",
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?",
volume = "284",
pages = "28-44",
doi = "10.1016/j.foodchem.2019.01.107"
}
Pešić, M. B., Milinčić, D. D., Kostić, A. Ž., Stanisavljević, N. S., Vukotić, G. N., Kojić, M. O., Gašić, U. M., Barać, M. B., Stanojević, S. P., Popović, D. A., Banjac, N. R.,& Tešić, Ž. Lj. (2019). In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?.
Food Chemistry
Elsevier., 284, 28-44.
https://doi.org/10.1016/j.foodchem.2019.01.107
Pešić MB, Milinčić DD, Kostić AŽ, Stanisavljević NS, Vukotić GN, Kojić MO, Gašić UM, Barać MB, Stanojević SP, Popović DA, Banjac NR, Tešić ŽL. In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?. Food Chemistry. 2019;284:28-44
Pešić Mirjana B., Milinčić Danijel D., Kostić Aleksandar Ž., Stanisavljević Nemanja S., Vukotić Goran N., Kojić Milan O., Gašić Uroš M., Barać Miroljub B., Stanojević Slađana P., Popović Dušanka A., Banjac Nebojša R., Tešić Živoslav Lj., "In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?" Food Chemistry, 284 (2019):28-44,
https://doi.org/10.1016/j.foodchem.2019.01.107 .
31
16
27

Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107

Pešić, Mirjana B.; Milinčić, Danijel D.; Kostić, Aleksandar Ž.; Stanisavljević, Nemanja S.; Vukotić, Goran N.; Kojić, Milan O.; Gašić, Uroš M.; Barać, Miroljub B.; Stanojević, Slađana P.; Popović, Dušanka A.; Banjac, Nebojša R.; Tešić, Živoslav Lj.

(2019)

TY  - BOOK
AU  - Pešić, Mirjana B.
AU  - Milinčić, Danijel D.
AU  - Kostić, Aleksandar Ž.
AU  - Stanisavljević, Nemanja S.
AU  - Vukotić, Goran N.
AU  - Kojić, Milan O.
AU  - Gašić, Uroš M.
AU  - Barać, Miroljub B.
AU  - Stanojević, Slađana P.
AU  - Popović, Dušanka A.
AU  - Banjac, Nebojša R.
AU  - Tešić, Živoslav Lj.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2856
T2  - Food Chemistry
T1  - Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107
ER  - 
@book{
author = "Pešić, Mirjana B. and Milinčić, Danijel D. and Kostić, Aleksandar Ž. and Stanisavljević, Nemanja S. and Vukotić, Goran N. and Kojić, Milan O. and Gašić, Uroš M. and Barać, Miroljub B. and Stanojević, Slađana P. and Popović, Dušanka A. and Banjac, Nebojša R. and Tešić, Živoslav Lj.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2856",
journal = "Food Chemistry",
title = "Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107"
}
Pešić, M. B., Milinčić, D. D., Kostić, A. Ž., Stanisavljević, N. S., Vukotić, G. N., Kojić, M. O., Gašić, U. M., Barać, M. B., Stanojević, S. P., Popović, D. A., Banjac, N. R.,& Tešić, Ž. Lj. (2019). Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107.
Food Chemistry.
Pešić MB, Milinčić DD, Kostić AŽ, Stanisavljević NS, Vukotić GN, Kojić MO, Gašić UM, Barać MB, Stanojević SP, Popović DA, Banjac NR, Tešić ŽL. Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107. Food Chemistry. 2019;
Pešić Mirjana B., Milinčić Danijel D., Kostić Aleksandar Ž., Stanisavljević Nemanja S., Vukotić Goran N., Kojić Milan O., Gašić Uroš M., Barać Miroljub B., Stanojević Slađana P., Popović Dušanka A., Banjac Nebojša R., Tešić Živoslav Lj., "Supplementary data for the article: Pešić, M. B.; Milinčić, D. D.; Kostić, A.; Stanisavljević, N. S.; Vukotić, G. N.; Kojić, M. O.; Gašić, U. M.; Barać, M. B.; Stanojević, S. P.; Popović, D. A.; et al. In Vitro Digestion of Meat- and Cereal-Based Food Matrix Enriched with Grape Extracts: How Are Polyphenol Composition, Bioaccessibility and Antioxidant Activity Affected? Food Chem. 2019, 284, 28–44. https://doi.org/10.1016/j.foodchem.2019.01.107" Food Chemistry (2019)

In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?

Pešić, Mirjana B.; Milinčić, Danijel D.; Kostić, Aleksandar Ž.; Stanisavljević, Nemanja S.; Vukotić, Goran N.; Kojić, Milan O.; Gašić, Uroš M.; Barać, Miroljub B.; Stanojević, Slađana P.; Popović, Dušanka A.; Banjac, Nebojša R.; Tešić, Živoslav Lj.

(Elsevier, 2019)

TY  - JOUR
AU  - Pešić, Mirjana B.
AU  - Milinčić, Danijel D.
AU  - Kostić, Aleksandar Ž.
AU  - Stanisavljević, Nemanja S.
AU  - Vukotić, Goran N.
AU  - Kojić, Milan O.
AU  - Gašić, Uroš M.
AU  - Barać, Miroljub B.
AU  - Stanojević, Slađana P.
AU  - Popović, Dušanka A.
AU  - Banjac, Nebojša R.
AU  - Tešić, Živoslav Lj.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2867
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 [rad]+ 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
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?
VL  - 284
SP  - 28
EP  - 44
DO  - 10.1016/j.foodchem.2019.01.107
ER  - 
@article{
author = "Pešić, Mirjana B. and Milinčić, Danijel D. and Kostić, Aleksandar Ž. and Stanisavljević, Nemanja S. and Vukotić, Goran N. and Kojić, Milan O. and Gašić, Uroš M. and Barać, Miroljub B. and Stanojević, Slađana P. and Popović, Dušanka A. and Banjac, Nebojša R. and Tešić, Živoslav Lj.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2867",
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 [rad]+ 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",
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?",
volume = "284",
pages = "28-44",
doi = "10.1016/j.foodchem.2019.01.107"
}
Pešić, M. B., Milinčić, D. D., Kostić, A. Ž., Stanisavljević, N. S., Vukotić, G. N., Kojić, M. O., Gašić, U. M., Barać, M. B., Stanojević, S. P., Popović, D. A., Banjac, N. R.,& Tešić, Ž. Lj. (2019). In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?.
Food Chemistry
Elsevier., 284, 28-44.
https://doi.org/10.1016/j.foodchem.2019.01.107
Pešić MB, Milinčić DD, Kostić AŽ, Stanisavljević NS, Vukotić GN, Kojić MO, Gašić UM, Barać MB, Stanojević SP, Popović DA, Banjac NR, Tešić ŽL. In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?. Food Chemistry. 2019;284:28-44
Pešić Mirjana B., Milinčić Danijel D., Kostić Aleksandar Ž., Stanisavljević Nemanja S., Vukotić Goran N., Kojić Milan O., Gašić Uroš M., Barać Miroljub B., Stanojević Slađana P., Popović Dušanka A., Banjac Nebojša R., Tešić Živoslav Lj., "In vitro digestion of meat- and cereal-based food matrix enriched with grape extracts: How are polyphenol composition, bioaccessibility and antioxidant activity affected?" Food Chemistry, 284 (2019):28-44,
https://doi.org/10.1016/j.foodchem.2019.01.107 .
31
16
27

Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic

Mirković, Nemanja; Polović, Natalija; Vukotić, Goran N.; Jovčić, Branko; Miljković, Marija; Radulovic, Zorica; Diep, Dzung B.; Kojić, Milan O.

(Amer Soc Microbiology, Washington, 2016)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1908",
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.
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. Applied and Environmental Microbiology. 2016;82(8):2555-2562
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" Applied and Environmental Microbiology, 82, no. 8 (2016):2555-2562,
https://doi.org/10.1128/AEM.03988-15 .
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Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria

Stanisavljević, Nemanja S.; Vukotić, Goran N.; Pastor, Ferenc; Suznjevic, Desanka; Jovanović, Živko S.; Strahinic, Ivana D.; Fira, Dorde A.; Radovic, Svetlana S.

(Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd, 2015)

TY  - JOUR
AU  - Stanisavljević, Nemanja S.
AU  - Vukotić, Goran N.
AU  - Pastor, Ferenc
AU  - Suznjevic, Desanka
AU  - Jovanović, Živko S.
AU  - Strahinic, Ivana D.
AU  - Fira, Dorde A.
AU  - Radovic, Svetlana S.
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1961
AB  - Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria
VL  - 67
IS  - 3
SP  - 1033
EP  - 1042
DO  - 10.2298/ABS150130066S
ER  - 
@article{
author = "Stanisavljević, Nemanja S. and Vukotić, Goran N. and Pastor, Ferenc and Suznjevic, Desanka and Jovanović, Živko S. and Strahinic, Ivana D. and Fira, Dorde A. and Radovic, Svetlana S.",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1961",
abstract = "Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria",
volume = "67",
number = "3",
pages = "1033-1042",
doi = "10.2298/ABS150130066S"
}
Stanisavljević, N. S., Vukotić, G. N., Pastor, F., Suznjevic, D., Jovanović, Ž. S., Strahinic, I. D., Fira, D. A.,& Radovic, S. S. (2015). Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria.
Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 67(3), 1033-1042.
https://doi.org/10.2298/ABS150130066S
Stanisavljević NS, Vukotić GN, Pastor F, Suznjevic D, Jovanović ŽS, Strahinic ID, Fira DA, Radovic SS. Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria. Archives of biological sciences. 2015;67(3):1033-1042
Stanisavljević Nemanja S., Vukotić Goran N., Pastor Ferenc, Suznjevic Desanka, Jovanović Živko S., Strahinic Ivana D., Fira Dorde A., Radovic Svetlana S., "Antioxidant Activity of Pea Protein Hydrolysates Produced by Batch Fermentation with Lactic Acid Bacteria" Archives of biological sciences, 67, no. 3 (2015):1033-1042,
https://doi.org/10.2298/ABS150130066S .
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