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  - 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 . .