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149 results on '"Jovcic, Branko"'

4. CONTROL OF LISTERIA MONOCYTOGENES AND STAPHYLOCOCCUS AUREUS IN MEAT AND MEAT PRODUCTS BY CELL-FREE SUPERNATANT OF BREVIBACILLUS LATEROSPORUS BGSP7 AND BGSP9.

Author

Mirkovic, Nemanja, Radulovic, Zorica, Jovcic, Branko, Stanisavljevic, Nemanja, Kojic, Milan, Oz, Fatih, Proestos, Charalampos, Heinz, Volker, and Tomasevic, Igor

Abstract

The presence of pathogens in food has increased awareness of food safety, but it also causes large economic losses. Fresh meat and meat products contain a sufficient quantity of proteins, lipids, water, and a favorable pH that stimulates the growth of various microorganisms, including pathogens. The aim of this study was to investigate the efficacy of Brevibacillus laterosporus BGSP7 (CFS-BGSP7) and BGSP9 (CFS-BGSP9) cellfree supernatants in the control of Listeria monocytogenes and Staphylococcus aureus in raw meat and meat products. Raw meat and meat products were sliced and then aseptically treated by immersion for 2 minutes into solutions containing: i) CFS-BGSP7; ii) CFS-BGSP9; iii) no treatment. The samples were then artificially contaminated with: Group I - L. monocytogenes (~4 log cfu g-1); Group II - S. aureus LMM322 (~4 log cfu g-1). Each sample was individually aseptically vacuum-packed and stored at 4°C for 8 weeks. The number of surviving bacteria in the samples were analyzed immediately after contamination with L. monocytogenes and S. aureus and at regular time-intervals: after 1, 3, 5 and 8 weeks of storage at 4°C. Meat samples treated with CFS-BGSP7 and CFS-SP9 showed a significant decrease in the cell counts of L. monocytogenes and S. aureus. When meat samples treated with CFS-BGSP7 and CFS-BGSP9 are compared, the results show a more intense reduction rate of both L. monocytogenes and S. aureus in all samples treated with CFS-BGSP7. [ABSTRACT FROM AUTHOR]

Published
2024
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15. Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants

Author

Malesevic, Milka, primary, Gardijan, Lazar, additional, Miljkovic, Marija, additional, O'Connor, Paula M, additional, Mirkovic, Nemanja, additional, Jovcic, Branko, additional, Cotter, Paul D, additional, Jovanovic, Goran, additional, and Kojic, Milan, additional

Published
2023
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34. Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials

Author

Miljkovic, Marija, primary, Jovanovic, Sofija, additional, O’Connor, Paula M., additional, Mirkovic, Nemanja, additional, Jovcic, Branko, additional, Filipic, Brankica, additional, Dinic, Miroslav, additional, Studholme, David John, additional, Fira, Djordje, additional, Cotter, Paul D., additional, and Kojic, Milan, additional

Published
2019
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36. Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp. lactis BGKP1

Author

Kojic Milan, Jovcic Branko, Strahinic Ivana, Begovic Jelena, Lozo Jelena, Veljovic Katarina, and Topisirovic Ljubisa

Subjects
Microbiology, QR1-502
Abstract

Abstract Background Aggregation may play a main role in the adhesion of bacteria to the gastrointestinal epithelium and their colonization ability, as well as in probiotic effects through co-aggregation with intestinal pathogens and their subsequent removal. The aggregation phenomenon in lactococci is directly associated with the sex factor and lactose plasmid co-integration event or duplication of the cell wall spanning (CWS) domain of PrtP proteinase. Results Lactococcus lactis subsp. lactis BGKP1 was isolated from artisanal semi-hard homemade cheese and selected due to its strong auto-aggregation phenotype. Subsequently, non-aggregating derivative (Agg-) of BGKP1, designated as BGKP1-20, was isolated, too. Comparative analysis of cell surface proteins of BGKP1 and derivative BGKP1-20 revealed a protein of approximately 200 kDa only in the parental strain BGKP1. The gene involved in aggregation (aggL) was mapped on plasmid pKP1 (16.2 kb), cloned and expressed in homologous and heterologous lactococci and enterococci. This novel lactococcal aggregation protein was shown to be sufficient for cell aggregation in all tested hosts. In addition to the aggL gene, six more ORFs involved in replication (repB and repX), restriction and modification (hsdS), transposition (tnp) and possible interaction with mucin (mbpL) were also located on plasmid pKP1. Conclusion AggL is a new protein belonging to the collagen-binding superfamily of proteins and is sufficient for cell aggregation in lactococci.

Published
2011
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