TY  - JOUR
AU  - Ilić, Dora S.
AU  - Dimkić, Ivica
AU  - Waisi, Hadi K.
AU  - Gkorezis, Panagiotis M.
AU  - Hamidović, Saud
AU  - Raičević, Vera
AU  - Lalević, Blažo
PY  - 2019
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4922
AB  - Hexavalent chromium, Cr(VI), one of the major pollutants from industrial facilities, is very toxic and harmful for human health and environmental quaky. Due to the lack of conventional methods, bioremediation was recommended as an environmentally friendly and effective technique. The aim of this paper was the isolation, identification and selection of the microorganisms which are capable of Cr(VI) reduction in vitro. Heavy metal concentration, detected in four soil samples, within and around the former bicycle factory Wog" (Republic . of Slovenia), was measured using the ICP-OES method. Bacteria were isolated and tested for chromium tolerance using LB agar supplemented with various Cr(VI) concentrations, whilst Cr(VI) reduction and bacterial growth was determined using the LB liquid medium. From 53 bacterial isolates, five of them showed a tolerance of 1000 mg/L of Cr(VI). Those five isolates showed the capability of growth under various Cr(VI) concentrations (50-1000 mg/L). Initial Cr(VI) concentrations ranging from 50 to 100 mg/L were completely reduced by four bacterial isolates, whilst 500 to 1000 mg/L by Bacillus safensis 342-9. Using 16S rDNA and tuf gene sequence analyses, isolates 270-9R and 342-9 were identified as Bacillus safensis, isolates 351-9 and 270-9C as Bacillus subtilis subsp. subtilis, and 212-9 as Bacillus thuringiensis. These results indicated that these bacteria may be promising tools for remediation of metal-polluted sites.
PB  - Savez hemijskih inženjera, Beograd
T2  - Chemical Industry and Chemical Engineering Quarterly / CICEQ
T1  - Reduction of hexavalent chromium by bacillusspp. Isolated from heavy metal-polluted soil
EP  - 258
IS  - 3
SP  - 247
VL  - 25
DO  - 10.2298/CICEQ180607003I
ER  - 

@article{
author = "Ilić, Dora S. and Dimkić, Ivica and Waisi, Hadi K. and Gkorezis, Panagiotis M. and Hamidović, Saud and Raičević, Vera and Lalević, Blažo",
year = "2019",
abstract = "Hexavalent chromium, Cr(VI), one of the major pollutants from industrial facilities, is very toxic and harmful for human health and environmental quaky. Due to the lack of conventional methods, bioremediation was recommended as an environmentally friendly and effective technique. The aim of this paper was the isolation, identification and selection of the microorganisms which are capable of Cr(VI) reduction in vitro. Heavy metal concentration, detected in four soil samples, within and around the former bicycle factory Wog" (Republic . of Slovenia), was measured using the ICP-OES method. Bacteria were isolated and tested for chromium tolerance using LB agar supplemented with various Cr(VI) concentrations, whilst Cr(VI) reduction and bacterial growth was determined using the LB liquid medium. From 53 bacterial isolates, five of them showed a tolerance of 1000 mg/L of Cr(VI). Those five isolates showed the capability of growth under various Cr(VI) concentrations (50-1000 mg/L). Initial Cr(VI) concentrations ranging from 50 to 100 mg/L were completely reduced by four bacterial isolates, whilst 500 to 1000 mg/L by Bacillus safensis 342-9. Using 16S rDNA and tuf gene sequence analyses, isolates 270-9R and 342-9 were identified as Bacillus safensis, isolates 351-9 and 270-9C as Bacillus subtilis subsp. subtilis, and 212-9 as Bacillus thuringiensis. These results indicated that these bacteria may be promising tools for remediation of metal-polluted sites.",
publisher = "Savez hemijskih inženjera, Beograd",
journal = "Chemical Industry and Chemical Engineering Quarterly / CICEQ",
title = "Reduction of hexavalent chromium by bacillusspp. Isolated from heavy metal-polluted soil",
pages = "258-247",
number = "3",
volume = "25",
doi = "10.2298/CICEQ180607003I"
}

Ilić, D. S., Dimkić, I., Waisi, H. K., Gkorezis, P. M., Hamidović, S., Raičević, V.,& Lalević, B.. (2019). Reduction of hexavalent chromium by bacillusspp. Isolated from heavy metal-polluted soil. in Chemical Industry and Chemical Engineering Quarterly / CICEQ
Savez hemijskih inženjera, Beograd., 25(3), 247-258.
https://doi.org/10.2298/CICEQ180607003I

Ilić DS, Dimkić I, Waisi HK, Gkorezis PM, Hamidović S, Raičević V, Lalević B. Reduction of hexavalent chromium by bacillusspp. Isolated from heavy metal-polluted soil. in Chemical Industry and Chemical Engineering Quarterly / CICEQ. 2019;25(3):247-258.
doi:10.2298/CICEQ180607003I .

Ilić, Dora S., Dimkić, Ivica, Waisi, Hadi K., Gkorezis, Panagiotis M., Hamidović, Saud, Raičević, Vera, Lalević, Blažo, "Reduction of hexavalent chromium by bacillusspp. Isolated from heavy metal-polluted soil" in Chemical Industry and Chemical Engineering Quarterly / CICEQ, 25, no. 3 (2019):247-258,
https://doi.org/10.2298/CICEQ180607003I . .

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 . .