TY  - JOUR
AU  - Medić, Ana
AU  - Stojanović, Ksenija A.
AU  - Izrael-Živković, Lidija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka D.
AU  - Kazazić, Saša
AU  - Karadžić, Ivanka M.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3346
AB  - The Pseudomonas aeruginosa san ai strain was investigated for its capability to degrade the 2,6-di-tert-butylphenol (2,6-DTBP) plastic additive, a hazardous and toxic substance for aquatic life. This investigation was performed under different parameter values: 2,6-DTBP concentration, inoculum size, pH, and temperature. The GC-MS study showed that P. aeruginosa efficiently degraded 2,6-DTBP in the pH range of 5-8 at higher temperatures. Under exposure to 2,6-DTBP concentrations of 2, 10, and 100 mg L-1, the strain degraded by 100, 100, and 85%, respectively, for 7 days. Crude enzyme preparation from the biomass of P. aeruginosa san ai showed higher efficiency in 2,6-DTBP removal than that shown by whole microbial cells. Gene encoding for the enzymes involved in the degradation of aromatic compounds in P. aeruginosa san ai was identified. To complement the genomic data, a comparative proteomic study of P. aeruginosa san ai grown on 2,6-DTBP or sunflower oil was conducted by means of nanoLC-MS/MS. The presence of aromatic substances resulted in the upregulation of aromatic ring cleavage enzymes, whose activity was confirmed by enzymatic tests; therefore, it could be concluded that 2,6-DTBP might be degraded by ortho-ring cleavage. A comparative proteomics study of P. aeruginosa san ai indicated that the core molecular responses to aromatic substances can be summarized as the upregulation of proteins responsible for amino acid metabolism with emphasized glutamate metabolism and energy production with upregulated enzymes of glyoxylate bypass. P. aeruginosa san ai has a high capacity to efficiently degrade aromatic compounds, and therefore its whole cells or enzymes could be used in the treatment of contaminated areas.
T2  - RSC Advances
T1  - A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-: Tert -butylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai
VL  - 9
IS  - 41
SP  - 23696
EP  - 23710
DO  - 10.1039/C9RA04298A
ER  - 

@article{
author = "Medić, Ana and Stojanović, Ksenija A. and Izrael-Živković, Lidija and Beškoski, Vladimir and Lončarević, Branka D. and Kazazić, Saša and Karadžić, Ivanka M.",
year = "2019",
abstract = "The Pseudomonas aeruginosa san ai strain was investigated for its capability to degrade the 2,6-di-tert-butylphenol (2,6-DTBP) plastic additive, a hazardous and toxic substance for aquatic life. This investigation was performed under different parameter values: 2,6-DTBP concentration, inoculum size, pH, and temperature. The GC-MS study showed that P. aeruginosa efficiently degraded 2,6-DTBP in the pH range of 5-8 at higher temperatures. Under exposure to 2,6-DTBP concentrations of 2, 10, and 100 mg L-1, the strain degraded by 100, 100, and 85%, respectively, for 7 days. Crude enzyme preparation from the biomass of P. aeruginosa san ai showed higher efficiency in 2,6-DTBP removal than that shown by whole microbial cells. Gene encoding for the enzymes involved in the degradation of aromatic compounds in P. aeruginosa san ai was identified. To complement the genomic data, a comparative proteomic study of P. aeruginosa san ai grown on 2,6-DTBP or sunflower oil was conducted by means of nanoLC-MS/MS. The presence of aromatic substances resulted in the upregulation of aromatic ring cleavage enzymes, whose activity was confirmed by enzymatic tests; therefore, it could be concluded that 2,6-DTBP might be degraded by ortho-ring cleavage. A comparative proteomics study of P. aeruginosa san ai indicated that the core molecular responses to aromatic substances can be summarized as the upregulation of proteins responsible for amino acid metabolism with emphasized glutamate metabolism and energy production with upregulated enzymes of glyoxylate bypass. P. aeruginosa san ai has a high capacity to efficiently degrade aromatic compounds, and therefore its whole cells or enzymes could be used in the treatment of contaminated areas.",
journal = "RSC Advances",
title = "A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-: Tert -butylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai",
volume = "9",
number = "41",
pages = "23696-23710",
doi = "10.1039/C9RA04298A"
}

Medić, A., Stojanović, K. A., Izrael-Živković, L., Beškoski, V., Lončarević, B. D., Kazazić, S.,& Karadžić, I. M.. (2019). A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-: Tert -butylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai. in RSC Advances, 9(41), 23696-23710.
https://doi.org/10.1039/C9RA04298A

Medić A, Stojanović KA, Izrael-Živković L, Beškoski V, Lončarević BD, Kazazić S, Karadžić IM. A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-: Tert -butylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai. in RSC Advances. 2019;9(41):23696-23710.
doi:10.1039/C9RA04298A .

Medić, Ana, Stojanović, Ksenija A., Izrael-Živković, Lidija, Beškoski, Vladimir, Lončarević, Branka D., Kazazić, Saša, Karadžić, Ivanka M., "A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-: Tert -butylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai" in RSC Advances, 9, no. 41 (2019):23696-23710,
https://doi.org/10.1039/C9RA04298A . .

TY  - DATA
AU  - Medić, Ana
AU  - Stojanović, Ksenija A.
AU  - Izrael-Živković, Lidija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka D.
AU  - Kazazić, Saša
AU  - Karadžić, Ivanka M.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3347
T2  - RSC Advances
T1  - Supplementary data for the article: Medić, A.; Stojanović, K.; Izrael-Živković, L.; Beškoski, V.; Lončarević, B.; Kazazić, S.; Karadžić, I. A Comprehensive Study of Conditions of the Biodegradation of a Plastic Additive 2,6-Di-: Tert -Butylphenol and Proteomic Changes in the Degrader Pseudomonas Aeruginosa San Ai. RSC Advances 2019, 9 (41), 23696–23710. https://doi.org/10.1039/c9ra04298a
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3347
ER  - 

@misc{
author = "Medić, Ana and Stojanović, Ksenija A. and Izrael-Živković, Lidija and Beškoski, Vladimir and Lončarević, Branka D. and Kazazić, Saša and Karadžić, Ivanka M.",
year = "2019",
journal = "RSC Advances",
title = "Supplementary data for the article: Medić, A.; Stojanović, K.; Izrael-Živković, L.; Beškoski, V.; Lončarević, B.; Kazazić, S.; Karadžić, I. A Comprehensive Study of Conditions of the Biodegradation of a Plastic Additive 2,6-Di-: Tert -Butylphenol and Proteomic Changes in the Degrader Pseudomonas Aeruginosa San Ai. RSC Advances 2019, 9 (41), 23696–23710. https://doi.org/10.1039/c9ra04298a",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3347"
}

Medić, A., Stojanović, K. A., Izrael-Živković, L., Beškoski, V., Lončarević, B. D., Kazazić, S.,& Karadžić, I. M.. (2019). Supplementary data for the article: Medić, A.; Stojanović, K.; Izrael-Živković, L.; Beškoski, V.; Lončarević, B.; Kazazić, S.; Karadžić, I. A Comprehensive Study of Conditions of the Biodegradation of a Plastic Additive 2,6-Di-: Tert -Butylphenol and Proteomic Changes in the Degrader Pseudomonas Aeruginosa San Ai. RSC Advances 2019, 9 (41), 23696–23710. https://doi.org/10.1039/c9ra04298a. in RSC Advances.
https://hdl.handle.net/21.15107/rcub_cherry_3347

Medić A, Stojanović KA, Izrael-Živković L, Beškoski V, Lončarević BD, Kazazić S, Karadžić IM. Supplementary data for the article: Medić, A.; Stojanović, K.; Izrael-Živković, L.; Beškoski, V.; Lončarević, B.; Kazazić, S.; Karadžić, I. A Comprehensive Study of Conditions of the Biodegradation of a Plastic Additive 2,6-Di-: Tert -Butylphenol and Proteomic Changes in the Degrader Pseudomonas Aeruginosa San Ai. RSC Advances 2019, 9 (41), 23696–23710. https://doi.org/10.1039/c9ra04298a. in RSC Advances. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3347 .

Medić, Ana, Stojanović, Ksenija A., Izrael-Živković, Lidija, Beškoski, Vladimir, Lončarević, Branka D., Kazazić, Saša, Karadžić, Ivanka M., "Supplementary data for the article: Medić, A.; Stojanović, K.; Izrael-Živković, L.; Beškoski, V.; Lončarević, B.; Kazazić, S.; Karadžić, I. A Comprehensive Study of Conditions of the Biodegradation of a Plastic Additive 2,6-Di-: Tert -Butylphenol and Proteomic Changes in the Degrader Pseudomonas Aeruginosa San Ai. RSC Advances 2019, 9 (41), 23696–23710. https://doi.org/10.1039/c9ra04298a" in RSC Advances (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3347 .

TY  - JOUR
AU  - Izrael-Živković, Lidija
AU  - Beškoski, Vladimir
AU  - Rikalović, Milena G.
AU  - Kazazić, Snježana
AU  - Shapiro, Nicole
AU  - Woyke, Tanja
AU  - Gojgić-Cvijović, Gordana D.
AU  - Vrvić, Miroslav M.
AU  - Maksimović, Nela
AU  - Karadžić, Ivanka M.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3705
AB  - The strain Pseudomonas aeruginosa san ai, isolated from an extreme environment (industrial mineral cutting oil, pH 10), is able to survive and persist in the presence of a variety of pollutants such as heavy metals and organic chemicals. The genome of P. aeruginosa san ai is 6.98 Mbp long with a GC content of 66.08% and 6485 protein encoding genes. A large number of genes associated with proteins, responsible for microbial resistance to heavy metal ions and involved in catabolism of toxic aromatic organic compounds were identified. P. aeruginosa san ai is a highly cadmium-resistant strain. Proteome analysis of biomass after cadmium exposal confirmed a high tolerance to sublethal concentrations of cadmium (100 mg/L), based on: extracellular biosorption, bioaccumulation, biofilm formation, controlled siderophore production and a pronounced metalloprotein synthesis. Proteins responsible for survival in osmostress conditions during exposure to elevated concentrations of cadmium (200 mg/L) demonstrate a strong genetic potential of P. aeruginosa san ai for survival and adaptation. Sequencing of P. aeruginosa san ai genome provides valuable insights into the evolution and adaptation of this microbe to environmental extremes at the whole-genome level, as well as how to optimally use the strain in bioremediation of chemically polluted sites.
PB  - Springer Japan
T2  - Extremophiles
T1  - High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals
VL  - 23
IS  - 4
SP  - 399
EP  - 405
DO  - 10.1007/s00792-019-01092-w
ER  - 

@article{
author = "Izrael-Živković, Lidija and Beškoski, Vladimir and Rikalović, Milena G. and Kazazić, Snježana and Shapiro, Nicole and Woyke, Tanja and Gojgić-Cvijović, Gordana D. and Vrvić, Miroslav M. and Maksimović, Nela and Karadžić, Ivanka M.",
year = "2019",
abstract = "The strain Pseudomonas aeruginosa san ai, isolated from an extreme environment (industrial mineral cutting oil, pH 10), is able to survive and persist in the presence of a variety of pollutants such as heavy metals and organic chemicals. The genome of P. aeruginosa san ai is 6.98 Mbp long with a GC content of 66.08% and 6485 protein encoding genes. A large number of genes associated with proteins, responsible for microbial resistance to heavy metal ions and involved in catabolism of toxic aromatic organic compounds were identified. P. aeruginosa san ai is a highly cadmium-resistant strain. Proteome analysis of biomass after cadmium exposal confirmed a high tolerance to sublethal concentrations of cadmium (100 mg/L), based on: extracellular biosorption, bioaccumulation, biofilm formation, controlled siderophore production and a pronounced metalloprotein synthesis. Proteins responsible for survival in osmostress conditions during exposure to elevated concentrations of cadmium (200 mg/L) demonstrate a strong genetic potential of P. aeruginosa san ai for survival and adaptation. Sequencing of P. aeruginosa san ai genome provides valuable insights into the evolution and adaptation of this microbe to environmental extremes at the whole-genome level, as well as how to optimally use the strain in bioremediation of chemically polluted sites.",
publisher = "Springer Japan",
journal = "Extremophiles",
title = "High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals",
volume = "23",
number = "4",
pages = "399-405",
doi = "10.1007/s00792-019-01092-w"
}

Izrael-Živković, L., Beškoski, V., Rikalović, M. G., Kazazić, S., Shapiro, N., Woyke, T., Gojgić-Cvijović, G. D., Vrvić, M. M., Maksimović, N.,& Karadžić, I. M.. (2019). High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals. in Extremophiles
Springer Japan., 23(4), 399-405.
https://doi.org/10.1007/s00792-019-01092-w

Izrael-Živković L, Beškoski V, Rikalović MG, Kazazić S, Shapiro N, Woyke T, Gojgić-Cvijović GD, Vrvić MM, Maksimović N, Karadžić IM. High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals. in Extremophiles. 2019;23(4):399-405.
doi:10.1007/s00792-019-01092-w .

Izrael-Živković, Lidija, Beškoski, Vladimir, Rikalović, Milena G., Kazazić, Snježana, Shapiro, Nicole, Woyke, Tanja, Gojgić-Cvijović, Gordana D., Vrvić, Miroslav M., Maksimović, Nela, Karadžić, Ivanka M., "High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals" in Extremophiles, 23, no. 4 (2019):399-405,
https://doi.org/10.1007/s00792-019-01092-w . .

TY  - JOUR
AU  - Izrael-Živković, Lidija
AU  - Rikalović, Milena G.
AU  - Gojgić-Cvijović, Gordana D.
AU  - Kazazić, Saša
AU  - Vrvić, Miroslav M.
AU  - Brčeski, Ilija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka D.
AU  - Gopčević, Kristina
AU  - Karadžić, Ivanka M.
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2118
AB  - Pseudomonas aeruginosa san ai is a promising candidate for bioremediation of cadmium pollution, as it resists a high concentration of up to 7.2 mM of cadmium. Leaving biomass of P. aeruginosa san ai exposed to cadmium has a large biosorption potential, implying its capacity to extract heavy metal from contaminated medium. In the present study, we investigated tolerance and accumulation of cadmium on protein level by shotgun proteomics approach based on liquid chromatography and tandem mass spectrometry coupled with bioinformatics to identify proteins. Size exclusion chromatography was used for protein prefractionation to preserve native forms of metalloproteins and protein complexes. Using this approach a total of 60 proteins were observed as up-regulated in cadmium-amended culture. Almost a third of the total numbers of up-regulated were metalloproteins. Particularly interesting are denitrification proteins which are over expressed but not active, suggesting their protective role in conditions of heavy metal exposure. P. aeruginosa san ai developed a complex mechanism to adapt to cadmium, based on: extracellular biosorption, bioaccumulation, the formation of biofilm, controlled siderophore production, enhanced respiration and modified protein profile. An increased abundance of proteins involved in: cell energy metabolism, including denitrification proteins; amino acid metabolism; cell motility and posttranslational modifications, primarily based on thiol-disulfide exchange, were observed. Enhanced oxygen consumption of biomass in cadmium-amended culture versus control was found. Our results signify that P. aeruginosa san ai is naturally well equipped to overcome and survive high doses of cadmium and, as such, has a great potential for application in bioremediation of cadmium polluted sites.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai
VL  - 8
IS  - 19
SP  - 10549
EP  - 10560
DO  - 10.1039/c8ra00371h
ER  - 

@article{
author = "Izrael-Živković, Lidija and Rikalović, Milena G. and Gojgić-Cvijović, Gordana D. and Kazazić, Saša and Vrvić, Miroslav M. and Brčeski, Ilija and Beškoski, Vladimir and Lončarević, Branka D. and Gopčević, Kristina and Karadžić, Ivanka M.",
year = "2018",
abstract = "Pseudomonas aeruginosa san ai is a promising candidate for bioremediation of cadmium pollution, as it resists a high concentration of up to 7.2 mM of cadmium. Leaving biomass of P. aeruginosa san ai exposed to cadmium has a large biosorption potential, implying its capacity to extract heavy metal from contaminated medium. In the present study, we investigated tolerance and accumulation of cadmium on protein level by shotgun proteomics approach based on liquid chromatography and tandem mass spectrometry coupled with bioinformatics to identify proteins. Size exclusion chromatography was used for protein prefractionation to preserve native forms of metalloproteins and protein complexes. Using this approach a total of 60 proteins were observed as up-regulated in cadmium-amended culture. Almost a third of the total numbers of up-regulated were metalloproteins. Particularly interesting are denitrification proteins which are over expressed but not active, suggesting their protective role in conditions of heavy metal exposure. P. aeruginosa san ai developed a complex mechanism to adapt to cadmium, based on: extracellular biosorption, bioaccumulation, the formation of biofilm, controlled siderophore production, enhanced respiration and modified protein profile. An increased abundance of proteins involved in: cell energy metabolism, including denitrification proteins; amino acid metabolism; cell motility and posttranslational modifications, primarily based on thiol-disulfide exchange, were observed. Enhanced oxygen consumption of biomass in cadmium-amended culture versus control was found. Our results signify that P. aeruginosa san ai is naturally well equipped to overcome and survive high doses of cadmium and, as such, has a great potential for application in bioremediation of cadmium polluted sites.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai",
volume = "8",
number = "19",
pages = "10549-10560",
doi = "10.1039/c8ra00371h"
}

Izrael-Živković, L., Rikalović, M. G., Gojgić-Cvijović, G. D., Kazazić, S., Vrvić, M. M., Brčeski, I., Beškoski, V., Lončarević, B. D., Gopčević, K.,& Karadžić, I. M.. (2018). Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai. in RSC Advances
Royal Soc Chemistry, Cambridge., 8(19), 10549-10560.
https://doi.org/10.1039/c8ra00371h

Izrael-Živković L, Rikalović MG, Gojgić-Cvijović GD, Kazazić S, Vrvić MM, Brčeski I, Beškoski V, Lončarević BD, Gopčević K, Karadžić IM. Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai. in RSC Advances. 2018;8(19):10549-10560.
doi:10.1039/c8ra00371h .

Izrael-Živković, Lidija, Rikalović, Milena G., Gojgić-Cvijović, Gordana D., Kazazić, Saša, Vrvić, Miroslav M., Brčeski, Ilija, Beškoski, Vladimir, Lončarević, Branka D., Gopčević, Kristina, Karadžić, Ivanka M., "Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai" in RSC Advances, 8, no. 19 (2018):10549-10560,
https://doi.org/10.1039/c8ra00371h . .

TY  - DATA
AU  - Izrael-Živković, Lidija
AU  - Rikalović, Milena G.
AU  - Gojgić-Cvijović, Gordana D.
AU  - Kazazić, Saša
AU  - Vrvić, Miroslav M.
AU  - Brčeski, Ilija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka D.
AU  - Gopčević, Kristina
AU  - Karadžić, Ivanka M.
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3179
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.;  Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic  Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8  (19), 10549–10560. https://doi.org/10.1039/c8ra00371h
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3179
ER  - 

@misc{
author = "Izrael-Živković, Lidija and Rikalović, Milena G. and Gojgić-Cvijović, Gordana D. and Kazazić, Saša and Vrvić, Miroslav M. and Brčeski, Ilija and Beškoski, Vladimir and Lončarević, Branka D. and Gopčević, Kristina and Karadžić, Ivanka M.",
year = "2018",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.;  Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic  Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8  (19), 10549–10560. https://doi.org/10.1039/c8ra00371h",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3179"
}

Izrael-Živković, L., Rikalović, M. G., Gojgić-Cvijović, G. D., Kazazić, S., Vrvić, M. M., Brčeski, I., Beškoski, V., Lončarević, B. D., Gopčević, K.,& Karadžić, I. M.. (2018). Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.;  Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic  Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8  (19), 10549–10560. https://doi.org/10.1039/c8ra00371h. in RSC Advances
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3179

Izrael-Živković L, Rikalović MG, Gojgić-Cvijović GD, Kazazić S, Vrvić MM, Brčeski I, Beškoski V, Lončarević BD, Gopčević K, Karadžić IM. Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.;  Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic  Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8  (19), 10549–10560. https://doi.org/10.1039/c8ra00371h. in RSC Advances. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3179 .

Izrael-Živković, Lidija, Rikalović, Milena G., Gojgić-Cvijović, Gordana D., Kazazić, Saša, Vrvić, Miroslav M., Brčeski, Ilija, Beškoski, Vladimir, Lončarević, Branka D., Gopčević, Kristina, Karadžić, Ivanka M., "Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.;  Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic  Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8  (19), 10549–10560. https://doi.org/10.1039/c8ra00371h" in RSC Advances (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3179 .

TY  - DATA
AU  - Izrael-Živković, Lidija
AU  - Živković, Ljiljana S.
AU  - Beškoski, Vladimir
AU  - Gopčević, Kristina
AU  - Jokić, Bojan
AU  - Radosavljević, Dragoslav S.
AU  - Karadžić, Ivanka M.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3649
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3649
ER  - 

@misc{
author = "Izrael-Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Jokić, Bojan and Radosavljević, Dragoslav S. and Karadžić, Ivanka M.",
year = "2016",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3649"
}

Izrael-Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Jokić, B., Radosavljević, D. S.,& Karadžić, I. M.. (2016). Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001. in Journal of Molecular Catalysis. B: Enzymatic.
https://hdl.handle.net/21.15107/rcub_cherry_3649

Izrael-Živković L, Živković LS, Beškoski V, Gopčević K, Jokić B, Radosavljević DS, Karadžić IM. Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001. in Journal of Molecular Catalysis. B: Enzymatic. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3649 .

Izrael-Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Jokić, Bojan, Radosavljević, Dragoslav S., Karadžić, Ivanka M., "Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001" in Journal of Molecular Catalysis. B: Enzymatic (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3649 .

TY  - JOUR
AU  - Izrael-Živković, Lidija
AU  - Živković, Ljiljana S.
AU  - Beškoski, Vladimir
AU  - Gopčević, Kristina
AU  - Jokić, Bojan
AU  - Radosavljević, Dragoslav S.
AU  - Karadžić, Ivanka M.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3648
AB  - The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media
VL  - 133
DO  - 10.1016/j.molcatb.2017.06.001
ER  - 

@article{
author = "Izrael-Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Jokić, Bojan and Radosavljević, Dragoslav S. and Karadžić, Ivanka M.",
year = "2016",
abstract = "The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media",
volume = "133",
doi = "10.1016/j.molcatb.2017.06.001"
}

Izrael-Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Jokić, B., Radosavljević, D. S.,& Karadžić, I. M.. (2016). The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic, 133.
https://doi.org/10.1016/j.molcatb.2017.06.001

Izrael-Živković L, Živković LS, Beškoski V, Gopčević K, Jokić B, Radosavljević DS, Karadžić IM. The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic. 2016;133.
doi:10.1016/j.molcatb.2017.06.001 .

Izrael-Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Jokić, Bojan, Radosavljević, Dragoslav S., Karadžić, Ivanka M., "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media" in Journal of Molecular Catalysis. B: Enzymatic, 133 (2016),
https://doi.org/10.1016/j.molcatb.2017.06.001 . .

TY  - JOUR
AU  - Izrael-Živković, Lidija
AU  - Živković, Ljiljana S.
AU  - Beškoski, Vladimir
AU  - Gopčević, Kristina
AU  - Jokić, Bojan
AU  - Radosavljević, Dragoslav S.
AU  - Karadžić, Ivanka M.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/315
AB  - The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media
VL  - 133
DO  - 10.1016/j.molcatb.2017.06.001
ER  - 

@article{
author = "Izrael-Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Jokić, Bojan and Radosavljević, Dragoslav S. and Karadžić, Ivanka M.",
year = "2016",
abstract = "The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media",
volume = "133",
doi = "10.1016/j.molcatb.2017.06.001"
}

Izrael-Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Jokić, B., Radosavljević, D. S.,& Karadžić, I. M.. (2016). The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic, 133.
https://doi.org/10.1016/j.molcatb.2017.06.001

Izrael-Živković L, Živković LS, Beškoski V, Gopčević K, Jokić B, Radosavljević DS, Karadžić IM. The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic. 2016;133.
doi:10.1016/j.molcatb.2017.06.001 .

Izrael-Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Jokić, Bojan, Radosavljević, Dragoslav S., Karadžić, Ivanka M., "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media" in Journal of Molecular Catalysis. B: Enzymatic, 133 (2016),
https://doi.org/10.1016/j.molcatb.2017.06.001 . .

TY  - JOUR
AU  - Karadžić, Ivanka M.
AU  - Izrael-Živković, Lidija
AU  - Gojgić-Cvijović, Gordana D.
AU  - Vujčić, Zoran
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/518
AB  - In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40degreesC. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70degreesC. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensive antibiotic production.
PB  - Soc Bioscience Bioengineering Japan, Osaka
T2  - Journal of Bioscience and Bioengineering
T1  - Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor
VL  - 94
IS  - 4
SP  - 309
EP  - 314
DO  - 10.1016/S1389-1723(02)80169-4
ER  - 

@article{
author = "Karadžić, Ivanka M. and Izrael-Živković, Lidija and Gojgić-Cvijović, Gordana D. and Vujčić, Zoran",
year = "2002",
abstract = "In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40degreesC. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70degreesC. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensive antibiotic production.",
publisher = "Soc Bioscience Bioengineering Japan, Osaka",
journal = "Journal of Bioscience and Bioengineering",
title = "Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor",
volume = "94",
number = "4",
pages = "309-314",
doi = "10.1016/S1389-1723(02)80169-4"
}

Karadžić, I. M., Izrael-Živković, L., Gojgić-Cvijović, G. D.,& Vujčić, Z.. (2002). Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering
Soc Bioscience Bioengineering Japan, Osaka., 94(4), 309-314.
https://doi.org/10.1016/S1389-1723(02)80169-4

Karadžić IM, Izrael-Živković L, Gojgić-Cvijović GD, Vujčić Z. Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering. 2002;94(4):309-314.
doi:10.1016/S1389-1723(02)80169-4 .

Karadžić, Ivanka M., Izrael-Živković, Lidija, Gojgić-Cvijović, Gordana D., Vujčić, Zoran, "Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor" in Journal of Bioscience and Bioengineering, 94, no. 4 (2002):309-314,
https://doi.org/10.1016/S1389-1723(02)80169-4 . .