TY  - JOUR
AU  - Izrael‑Živković, Lidija
AU  - Beškoski, Vladimir
AU  - Rikalović, Milena
AU  - Kazazić, Snježana
AU  - Shapiro, Nicole
AU  - Woyke, Tanja
AU  - Gojgić-Cvijović, Gordana
AU  - Vrvić, Miroslav
AU  - Maksimović, Nela
AU  - Karadžić, Ivanka
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3026
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 andinvolved 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 (100mg/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 (200mg/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
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 and Kazazić, Snježana and Shapiro, Nicole and Woyke, Tanja and Gojgić-Cvijović, Gordana and Vrvić, Miroslav and Maksimović, Nela and Karadžić, Ivanka",
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 andinvolved 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 (100mg/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 (200mg/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",
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., Kazazić, S., Shapiro, N., Woyke, T., Gojgić-Cvijović, G., Vrvić, M., Maksimović, N.,& Karadžić, I.. (2019). High-quality draft genome sequence of Pseudomonas aeruginosa san ai, an environmental isolate resistant to heavy metals. in Extremophiles
Springer., 23(4), 399-405.
https://doi.org/10.1007/s00792-019-01092-w

Izrael‑Živković L, Beškoski V, Rikalović M, Kazazić S, Shapiro N, Woyke T, Gojgić-Cvijović G, Vrvić M, Maksimović N, Karadžić I. 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, Kazazić, Snježana, Shapiro, Nicole, Woyke, Tanja, Gojgić-Cvijović, Gordana, Vrvić, Miroslav, Maksimović, Nela, Karadžić, Ivanka, "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  - Medić, Ana
AU  - Stojanović, Ksenija
AU  - Izrael-Živković, Lidija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka
AU  - Kazazić, Saša
AU  - Karadžić, Ivanka
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3214
AB  - The Pseudomonas aeruginosa san ai strain was investigated for its capability to degrade the 2,6-di-tertbutylphenol (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
PB  - Royal Society of Chemistry
T2  - RSC Advances
T1  - A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-tertbutylphenol 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 and Izrael-Živković, Lidija and Beškoski, Vladimir and Lončarević, Branka and Kazazić, Saša and Karadžić, Ivanka",
year = "2019",
abstract = "The Pseudomonas aeruginosa san ai strain was investigated for its capability to degrade the 2,6-di-tertbutylphenol (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",
publisher = "Royal Society of Chemistry",
journal = "RSC Advances",
title = "A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-tertbutylphenol 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., Izrael-Živković, L., Beškoski, V., Lončarević, B., Kazazić, S.,& Karadžić, I.. (2019). A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-tertbutylphenol and proteomic changes in the degrader Pseudomonas aeruginosa san ai. in RSC Advances
Royal Society of Chemistry., 9(41), 23696-23710.
https://doi.org/10.1039/c9ra04298a

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-tertbutylphenol 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, Izrael-Živković, Lidija, Beškoski, Vladimir, Lončarević, Branka, Kazazić, Saša, Karadžić, Ivanka, "A comprehensive study of conditions of the biodegradation of a plastic additive 2,6-di-tertbutylphenol 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  - JOUR
AU  - Izrael‑Živković, Lidija
AU  - Rikalović, Milena
AU  - Gojgić-Cvijović, Gordana
AU  - Kazazic, Sasa
AU  - Vrvić, Miroslav
AU  - Brčeski, Ilija
AU  - Beškoski, Vladimir
AU  - Lončarević, Branka
AU  - Gopcevic, Kristina
AU  - Karadžić, Ivanka
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2347
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 and Gojgić-Cvijović, Gordana and Kazazic, Sasa and Vrvić, Miroslav and Brčeski, Ilija and Beškoski, Vladimir and Lončarević, Branka and Gopcevic, Kristina and Karadžić, Ivanka",
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., Gojgić-Cvijović, G., Kazazic, S., Vrvić, M., Brčeski, I., Beškoski, V., Lončarević, B., Gopcevic, K.,& Karadžić, I.. (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 M, Gojgić-Cvijović G, Kazazic S, Vrvić M, Brčeski I, Beškoski V, Lončarević B, Gopcevic K, Karadžić I. 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, Gojgić-Cvijović, Gordana, Kazazic, Sasa, Vrvić, Miroslav, Brčeski, Ilija, Beškoski, Vladimir, Lončarević, Branka, Gopcevic, Kristina, Karadžić, Ivanka, "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  - GEN
AU  - Izrael-Živković, Lidija
AU  - Karadžić, Ivanka
AU  - Gojgić-Cvijović, Gordana
AU  - Rikalović, Milena
AU  - Vrvić, Miroslav
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5090
AB  - Tehničko rešenje je iz oblasti mikrobiološke proizvodnje enzima. Odnosi se na nov i ekonomičan postupak fermentacije za proizvodnju lipaze. Tehničko rešenje omogućava proizvodnju enzima koji je stabilan i aktivan u organskim rastvaračima. Lipaza se može primeniti u hidrolizi i sintezi (u nevodenoj sredini) složenih lipidnih molekula.
PB  - University of Belgrade - Institute of Chemistry, Technology and Metallurgy
T1  - Novi tehnološki postupak za dobijanje mikrobne lipaze pomoću Pseudomonas aeruginosa NCAIM(P)B 001380
UR  - https://hdl.handle.net/21.15107/rcub_cer_5090
ER  - 

@misc{
author = "Izrael-Živković, Lidija and Karadžić, Ivanka and Gojgić-Cvijović, Gordana and Rikalović, Milena and Vrvić, Miroslav",
year = "2012",
abstract = "Tehničko rešenje je iz oblasti mikrobiološke proizvodnje enzima. Odnosi se na nov i ekonomičan postupak fermentacije za proizvodnju lipaze. Tehničko rešenje omogućava proizvodnju enzima koji je stabilan i aktivan u organskim rastvaračima. Lipaza se može primeniti u hidrolizi i sintezi (u nevodenoj sredini) složenih lipidnih molekula.",
publisher = "University of Belgrade - Institute of Chemistry, Technology and Metallurgy",
title = "Novi tehnološki postupak za dobijanje mikrobne lipaze pomoću Pseudomonas aeruginosa NCAIM(P)B 001380",
url = "https://hdl.handle.net/21.15107/rcub_cer_5090"
}

Izrael-Živković, L., Karadžić, I., Gojgić-Cvijović, G., Rikalović, M.,& Vrvić, M.. (2012). Novi tehnološki postupak za dobijanje mikrobne lipaze pomoću Pseudomonas aeruginosa NCAIM(P)B 001380. 
University of Belgrade - Institute of Chemistry, Technology and Metallurgy..
https://hdl.handle.net/21.15107/rcub_cer_5090

Izrael-Živković L, Karadžić I, Gojgić-Cvijović G, Rikalović M, Vrvić M. Novi tehnološki postupak za dobijanje mikrobne lipaze pomoću Pseudomonas aeruginosa NCAIM(P)B 001380. 2012;.
https://hdl.handle.net/21.15107/rcub_cer_5090 .

Izrael-Živković, Lidija, Karadžić, Ivanka, Gojgić-Cvijović, Gordana, Rikalović, Milena, Vrvić, Miroslav, "Novi tehnološki postupak za dobijanje mikrobne lipaze pomoću Pseudomonas aeruginosa NCAIM(P)B 001380" (2012),
https://hdl.handle.net/21.15107/rcub_cer_5090 .

TY  - CONF
AU  - Izrael-Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Natić, Maja
AU  - Vrvić, Miroslav
AU  - Karadžić, Ivanka
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5201
AB  - Poster presented at 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011
T1  - Pseudomonas lipase catalyzed synthesis of ergosterol oleate
UR  - https://hdl.handle.net/21.15107/rcub_cer_5201
ER  - 

@conference{
author = "Izrael-Živković, Lidija and Gojgić-Cvijović, Gordana and Natić, Maja and Vrvić, Miroslav and Karadžić, Ivanka",
year = "2011",
abstract = "Poster presented at 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011",
title = "Pseudomonas lipase catalyzed synthesis of ergosterol oleate",
url = "https://hdl.handle.net/21.15107/rcub_cer_5201"
}

Izrael-Živković, L., Gojgić-Cvijović, G., Natić, M., Vrvić, M.,& Karadžić, I.. (2011). Pseudomonas lipase catalyzed synthesis of ergosterol oleate. .
https://hdl.handle.net/21.15107/rcub_cer_5201

Izrael-Živković L, Gojgić-Cvijović G, Natić M, Vrvić M, Karadžić I. Pseudomonas lipase catalyzed synthesis of ergosterol oleate. 2011;.
https://hdl.handle.net/21.15107/rcub_cer_5201 .

Izrael-Živković, Lidija, Gojgić-Cvijović, Gordana, Natić, Maja, Vrvić, Miroslav, Karadžić, Ivanka, "Pseudomonas lipase catalyzed synthesis of ergosterol oleate" (2011),
https://hdl.handle.net/21.15107/rcub_cer_5201 .

TY  - CONF
AU  - Izrael-Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Natić, Maja
AU  - Vrvić, Miroslav
AU  - Karadžić, Ivanka
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5200
AB  - In the present study, the potential of bacterial lipase isolated from Pseudomonas aeruginosa NCATM (P) B 001380 to catalyze the esterification of ergosterol with oleic acid in the simple process, was evaluated. The prepared ergosterol oleate was purified by column chromatography and identification was conducted by NMR.
PB  - Beograd: Udruženje mikrobioologa Srbije
C3  - Proceedings - 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011
T1  - Pseudomonas lipase catalyzed synthesis of ergosterol oleate
SP  - pp. 2
UR  - https://hdl.handle.net/21.15107/rcub_cer_5200
ER  - 

@conference{
author = "Izrael-Živković, Lidija and Gojgić-Cvijović, Gordana and Natić, Maja and Vrvić, Miroslav and Karadžić, Ivanka",
year = "2011",
abstract = "In the present study, the potential of bacterial lipase isolated from Pseudomonas aeruginosa NCATM (P) B 001380 to catalyze the esterification of ergosterol with oleic acid in the simple process, was evaluated. The prepared ergosterol oleate was purified by column chromatography and identification was conducted by NMR.",
publisher = "Beograd: Udruženje mikrobioologa Srbije",
journal = "Proceedings - 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011",
title = "Pseudomonas lipase catalyzed synthesis of ergosterol oleate",
pages = "pp. 2",
url = "https://hdl.handle.net/21.15107/rcub_cer_5200"
}

Izrael-Živković, L., Gojgić-Cvijović, G., Natić, M., Vrvić, M.,& Karadžić, I.. (2011). Pseudomonas lipase catalyzed synthesis of ergosterol oleate. in Proceedings - 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011
Beograd: Udruženje mikrobioologa Srbije., pp. 2.
https://hdl.handle.net/21.15107/rcub_cer_5200

Izrael-Živković L, Gojgić-Cvijović G, Natić M, Vrvić M, Karadžić I. Pseudomonas lipase catalyzed synthesis of ergosterol oleate. in Proceedings - 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011. 2011;:pp. 2.
https://hdl.handle.net/21.15107/rcub_cer_5200 .

Izrael-Živković, Lidija, Gojgić-Cvijović, Gordana, Natić, Maja, Vrvić, Miroslav, Karadžić, Ivanka, "Pseudomonas lipase catalyzed synthesis of ergosterol oleate" in Proceedings - 7th Balkan Congress of Microbiology and 8th Congress of Serbian Microbiologists, Belgrade, October 25-29, 2011 (2011):pp. 2,
https://hdl.handle.net/21.15107/rcub_cer_5200 .

TY  - CONF
AU  - Izrael-Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Rikalović, Milena
AU  - Vrvić, Miroslav
AU  - Karadžić, Ivanka
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5062
PB  - Belgrade : Serbian Chemical Society
C3  - Program i kratki izvodi radova XLIX Savetovanja Srpskog hemijskog društva, (13-14. maj 2011., Kragujevac)
T1  - Ispitivanja potencijala lipaze Pseudomonas aeruginosa san ai za sintezu estara u nevodenoj sredini
SP  - 104
UR  - https://hdl.handle.net/21.15107/rcub_cer_5062
ER  - 

@conference{
author = "Izrael-Živković, Lidija and Gojgić-Cvijović, Gordana and Rikalović, Milena and Vrvić, Miroslav and Karadžić, Ivanka",
year = "2011",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Program i kratki izvodi radova XLIX Savetovanja Srpskog hemijskog društva, (13-14. maj 2011., Kragujevac)",
title = "Ispitivanja potencijala lipaze Pseudomonas aeruginosa san ai za sintezu estara u nevodenoj sredini",
pages = "104",
url = "https://hdl.handle.net/21.15107/rcub_cer_5062"
}

Izrael-Živković, L., Gojgić-Cvijović, G., Rikalović, M., Vrvić, M.,& Karadžić, I.. (2011). Ispitivanja potencijala lipaze Pseudomonas aeruginosa san ai za sintezu estara u nevodenoj sredini. in Program i kratki izvodi radova XLIX Savetovanja Srpskog hemijskog društva, (13-14. maj 2011., Kragujevac)
Belgrade : Serbian Chemical Society., 104.
https://hdl.handle.net/21.15107/rcub_cer_5062

Izrael-Živković L, Gojgić-Cvijović G, Rikalović M, Vrvić M, Karadžić I. Ispitivanja potencijala lipaze Pseudomonas aeruginosa san ai za sintezu estara u nevodenoj sredini. in Program i kratki izvodi radova XLIX Savetovanja Srpskog hemijskog društva, (13-14. maj 2011., Kragujevac). 2011;:104.
https://hdl.handle.net/21.15107/rcub_cer_5062 .

Izrael-Živković, Lidija, Gojgić-Cvijović, Gordana, Rikalović, Milena, Vrvić, Miroslav, Karadžić, Ivanka, "Ispitivanja potencijala lipaze Pseudomonas aeruginosa san ai za sintezu estara u nevodenoj sredini" in Program i kratki izvodi radova XLIX Savetovanja Srpskog hemijskog društva, (13-14. maj 2011., Kragujevac) (2011):104,
https://hdl.handle.net/21.15107/rcub_cer_5062 .

TY  - JOUR
AU  - Izrael‑Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Karadžić, Ivanka
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/713
AB  - Enzymatic characteristics of a protease from a medically important, referent strain of Pseudomonas aeruginosa ATCC 27853 were determined. According to sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDS-PAGE, and gel filtration, it was estimated that the molecular mass of the purified enzyme was about 15 kDa. Other enzymatic properties were found to be: pH optimum 7.1, pH stability between 6.5 and 10; temperature optimum around 60 °C while the enzyme was stable at 60°C for 30 min. Inhibition of the enzyme was observed with metal chelators, such as EDTA and 1,10-phenanthroline, suggesting that the protease is a metalloenzyme. Furthermore, the enzyme contains one mole of zinc ion per mole of enzyme. The protease was stable in the presence of different organic solvents, which enables its potential use for the synthesis of peptides.
AB  - U ovom radu je okarakterisana ekstracelularna proteaza medicinski značajnog, referentnog soja Pseudomonas aeruginosa ATCC 27853. Molekulska masa prečišćenog enzima određena SDS PAGE i gel filtracijom iznosi oko 15 kDa. Određeni su sledeći enzimski parametri: pH optimum 7,1; pH stabilnost u opsegu 6,5-10; temperaturni optimum 60°C, a enzim je stabilan na 60°C 30 min. Na osnovu inhibicije enzima pomoću EDTA i 1,10-fenantrolina, utvrđeno je da proteaza predstavlja metaloenzim. Pokazano da proteaza sadrži 1 mol jona cinka po molu enzima. Proteaza je stabilna u prisustvu različitih organskih rastvarača, što omogućava upotrebu za sintezu peptida.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853
T1  - Izolovanje i delimično karakterisanje proteaze iz Pseudomonas aeruginosa ATCC 27853
VL  - 75
IS  - 8
SP  - 1041
EP  - 1052
DO  - 10.2298/JSC100125088I
ER  - 

@article{
author = "Izrael‑Živković, Lidija and Gojgić-Cvijović, Gordana and Karadžić, Ivanka",
year = "2010",
abstract = "Enzymatic characteristics of a protease from a medically important, referent strain of Pseudomonas aeruginosa ATCC 27853 were determined. According to sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDS-PAGE, and gel filtration, it was estimated that the molecular mass of the purified enzyme was about 15 kDa. Other enzymatic properties were found to be: pH optimum 7.1, pH stability between 6.5 and 10; temperature optimum around 60 °C while the enzyme was stable at 60°C for 30 min. Inhibition of the enzyme was observed with metal chelators, such as EDTA and 1,10-phenanthroline, suggesting that the protease is a metalloenzyme. Furthermore, the enzyme contains one mole of zinc ion per mole of enzyme. The protease was stable in the presence of different organic solvents, which enables its potential use for the synthesis of peptides., U ovom radu je okarakterisana ekstracelularna proteaza medicinski značajnog, referentnog soja Pseudomonas aeruginosa ATCC 27853. Molekulska masa prečišćenog enzima određena SDS PAGE i gel filtracijom iznosi oko 15 kDa. Određeni su sledeći enzimski parametri: pH optimum 7,1; pH stabilnost u opsegu 6,5-10; temperaturni optimum 60°C, a enzim je stabilan na 60°C 30 min. Na osnovu inhibicije enzima pomoću EDTA i 1,10-fenantrolina, utvrđeno je da proteaza predstavlja metaloenzim. Pokazano da proteaza sadrži 1 mol jona cinka po molu enzima. Proteaza je stabilna u prisustvu različitih organskih rastvarača, što omogućava upotrebu za sintezu peptida.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853, Izolovanje i delimično karakterisanje proteaze iz Pseudomonas aeruginosa ATCC 27853",
volume = "75",
number = "8",
pages = "1041-1052",
doi = "10.2298/JSC100125088I"
}

Izrael‑Živković, L., Gojgić-Cvijović, G.,& Karadžić, I.. (2010). Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 75(8), 1041-1052.
https://doi.org/10.2298/JSC100125088I

Izrael‑Živković L, Gojgić-Cvijović G, Karadžić I. Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853. in Journal of the Serbian Chemical Society. 2010;75(8):1041-1052.
doi:10.2298/JSC100125088I .

Izrael‑Živković, Lidija, Gojgić-Cvijović, Gordana, Karadžić, Ivanka, "Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853" in Journal of the Serbian Chemical Society, 75, no. 8 (2010):1041-1052,
https://doi.org/10.2298/JSC100125088I . .

TY  - JOUR
AU  - Izrael‑Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Gopcevic, K.R.
AU  - Vrvić, Miroslav
AU  - Karadžić, Ivanka
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/587
AB  - An extracellular lipase from Pseudomonas aeruginosa ATCC 27853 has been purified and its enzymatic characteristics were determined. According to SDS-PAGE and gel filtration molecular mass estimated to be 30 kDa, what classified the lipase in group I.1. Although 14 lipases from P. aeruginosa with similar molecular mass are referred to date, their basic enzymatic properties have not been reported yet. To address the gap we found: the optimal temperature and pH in water solution being 50 °C and 9.3, respectively; the lipase was inhibited with Hg2+ ions and sodium dodecylsulphate (SDS), while non-ionic detergent Triton X-100 activated the enzyme; the lipase hydrolyzed more rapidly middle chain triglycerides and it was not regiospecific; the lipase demonstrated naturally occurring stability in different organic solvents with concentrations ranging from 30 to 70%, including good thermal stability in 30% organic solvent solution. Even though strain P. aeruginosa ATCC 27853 was not isolated from extreme environment it showed activity in organic solvent suggesting that this lipase is suitable for variety of applications, including reactions in water restricted medium and bioremediation of contaminations by organic solvents.
T2  - Journal of Basic Microbiology
T1  - Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853
VL  - 49
IS  - 5
SP  - 452
EP  - 462
DO  - 10.1002/jobm.200800229
ER  - 

@article{
author = "Izrael‑Živković, Lidija and Gojgić-Cvijović, Gordana and Gopcevic, K.R. and Vrvić, Miroslav and Karadžić, Ivanka",
year = "2009",
abstract = "An extracellular lipase from Pseudomonas aeruginosa ATCC 27853 has been purified and its enzymatic characteristics were determined. According to SDS-PAGE and gel filtration molecular mass estimated to be 30 kDa, what classified the lipase in group I.1. Although 14 lipases from P. aeruginosa with similar molecular mass are referred to date, their basic enzymatic properties have not been reported yet. To address the gap we found: the optimal temperature and pH in water solution being 50 °C and 9.3, respectively; the lipase was inhibited with Hg2+ ions and sodium dodecylsulphate (SDS), while non-ionic detergent Triton X-100 activated the enzyme; the lipase hydrolyzed more rapidly middle chain triglycerides and it was not regiospecific; the lipase demonstrated naturally occurring stability in different organic solvents with concentrations ranging from 30 to 70%, including good thermal stability in 30% organic solvent solution. Even though strain P. aeruginosa ATCC 27853 was not isolated from extreme environment it showed activity in organic solvent suggesting that this lipase is suitable for variety of applications, including reactions in water restricted medium and bioremediation of contaminations by organic solvents.",
journal = "Journal of Basic Microbiology",
title = "Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853",
volume = "49",
number = "5",
pages = "452-462",
doi = "10.1002/jobm.200800229"
}

Izrael‑Živković, L., Gojgić-Cvijović, G., Gopcevic, K.R., Vrvić, M.,& Karadžić, I.. (2009). Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853. in Journal of Basic Microbiology, 49(5), 452-462.
https://doi.org/10.1002/jobm.200800229

Izrael‑Živković L, Gojgić-Cvijović G, Gopcevic K, Vrvić M, Karadžić I. Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853. in Journal of Basic Microbiology. 2009;49(5):452-462.
doi:10.1002/jobm.200800229 .

Izrael‑Živković, Lidija, Gojgić-Cvijović, Gordana, Gopcevic, K.R., Vrvić, Miroslav, Karadžić, Ivanka, "Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853" in Journal of Basic Microbiology, 49, no. 5 (2009):452-462,
https://doi.org/10.1002/jobm.200800229 . .

TY  - JOUR
AU  - Karadžić, Ivanka
AU  - Izrael, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Vujčić, Zoran
PY  - 2002
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/93
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 40°C. 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 70°C. 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  - Society of Fermentation and Bioengineering
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 and Izrael, Lidija and Gojgić-Cvijović, Gordana 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 40°C. 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 70°C. 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 = "Society of Fermentation and Bioengineering",
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., Izrael, L., Gojgić-Cvijović, G.,& Vujčić, Z.. (2002). Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering
Society of Fermentation and Bioengineering., 94(4), 309-314.
https://doi.org/10.1016/S1389-1723(02)80169-4

Karadžić I, Izrael L, Gojgić-Cvijović G, 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, Izrael, Lidija, Gojgić-Cvijović, Gordana, 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 . .

TY  - CONF
AU  - Izrael-Živković, Lidija
AU  - Karadžić, Ivanka
AU  - Gojgić-Cvijović, Gordana
PY  - 2002
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/65
PB  - Medicinski fakultet, Beograd
C3  - Medicinska istraživanja
T1  - Leucinaminopeptidaza soja, streptomyces hygroscopicus - izolovanje i karakterizacija
VL  - 36
IS  - 4
SP  - 66
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cer_65
ER  - 

@conference{
author = "Izrael-Živković, Lidija and Karadžić, Ivanka and Gojgić-Cvijović, Gordana",
year = "2002",
publisher = "Medicinski fakultet, Beograd",
journal = "Medicinska istraživanja",
title = "Leucinaminopeptidaza soja, streptomyces hygroscopicus - izolovanje i karakterizacija",
volume = "36",
number = "4",
pages = "66-66",
url = "https://hdl.handle.net/21.15107/rcub_cer_65"
}

Izrael-Živković, L., Karadžić, I.,& Gojgić-Cvijović, G.. (2002). Leucinaminopeptidaza soja, streptomyces hygroscopicus - izolovanje i karakterizacija. in Medicinska istraživanja
Medicinski fakultet, Beograd., 36(4), 66-66.
https://hdl.handle.net/21.15107/rcub_cer_65

Izrael-Živković L, Karadžić I, Gojgić-Cvijović G. Leucinaminopeptidaza soja, streptomyces hygroscopicus - izolovanje i karakterizacija. in Medicinska istraživanja. 2002;36(4):66-66.
https://hdl.handle.net/21.15107/rcub_cer_65 .

Izrael-Živković, Lidija, Karadžić, Ivanka, Gojgić-Cvijović, Gordana, "Leucinaminopeptidaza soja, streptomyces hygroscopicus - izolovanje i karakterizacija" in Medicinska istraživanja, 36, no. 4 (2002):66-66,
https://hdl.handle.net/21.15107/rcub_cer_65 .

TY  - JOUR
AU  - Izrael, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Karadžić, Ivanka
PY  - 2001
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/30
AB  - We have witnessed an explosion of informations about properties, also mode of action and regulation of proteases from the metalloproteases at the cell surface to the AIDS protease. Protease inhibitors have a great importance in mechanism of proteolysis. One of the latest strategies to combat diseases like AIDS and cancer is to use proteinase inhibitors as drugs. Especially good source of protease inhibitors are microorganisms. A few low-molecular-weight proetease inhibitors of microbial origin, as a potential drugs, was described.
AB  - Budući da je upotreba inhibitora aminopetidaza u lečenju SIDE, takođe i kancera različitih vrsta, tzv. nova strategija u lečenju ovih bolesti [18] to je u toku traženje novih inhibitora AP a posebno LAP kao proizvoda metabolizma mikroorganizama, ali i stereoselektivna sinteza jedinjenja koja su im slična [19]. Može se pretpostaviti da će sledećih godina napredak u biohemiji patoloških procesa biti pod velikim uticajem napretka u istraživanju niskomolekulskih inhibitora koje produkuju mikroorganizmi ali i napretka u sintezi analoga ovih jedinjenja.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Hemijski pregled
T1  - Low-molecular-weight protease inhibitors of microbial origin
T1  - Niskomolekulski inhibitori proteaza mikrobnog porekla
VL  - 42
IS  - 1
SP  - 4
EP  - 9
UR  - https://hdl.handle.net/21.15107/rcub_cer_30
ER  - 

@article{
author = "Izrael, Lidija and Gojgić-Cvijović, Gordana and Karadžić, Ivanka",
year = "2001",
abstract = "We have witnessed an explosion of informations about properties, also mode of action and regulation of proteases from the metalloproteases at the cell surface to the AIDS protease. Protease inhibitors have a great importance in mechanism of proteolysis. One of the latest strategies to combat diseases like AIDS and cancer is to use proteinase inhibitors as drugs. Especially good source of protease inhibitors are microorganisms. A few low-molecular-weight proetease inhibitors of microbial origin, as a potential drugs, was described., Budući da je upotreba inhibitora aminopetidaza u lečenju SIDE, takođe i kancera različitih vrsta, tzv. nova strategija u lečenju ovih bolesti [18] to je u toku traženje novih inhibitora AP a posebno LAP kao proizvoda metabolizma mikroorganizama, ali i stereoselektivna sinteza jedinjenja koja su im slična [19]. Može se pretpostaviti da će sledećih godina napredak u biohemiji patoloških procesa biti pod velikim uticajem napretka u istraživanju niskomolekulskih inhibitora koje produkuju mikroorganizmi ali i napretka u sintezi analoga ovih jedinjenja.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Hemijski pregled",
title = "Low-molecular-weight protease inhibitors of microbial origin, Niskomolekulski inhibitori proteaza mikrobnog porekla",
volume = "42",
number = "1",
pages = "4-9",
url = "https://hdl.handle.net/21.15107/rcub_cer_30"
}

Izrael, L., Gojgić-Cvijović, G.,& Karadžić, I.. (2001). Low-molecular-weight protease inhibitors of microbial origin. in Hemijski pregled
Srpsko hemijsko društvo, Beograd., 42(1), 4-9.
https://hdl.handle.net/21.15107/rcub_cer_30

Izrael L, Gojgić-Cvijović G, Karadžić I. Low-molecular-weight protease inhibitors of microbial origin. in Hemijski pregled. 2001;42(1):4-9.
https://hdl.handle.net/21.15107/rcub_cer_30 .

Izrael, Lidija, Gojgić-Cvijović, Gordana, Karadžić, Ivanka, "Low-molecular-weight protease inhibitors of microbial origin" in Hemijski pregled, 42, no. 1 (2001):4-9,
https://hdl.handle.net/21.15107/rcub_cer_30 .

TY  - JOUR
AU  - Vučetić, Jovan
AU  - Gojgić-Cvijović, Gordana
AU  - Gopčević, Kristina
AU  - Izrael, Lidija
PY  - 2000
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5
AB  - In this paper mushrooms as an important food component were described. Their chemical composition: nitrogen compounds, carbohydrates, mineral and organic acids, as well as vitamins, enzymes and aromatic and extractable substances were discussed. Chemical composition of mushrooms was compared with the other foods - some kinds of meat. Also, micro and macroelements contents was presented. The role of mushrooms in medicine was described.
AB  - U radu su opisane gljive (pečurke) kao važan sastojak ishrane. Naveden je njihov hemijski sastav: azotne supstance, ugljeni hidrati, mineralne i organske kiseline, vitamini, enzimi, aromatične i ekstraktivne supstance. Dat je pregled zastupljenosti mikro- i makroelemenata u gljivama. Ukazano je i na ulogu gljiva u medicini.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Hemijski pregled
T1  - Mushrooms: An important food product
T1  - Jestive gljive (pečurke) - cenjen proizvod ishrane
VL  - 41
IS  - 2
SP  - 51
EP  - 55
UR  - https://hdl.handle.net/21.15107/rcub_cer_5
ER  - 

@article{
author = "Vučetić, Jovan and Gojgić-Cvijović, Gordana and Gopčević, Kristina and Izrael, Lidija",
year = "2000",
abstract = "In this paper mushrooms as an important food component were described. Their chemical composition: nitrogen compounds, carbohydrates, mineral and organic acids, as well as vitamins, enzymes and aromatic and extractable substances were discussed. Chemical composition of mushrooms was compared with the other foods - some kinds of meat. Also, micro and macroelements contents was presented. The role of mushrooms in medicine was described., U radu su opisane gljive (pečurke) kao važan sastojak ishrane. Naveden je njihov hemijski sastav: azotne supstance, ugljeni hidrati, mineralne i organske kiseline, vitamini, enzimi, aromatične i ekstraktivne supstance. Dat je pregled zastupljenosti mikro- i makroelemenata u gljivama. Ukazano je i na ulogu gljiva u medicini.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Hemijski pregled",
title = "Mushrooms: An important food product, Jestive gljive (pečurke) - cenjen proizvod ishrane",
volume = "41",
number = "2",
pages = "51-55",
url = "https://hdl.handle.net/21.15107/rcub_cer_5"
}

Vučetić, J., Gojgić-Cvijović, G., Gopčević, K.,& Izrael, L.. (2000). Mushrooms: An important food product. in Hemijski pregled
Srpsko hemijsko društvo, Beograd., 41(2), 51-55.
https://hdl.handle.net/21.15107/rcub_cer_5

Vučetić J, Gojgić-Cvijović G, Gopčević K, Izrael L. Mushrooms: An important food product. in Hemijski pregled. 2000;41(2):51-55.
https://hdl.handle.net/21.15107/rcub_cer_5 .

Vučetić, Jovan, Gojgić-Cvijović, Gordana, Gopčević, Kristina, Izrael, Lidija, "Mushrooms: An important food product" in Hemijski pregled, 41, no. 2 (2000):51-55,
https://hdl.handle.net/21.15107/rcub_cer_5 .

TY  - JOUR
AU  - Izrael, Lidija
AU  - Karadžić, Ivanka
AU  - Gojgić-Cvijović, Gordana
AU  - Vrvić, Miroslav
PY  - 2000
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/8
AB  - Strain Streptomyces (S.) hygroscopicus CH-7 during the fermen­tation of polyketide antibiotic produces as a by product proteolytic com­plex with significant trypsin like activity. Also, S. hygroscopicus CH-7 produces extracellulary proteinaceous protease inhibitor known as Streptomyces subtilisine like inhibitor (SSL-inhibitor). Detection of SSL-inhibitor is preformed on the base of stability of SSL-inhibitors on very low pH (final concentracion of TCA is 9%). Molecular mass of SSL-inhibitor is approximately 11 kDa, and it provides very wide range of inhibitory activity toward different serin proteases: trypsin, protease from Bacillus (B.) subtilis, proteinase K from Tritirachium (T.) album, pro­tease from B. licheniformis, protease from S. griseus and the complex of proteases from S. hygroscopicus CH-7.
AB  - Soj S. hygroscopicus CH-7 u toku fermentacije ekstracelularno proizvodi proteinski inhibitor proteaza koji pripada grupi Streptomyces subtilizinu sličnim inhibitorima (Streptomyces subtilisine like inhibitor: SSL-inhibitor). Postupak za detekciju je jednostavan i bazira se na činjenici da su SSL-inhibitori stabilni na veoma niskim pH. SSL-inhibitor iz S. hygroscopicus CH-7 pokazuje širok spektar inhibitornog dejstva na: tripsin, proteazu iz B. subtilis, proteinazu K iz T. album, proteazu iz B. licheniformis, proteazu iz S. griseus i na sirovi proteoliticki kompleks S. hygroscopicus CH-7. Molekulska masa SSL-inhibitora određena gel filtracijom iznosi 11 kDa, slično većini do sada izolovanih SSL.
T2  - Acta biologica iugoslavica - serija B: Mikrobiologija
T1  - Streptomyces subtilisine (SSL) inhibitor from streptomyces hygroscopius CH-7: Detection and partial characterization
T1  - Streptomyces subtilizinu sličan inhibitor (SSL-inhibitor) iz streptomyces hygroscopicus CH-7 - detekcija i delimična karakterizacija
VL  - 37
IS  - 1
SP  - 31
EP  - 36
UR  - https://hdl.handle.net/21.15107/rcub_cer_8
ER  - 

@article{
author = "Izrael, Lidija and Karadžić, Ivanka and Gojgić-Cvijović, Gordana and Vrvić, Miroslav",
year = "2000",
abstract = "Strain Streptomyces (S.) hygroscopicus CH-7 during the fermen­tation of polyketide antibiotic produces as a by product proteolytic com­plex with significant trypsin like activity. Also, S. hygroscopicus CH-7 produces extracellulary proteinaceous protease inhibitor known as Streptomyces subtilisine like inhibitor (SSL-inhibitor). Detection of SSL-inhibitor is preformed on the base of stability of SSL-inhibitors on very low pH (final concentracion of TCA is 9%). Molecular mass of SSL-inhibitor is approximately 11 kDa, and it provides very wide range of inhibitory activity toward different serin proteases: trypsin, protease from Bacillus (B.) subtilis, proteinase K from Tritirachium (T.) album, pro­tease from B. licheniformis, protease from S. griseus and the complex of proteases from S. hygroscopicus CH-7., Soj S. hygroscopicus CH-7 u toku fermentacije ekstracelularno proizvodi proteinski inhibitor proteaza koji pripada grupi Streptomyces subtilizinu sličnim inhibitorima (Streptomyces subtilisine like inhibitor: SSL-inhibitor). Postupak za detekciju je jednostavan i bazira se na činjenici da su SSL-inhibitori stabilni na veoma niskim pH. SSL-inhibitor iz S. hygroscopicus CH-7 pokazuje širok spektar inhibitornog dejstva na: tripsin, proteazu iz B. subtilis, proteinazu K iz T. album, proteazu iz B. licheniformis, proteazu iz S. griseus i na sirovi proteoliticki kompleks S. hygroscopicus CH-7. Molekulska masa SSL-inhibitora određena gel filtracijom iznosi 11 kDa, slično većini do sada izolovanih SSL.",
journal = "Acta biologica iugoslavica - serija B: Mikrobiologija",
title = "Streptomyces subtilisine (SSL) inhibitor from streptomyces hygroscopius CH-7: Detection and partial characterization, Streptomyces subtilizinu sličan inhibitor (SSL-inhibitor) iz streptomyces hygroscopicus CH-7 - detekcija i delimična karakterizacija",
volume = "37",
number = "1",
pages = "31-36",
url = "https://hdl.handle.net/21.15107/rcub_cer_8"
}

Izrael, L., Karadžić, I., Gojgić-Cvijović, G.,& Vrvić, M.. (2000). Streptomyces subtilisine (SSL) inhibitor from streptomyces hygroscopius CH-7: Detection and partial characterization. in Acta biologica iugoslavica - serija B: Mikrobiologija, 37(1), 31-36.
https://hdl.handle.net/21.15107/rcub_cer_8

Izrael L, Karadžić I, Gojgić-Cvijović G, Vrvić M. Streptomyces subtilisine (SSL) inhibitor from streptomyces hygroscopius CH-7: Detection and partial characterization. in Acta biologica iugoslavica - serija B: Mikrobiologija. 2000;37(1):31-36.
https://hdl.handle.net/21.15107/rcub_cer_8 .

Izrael, Lidija, Karadžić, Ivanka, Gojgić-Cvijović, Gordana, Vrvić, Miroslav, "Streptomyces subtilisine (SSL) inhibitor from streptomyces hygroscopius CH-7: Detection and partial characterization" in Acta biologica iugoslavica - serija B: Mikrobiologija, 37, no. 1 (2000):31-36,
https://hdl.handle.net/21.15107/rcub_cer_8 .