Izrael Živković, Lidija

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  • Izrael Živković, Lidija (3)
Projects

Author's Bibliography

A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity

Izrael Živković, Lidija; Hüttmann, Nico; Susevski, Vanessa; Medić, Ana; Beškoski, Vladimir; Berezovski, Maxim V.; Minić, Zoran; Živković, Ljiljana; Karadžić, Ivanka

(2023)

TY  - JOUR
AU  - Izrael Živković, Lidija
AU  - Hüttmann, Nico
AU  - Susevski, Vanessa
AU  - Medić, Ana
AU  - Beškoski, Vladimir
AU  - Berezovski, Maxim V.
AU  - Minić, Zoran
AU  - Živković, Ljiljana
AU  - Karadžić, Ivanka
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10736
AB  - The increased commercial use and spread of nanoceria raises concerns about the risks associated with its effects on living organisms. Although Pseudomonas aeruginosa may be ubiquitous in nature, it is largely found in locations closely linked with human activity. P. aeruginosa san ai was used as a model organism for a deeper understanding of the interaction between biomolecules of the bacteria with this intriguing nanomaterial. A comprehensive proteomics approach along with analysis of altered respiration and production of targeted/specific secondary metabolites was conducted to study the response of P. aeruginosa san ai to nanoceria. Quantitative proteomics found that proteins associated with redox homeostasis, biosynthesis of amino acids, and lipid catabolism were upregulated. Proteins from outer cellular structures were downregulated, including transporters responsible for peptides, sugars, amino acids and polyamines, and the crucial TolB protein of the Tol-Pal system, required for the structural formation of the outer membrane layer. In accordance with the altered redox homeostasis proteins, an increased amount of pyocyanin, a key redox shuttle, and the upregulation of the siderophore, pyoverdine, responsible for iron homeostasis, were found. Production of extracellular molecules, e.g. pyocyanin, pyoverdine, exopolysaccharides, lipase, and alkaline protease, was significantly increased in P. aeruginosa san ai exposed to nanoceria. Overall, nanoceria at sublethal concentrations induces profound metabolic changes in P. aeruginosa san ai and provokes increased secretion of extracellular virulence factors, revealing the powerful influence this nanomaterial has on the vital functions of the microorganism. © 2023 Informa UK Limited, trading as Taylor & Francis Group.
T2  - Nanotoxicology
T1  - A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity
VL  - 17
IS  - 1
SP  - 20
EP  - 41
DO  - 10.1080/17435390.2023.2180451
ER  - 
@article{
author = "Izrael Živković, Lidija and Hüttmann, Nico and Susevski, Vanessa and Medić, Ana and Beškoski, Vladimir and Berezovski, Maxim V. and Minić, Zoran and Živković, Ljiljana and Karadžić, Ivanka",
year = "2023",
abstract = "The increased commercial use and spread of nanoceria raises concerns about the risks associated with its effects on living organisms. Although Pseudomonas aeruginosa may be ubiquitous in nature, it is largely found in locations closely linked with human activity. P. aeruginosa san ai was used as a model organism for a deeper understanding of the interaction between biomolecules of the bacteria with this intriguing nanomaterial. A comprehensive proteomics approach along with analysis of altered respiration and production of targeted/specific secondary metabolites was conducted to study the response of P. aeruginosa san ai to nanoceria. Quantitative proteomics found that proteins associated with redox homeostasis, biosynthesis of amino acids, and lipid catabolism were upregulated. Proteins from outer cellular structures were downregulated, including transporters responsible for peptides, sugars, amino acids and polyamines, and the crucial TolB protein of the Tol-Pal system, required for the structural formation of the outer membrane layer. In accordance with the altered redox homeostasis proteins, an increased amount of pyocyanin, a key redox shuttle, and the upregulation of the siderophore, pyoverdine, responsible for iron homeostasis, were found. Production of extracellular molecules, e.g. pyocyanin, pyoverdine, exopolysaccharides, lipase, and alkaline protease, was significantly increased in P. aeruginosa san ai exposed to nanoceria. Overall, nanoceria at sublethal concentrations induces profound metabolic changes in P. aeruginosa san ai and provokes increased secretion of extracellular virulence factors, revealing the powerful influence this nanomaterial has on the vital functions of the microorganism. © 2023 Informa UK Limited, trading as Taylor & Francis Group.",
journal = "Nanotoxicology",
title = "A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity",
volume = "17",
number = "1",
pages = "20-41",
doi = "10.1080/17435390.2023.2180451"
}
Izrael Živković, L., Hüttmann, N., Susevski, V., Medić, A., Beškoski, V., Berezovski, M. V., Minić, Z., Živković, L.,& Karadžić, I.. (2023). A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity. in Nanotoxicology, 17(1), 20-41.
https://doi.org/10.1080/17435390.2023.2180451
Izrael Živković L, Hüttmann N, Susevski V, Medić A, Beškoski V, Berezovski MV, Minić Z, Živković L, Karadžić I. A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity. in Nanotoxicology. 2023;17(1):20-41.
doi:10.1080/17435390.2023.2180451 .
Izrael Živković, Lidija, Hüttmann, Nico, Susevski, Vanessa, Medić, Ana, Beškoski, Vladimir, Berezovski, Maxim V., Minić, Zoran, Živković, Ljiljana, Karadžić, Ivanka, "A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity" in Nanotoxicology, 17, no. 1 (2023):20-41,
https://doi.org/10.1080/17435390.2023.2180451 . .
2

Candida rugosa lipase immobilized onto titania as nanobiocatalyst in organic solvent

Izrael Živković, Lidija; Živković, Ljiljana S.; Beškoski, Vladimir; Gopčević, Kristina; Radosavljević, Dragoslav; Karadžić, Ivanka

(RAD Centre, Niš, Serbia, 2017)

TY  - CONF
AU  - Izrael Živković, Lidija
AU  - Živković, Ljiljana S.
AU  - Beškoski, Vladimir
AU  - Gopčević, Kristina
AU  - Radosavljević, Dragoslav
AU  - Karadžić, Ivanka
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11195
AB  - Kinetic measurements can be used to predict the optimum kinetic behaviour of a particular biocatalyst. Based on those predictions, optimisation of biocatalytic reactions, as well as process design to improve productivity and reduce the cost of various processes can be performed.
PB  - RAD Centre, Niš, Serbia
C3  - RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
T1  - Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent
SP  - 76
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11195
ER  - 
@conference{
author = "Izrael Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Radosavljević, Dragoslav and Karadžić, Ivanka",
year = "2017",
abstract = "Kinetic measurements can be used to predict the optimum kinetic behaviour of a particular biocatalyst. Based on those predictions, optimisation of biocatalytic reactions, as well as process design to improve productivity and reduce the cost of various processes can be performed.",
publisher = "RAD Centre, Niš, Serbia",
journal = "RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro",
title = "Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent",
pages = "76",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11195"
}
Izrael Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Radosavljević, D.,& Karadžić, I.. (2017). Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
RAD Centre, Niš, Serbia., 76.
https://hdl.handle.net/21.15107/rcub_vinar_11195
Izrael Živković L, Živković LS, Beškoski V, Gopčević K, Radosavljević D, Karadžić I. Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro. 2017;:76.
https://hdl.handle.net/21.15107/rcub_vinar_11195 .
Izrael Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Radosavljević, Dragoslav, Karadžić, Ivanka, "Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent" in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro (2017):76,
https://hdl.handle.net/21.15107/rcub_vinar_11195 .

Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential

Izrael Živković, Lidija; Živković, Ljiljana S.

(RAD Centre, Niš, Serbia, 2017)

TY  - CONF
AU  - Izrael Živković, Lidija
AU  - Živković, Ljiljana S.
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11194
AB  - Enzyme catalyzed reactions have been extensively exploited for a wide range of applications in biotechnology. In spite of a broad implementation of enzymes in different fields, some constraints referred to their cost and process stability still exists. To overcome a limit related to short catalytic lifetime of enzymes in process conditions, a spectrum of immobilization methods have been extensively studied to increase stability and enhance reuse, offer easier separation, making production economically viable.
PB  - RAD Centre, Niš, Serbia
C3  - RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
T1  - Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential
SP  - 75
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11194
ER  - 
@conference{
author = "Izrael Živković, Lidija and Živković, Ljiljana S.",
year = "2017",
abstract = "Enzyme catalyzed reactions have been extensively exploited for a wide range of applications in biotechnology. In spite of a broad implementation of enzymes in different fields, some constraints referred to their cost and process stability still exists. To overcome a limit related to short catalytic lifetime of enzymes in process conditions, a spectrum of immobilization methods have been extensively studied to increase stability and enhance reuse, offer easier separation, making production economically viable.",
publisher = "RAD Centre, Niš, Serbia",
journal = "RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro",
title = "Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential",
pages = "75",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11194"
}
Izrael Živković, L.,& Živković, L. S.. (2017). Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
RAD Centre, Niš, Serbia., 75.
https://hdl.handle.net/21.15107/rcub_vinar_11194
Izrael Živković L, Živković LS. Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro. 2017;:75.
https://hdl.handle.net/21.15107/rcub_vinar_11194 .
Izrael Živković, Lidija, Živković, Ljiljana S., "Candida rugosa lipase immobilized onto titania: improved thermal stability and reuse potential" in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro (2017):75,
https://hdl.handle.net/21.15107/rcub_vinar_11194 .