Kazazić, Saša

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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

Medić, Ana; Stojanović, Ksenija; Izrael-Živković, Lidija; Beškoski, Vladimir; Lončarević, Branka; Kazazić, Saša; Karadžić, Ivanka

(Royal Society of Chemistry, 2019)

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 . .
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