TY  - JOUR
AU  - Makryniotis, Konstantinos
AU  - Nikolaivits, Efstratios
AU  - Taxeidis, George
AU  - Nikodinović-Runić, Jasmina
AU  - Topakas, Evangelos
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1002/biot.202400053
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2341
AB  - The rapid escalation of plastic waste accumulation presents a significant threat of the modern world, demanding an immediate solution. Over the last years, utilization of the enzymatic machinery of various microorganisms has emerged as an environmentally friendly asset in tackling this pressing global challenge. Thus, various hydrolases have been demonstrated to effectively degrade polyesters. Plastic waste streams often consist of a variety of different polyesters, as impurities, mainly due to wrong disposal practices, rendering recycling process challenging. The elucidation of the selective degradation of polyesters by hydrolases could offer a proper solution to this problem, enhancing the recyclability performance. Towards this, our study focused on the investigation of four bacterial polyesterases, including DaPUase, IsPETase, PfPHOase, and Se1JFR, a novel PETase-like lipase. The enzymes, which were biochemically characterized and structurally analyzed, demonstrated degradation ability of synthetic plastics. While a consistent pattern of polyesters’ degradation was observed across all enzymes, Se1JFR stood out in the degradation of PBS, PLA, and polyether PU. Additionally, it exhibited comparable results to IsPETase, a benchmark mesophilic PETase, in the degradation of PCL and semi-crystalline PET. Our results point out the wide substrate spectrum of bacterial hydrolases and underscore the significant potential of PETase-like enzymes in polyesters degradation.
T2  - Biotechnology Journal
T2  - Biotechnology Journal
T1  - Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases
IS  - n/a
SP  - 2400053
VL  - n/a
DO  - 10.1002/biot.202400053
ER  - 

@article{
author = "Makryniotis, Konstantinos and Nikolaivits, Efstratios and Taxeidis, George and Nikodinović-Runić, Jasmina and Topakas, Evangelos",
abstract = "The rapid escalation of plastic waste accumulation presents a significant threat of the modern world, demanding an immediate solution. Over the last years, utilization of the enzymatic machinery of various microorganisms has emerged as an environmentally friendly asset in tackling this pressing global challenge. Thus, various hydrolases have been demonstrated to effectively degrade polyesters. Plastic waste streams often consist of a variety of different polyesters, as impurities, mainly due to wrong disposal practices, rendering recycling process challenging. The elucidation of the selective degradation of polyesters by hydrolases could offer a proper solution to this problem, enhancing the recyclability performance. Towards this, our study focused on the investigation of four bacterial polyesterases, including DaPUase, IsPETase, PfPHOase, and Se1JFR, a novel PETase-like lipase. The enzymes, which were biochemically characterized and structurally analyzed, demonstrated degradation ability of synthetic plastics. While a consistent pattern of polyesters’ degradation was observed across all enzymes, Se1JFR stood out in the degradation of PBS, PLA, and polyether PU. Additionally, it exhibited comparable results to IsPETase, a benchmark mesophilic PETase, in the degradation of PCL and semi-crystalline PET. Our results point out the wide substrate spectrum of bacterial hydrolases and underscore the significant potential of PETase-like enzymes in polyesters degradation.",
journal = "Biotechnology Journal, Biotechnology Journal",
title = "Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases",
number = "n/a",
pages = "2400053",
volume = "n/a",
doi = "10.1002/biot.202400053"
}

Makryniotis, K., Nikolaivits, E., Taxeidis, G., Nikodinović-Runić, J.,& Topakas, E..Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases. in Biotechnology Journal, n/a(n/a), 2400053.
https://doi.org/10.1002/biot.202400053

Makryniotis K, Nikolaivits E, Taxeidis G, Nikodinović-Runić J, Topakas E. Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases. in Biotechnology Journal.n/a(n/a):2400053.
doi:10.1002/biot.202400053 .

Makryniotis, Konstantinos, Nikolaivits, Efstratios, Taxeidis, George, Nikodinović-Runić, Jasmina, Topakas, Evangelos, "Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases" in Biotechnology Journal, n/a, no. n/a:2400053,
https://doi.org/10.1002/biot.202400053 . .

TY  - JOUR
AU  - Makryniotis, Konstantinos
AU  - Nikolaivits, Efstratios
AU  - Taxeidis, George
AU  - Nikodinović-Runić, Jasmina
AU  - Topakas, Evangelos
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1002/biot.202400053
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2345
AB  - The rapid escalation of plastic waste accumulation presents a significant threat of the modern world, demanding an immediate solution. Over the last years, utilization of the enzymatic machinery of various microorganisms has emerged as an environmentally friendly asset in tackling this pressing global challenge. Thus, various hydrolases have been demonstrated to effectively degrade polyesters. Plastic waste streams often consist of a variety of different polyesters, as impurities, mainly due to wrong disposal practices, rendering recycling process challenging. The elucidation of the selective degradation of polyesters by hydrolases could offer a proper solution to this problem, enhancing the recyclability performance. Towards this, our study focused on the investigation of four bacterial polyesterases, including DaPUase, IsPETase, PfPHOase, and Se1JFR, a novel PETase-like lipase. The enzymes, which were biochemically characterized and structurally analyzed, demonstrated degradation ability of synthetic plastics. While a consistent pattern of polyesters’ degradation was observed across all enzymes, Se1JFR stood out in the degradation of PBS, PLA, and polyether PU. Additionally, it exhibited comparable results to IsPETase, a benchmark mesophilic PETase, in the degradation of PCL and semi-crystalline PET. Our results point out the wide substrate spectrum of bacterial hydrolases and underscore the significant potential of PETase-like enzymes in polyesters degradation.
T2  - Biotechnology Journal
T1  - Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases
IS  - n/a
SP  - 2400053
VL  - n/a
DO  - 10.1002/biot.202400053
ER  - 

@article{
author = "Makryniotis, Konstantinos and Nikolaivits, Efstratios and Taxeidis, George and Nikodinović-Runić, Jasmina and Topakas, Evangelos",
abstract = "The rapid escalation of plastic waste accumulation presents a significant threat of the modern world, demanding an immediate solution. Over the last years, utilization of the enzymatic machinery of various microorganisms has emerged as an environmentally friendly asset in tackling this pressing global challenge. Thus, various hydrolases have been demonstrated to effectively degrade polyesters. Plastic waste streams often consist of a variety of different polyesters, as impurities, mainly due to wrong disposal practices, rendering recycling process challenging. The elucidation of the selective degradation of polyesters by hydrolases could offer a proper solution to this problem, enhancing the recyclability performance. Towards this, our study focused on the investigation of four bacterial polyesterases, including DaPUase, IsPETase, PfPHOase, and Se1JFR, a novel PETase-like lipase. The enzymes, which were biochemically characterized and structurally analyzed, demonstrated degradation ability of synthetic plastics. While a consistent pattern of polyesters’ degradation was observed across all enzymes, Se1JFR stood out in the degradation of PBS, PLA, and polyether PU. Additionally, it exhibited comparable results to IsPETase, a benchmark mesophilic PETase, in the degradation of PCL and semi-crystalline PET. Our results point out the wide substrate spectrum of bacterial hydrolases and underscore the significant potential of PETase-like enzymes in polyesters degradation.",
journal = "Biotechnology Journal",
title = "Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases",
number = "n/a",
pages = "2400053",
volume = "n/a",
doi = "10.1002/biot.202400053"
}

Makryniotis, K., Nikolaivits, E., Taxeidis, G., Nikodinović-Runić, J.,& Topakas, E..Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases. in Biotechnology Journal, n/a(n/a), 2400053.
https://doi.org/10.1002/biot.202400053

Makryniotis K, Nikolaivits E, Taxeidis G, Nikodinović-Runić J, Topakas E. Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases. in Biotechnology Journal.n/a(n/a):2400053.
doi:10.1002/biot.202400053 .

Makryniotis, Konstantinos, Nikolaivits, Efstratios, Taxeidis, George, Nikodinović-Runić, Jasmina, Topakas, Evangelos, "Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases" in Biotechnology Journal, n/a, no. n/a:2400053,
https://doi.org/10.1002/biot.202400053 . .

TY  - JOUR
AU  - Taxeidis, George
AU  - Đapović, Milica
AU  - Nikolaivits, Efstratios
AU  - Maslak, Veselin
AU  - Nikodinović-Runić, Jasmina
AU  - Topakas, Evangelos
PY  - 2024
UR  - https://doi.org/10.1021/acssuschemeng.4c00143
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2339
AB  - The discovery and engineering of novel biocatalysts capable of depolymerizing polyethylene terephthalate (PET) have gained significant attention since the need for green technologies to combat plastic pollution has become increasingly urgent. This study focuses on the development of novel substrates that can indicate enzymes with PET hydrolytic activity, streamlining the process of enzyme evaluation and selection. Four novel substrates, mimicking the structure of PET, were chemically synthesized and labeled with fluorogenic or chromogenic moieties, enabling the direct analysis of candidate enzymes without complex preparatory or analysis steps. The fluorogenic substrates, mUPET1, mUPET2, and mUPET3, not only identify enzymes capable of PET breakdown but also differentiate those with exceptional performance on the polymer, such as the benchmark PETase, LCCICCG. Among the substrates, the chromogenic p-NPhPET3 stands out as a reliable tool for screening both pure and crude enzymes, offering advantages over fluorogenic substrates such as ease of assay using UV–vis spectroscopy and compatibility with crude enzyme samples. However, ferulic acid esterases and mono-(2-hydroxyethyl) terephthalate esterases (MHETases), which exhibit remarkably high affinity for PET oligomers, also show high catalytic activity on these substrates. The substrates introduced in this study hold significant value in the function-based screening and characterization of enzymes that degrade PET, as well as the the potential to be used in screening mutant libraries derived from directed evolution experiments. Following this approach, a rapid and dependable assay method can be carried out using basic laboratory infrastructure, eliminating the necessity for intricate preparatory procedures before analysis.
PB  - American Chemical Society
T2  - ACS Sustainable Chemistry & Engineering
T1  - New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes
DO  - 10.1021/acssuschemeng.4c00143
ER  - 

@article{
author = "Taxeidis, George and Đapović, Milica and Nikolaivits, Efstratios and Maslak, Veselin and Nikodinović-Runić, Jasmina and Topakas, Evangelos",
year = "2024",
abstract = "The discovery and engineering of novel biocatalysts capable of depolymerizing polyethylene terephthalate (PET) have gained significant attention since the need for green technologies to combat plastic pollution has become increasingly urgent. This study focuses on the development of novel substrates that can indicate enzymes with PET hydrolytic activity, streamlining the process of enzyme evaluation and selection. Four novel substrates, mimicking the structure of PET, were chemically synthesized and labeled with fluorogenic or chromogenic moieties, enabling the direct analysis of candidate enzymes without complex preparatory or analysis steps. The fluorogenic substrates, mUPET1, mUPET2, and mUPET3, not only identify enzymes capable of PET breakdown but also differentiate those with exceptional performance on the polymer, such as the benchmark PETase, LCCICCG. Among the substrates, the chromogenic p-NPhPET3 stands out as a reliable tool for screening both pure and crude enzymes, offering advantages over fluorogenic substrates such as ease of assay using UV–vis spectroscopy and compatibility with crude enzyme samples. However, ferulic acid esterases and mono-(2-hydroxyethyl) terephthalate esterases (MHETases), which exhibit remarkably high affinity for PET oligomers, also show high catalytic activity on these substrates. The substrates introduced in this study hold significant value in the function-based screening and characterization of enzymes that degrade PET, as well as the the potential to be used in screening mutant libraries derived from directed evolution experiments. Following this approach, a rapid and dependable assay method can be carried out using basic laboratory infrastructure, eliminating the necessity for intricate preparatory procedures before analysis.",
publisher = "American Chemical Society",
journal = "ACS Sustainable Chemistry & Engineering",
title = "New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes",
doi = "10.1021/acssuschemeng.4c00143"
}

Taxeidis, G., Đapović, M., Nikolaivits, E., Maslak, V., Nikodinović-Runić, J.,& Topakas, E.. (2024). New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes. in ACS Sustainable Chemistry & Engineering
American Chemical Society..
https://doi.org/10.1021/acssuschemeng.4c00143

Taxeidis G, Đapović M, Nikolaivits E, Maslak V, Nikodinović-Runić J, Topakas E. New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes. in ACS Sustainable Chemistry & Engineering. 2024;.
doi:10.1021/acssuschemeng.4c00143 .

Taxeidis, George, Đapović, Milica, Nikolaivits, Efstratios, Maslak, Veselin, Nikodinović-Runić, Jasmina, Topakas, Evangelos, "New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes" in ACS Sustainable Chemistry & Engineering (2024),
https://doi.org/10.1021/acssuschemeng.4c00143 . .

TY  - JOUR
AU  - Taxeidis, George
AU  - Nikolaivits, Efstratios
AU  - Siaperas, Romanos
AU  - Gkountela, Christina
AU  - Vouyiouka, Stamatina
AU  - Pantelić, Brana
AU  - Nikodinović-Runić, Jasmina
AU  - Topakas, Evangelos
PY  - 2023
UR  - https://www.sciencedirect.com/science/article/pii/S0269749123004621
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1797
AB  - The uncontrollable disposal of plastic waste has raised the concern of the scientific community, which tries to face this environmental burden by discovering and applying new techniques. Regarding the biotechnology field, several important microorganisms possessing the necessary enzymatic arsenal to utilize recalcitrant synthetic polymers as an energy source have been discovered. In the present study, we screened various fungi for their ability to degrade intact polymers, such as ether-based polyurethane (PU) and low-density polyethylene (LDPE). For this, ImpranIil® DLN-SD and a mixture of long-chain alkanes were used as sole carbon sources, indicating not only the most promising strains in agar plate screening but also inducing the secretion of depolymerizing enzymatic activities, useful for polymer degradation. The agar plate screening revealed three fungal strains belonging to Fusarium and Aspergillus genera, whose secretome was further studied for its ability to degrade the aforementioned non-treated polymers. Specifically for ether-based PU, the secretome of a Fusarium species reduced the sample mass and the average molecular weight of the polymer by 24.5 and 20.4%, respectively, while the secretome of an Aspergillus species caused changes in the molecular structure of LDPE, as evidenced by FTIR. The proteomics analysis revealed that the enzymatic activities induced in presence of Impranil® DLN-SD can be associated with urethane bond cleavage, a fact which was also supported by the observed degradation of the ether-based PU. Although, the mechanism of LDPE degradation was not completely elucidated, the presence of oxidative enzymes could be the main factor contributing to polymer modification.
T2  - Environmental Pollution
T1  - Triggering and identifying the polyurethane and polyethylene-degrading machinery of filamentous fungi secretomes
SP  - 121460
VL  - 325
DO  - 10.1016/j.envpol.2023.121460
ER  - 

@article{
author = "Taxeidis, George and Nikolaivits, Efstratios and Siaperas, Romanos and Gkountela, Christina and Vouyiouka, Stamatina and Pantelić, Brana and Nikodinović-Runić, Jasmina and Topakas, Evangelos",
year = "2023",
abstract = "The uncontrollable disposal of plastic waste has raised the concern of the scientific community, which tries to face this environmental burden by discovering and applying new techniques. Regarding the biotechnology field, several important microorganisms possessing the necessary enzymatic arsenal to utilize recalcitrant synthetic polymers as an energy source have been discovered. In the present study, we screened various fungi for their ability to degrade intact polymers, such as ether-based polyurethane (PU) and low-density polyethylene (LDPE). For this, ImpranIil® DLN-SD and a mixture of long-chain alkanes were used as sole carbon sources, indicating not only the most promising strains in agar plate screening but also inducing the secretion of depolymerizing enzymatic activities, useful for polymer degradation. The agar plate screening revealed three fungal strains belonging to Fusarium and Aspergillus genera, whose secretome was further studied for its ability to degrade the aforementioned non-treated polymers. Specifically for ether-based PU, the secretome of a Fusarium species reduced the sample mass and the average molecular weight of the polymer by 24.5 and 20.4%, respectively, while the secretome of an Aspergillus species caused changes in the molecular structure of LDPE, as evidenced by FTIR. The proteomics analysis revealed that the enzymatic activities induced in presence of Impranil® DLN-SD can be associated with urethane bond cleavage, a fact which was also supported by the observed degradation of the ether-based PU. Although, the mechanism of LDPE degradation was not completely elucidated, the presence of oxidative enzymes could be the main factor contributing to polymer modification.",
journal = "Environmental Pollution",
title = "Triggering and identifying the polyurethane and polyethylene-degrading machinery of filamentous fungi secretomes",
pages = "121460",
volume = "325",
doi = "10.1016/j.envpol.2023.121460"
}

Taxeidis, G., Nikolaivits, E., Siaperas, R., Gkountela, C., Vouyiouka, S., Pantelić, B., Nikodinović-Runić, J.,& Topakas, E.. (2023). Triggering and identifying the polyurethane and polyethylene-degrading machinery of filamentous fungi secretomes. in Environmental Pollution, 325, 121460.
https://doi.org/10.1016/j.envpol.2023.121460

Taxeidis G, Nikolaivits E, Siaperas R, Gkountela C, Vouyiouka S, Pantelić B, Nikodinović-Runić J, Topakas E. Triggering and identifying the polyurethane and polyethylene-degrading machinery of filamentous fungi secretomes. in Environmental Pollution. 2023;325:121460.
doi:10.1016/j.envpol.2023.121460 .

Taxeidis, George, Nikolaivits, Efstratios, Siaperas, Romanos, Gkountela, Christina, Vouyiouka, Stamatina, Pantelić, Brana, Nikodinović-Runić, Jasmina, Topakas, Evangelos, "Triggering and identifying the polyurethane and polyethylene-degrading machinery of filamentous fungi secretomes" in Environmental Pollution, 325 (2023):121460,
https://doi.org/10.1016/j.envpol.2023.121460 . .

TY  - JOUR
AU  - Đapović, Milica
AU  - Milivojević, Dušan
AU  - Ilić-Tomić, Tatjana
AU  - Lješević, Marija
AU  - Nikolaivits, Efstratios
AU  - Topakas, Evangelos
AU  - Maslak, Veselin
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0045653521004744
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1732
AB  - Polyethylene terephthalate (PET) is widely used material and as such became highly enriched in nature. It is generally considered inert and safe plastic, but due to the recent increased efforts to break-down PET using biotechnological approaches, we realized the scarcity of information about structural analysis of possible degradation products and their ecotoxicological assessment. Therefore, in this study, 11 compounds belonging to the group of PET precursors and possible degradation products have been comprehensively characterized. Seven of these compounds including 1-(2-hydroxyethyl)-4-methylterephthalate, ethylene glycol bis(methyl terephthalate), methyl bis(2-hydroxyethyl terephtahalate), 1,4-benzenedicarboxylic acid, 1,4-bis[2-[[4-(methoxycarbonyl)benzoyl]oxy]ethyl] ester and methyl tris(2-hydroxyethyl terephthalate) corresponding to mono-, 1.5-, di-, 2,5- and trimer of PET were synthetized and structurally characterized for the first time. In-silico druglikeness and physico-chemical properties of these compounds were predicted using variety of platforms. No antimicrobial properties were detected even at 1000 μg/mL. Ecotoxicological impact of the compounds against marine bacteria Allivibrio fischeri proved that the 6 out of 11 tested PET-associated compounds may be classified as harmful to aquatic microorganisms, with PET trimer being one of the most toxic. In comparison, most of the compounds were not toxic on human lung fibroblasts (MRC-5) at 200 μg/mL with inhibiting concentration (IC50) values of 30 μg/mL and 50 μg/mL determined for PET dimer and trimer. Only three of these compounds including PET monomer were toxic to nematode Caenorhabditis elegans at high concentration of 500 μg/mL. In terms of the applicative potential, PET dimer can be used as suitable substrate for the screening, identification and characterization of novel PET-depolymerizing enzymes.
PB  - Elsevier
T2  - Chemosphere
T2  - ChemosphereChemosphere
T1  - Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases
SP  - 130005
VL  - 275
DO  - 10.1016/j.chemosphere.2021.130005
ER  - 

@article{
author = "Đapović, Milica and Milivojević, Dušan and Ilić-Tomić, Tatjana and Lješević, Marija and Nikolaivits, Efstratios and Topakas, Evangelos and Maslak, Veselin and Nikodinović-Runić, Jasmina",
year = "2021",
abstract = "Polyethylene terephthalate (PET) is widely used material and as such became highly enriched in nature. It is generally considered inert and safe plastic, but due to the recent increased efforts to break-down PET using biotechnological approaches, we realized the scarcity of information about structural analysis of possible degradation products and their ecotoxicological assessment. Therefore, in this study, 11 compounds belonging to the group of PET precursors and possible degradation products have been comprehensively characterized. Seven of these compounds including 1-(2-hydroxyethyl)-4-methylterephthalate, ethylene glycol bis(methyl terephthalate), methyl bis(2-hydroxyethyl terephtahalate), 1,4-benzenedicarboxylic acid, 1,4-bis[2-[[4-(methoxycarbonyl)benzoyl]oxy]ethyl] ester and methyl tris(2-hydroxyethyl terephthalate) corresponding to mono-, 1.5-, di-, 2,5- and trimer of PET were synthetized and structurally characterized for the first time. In-silico druglikeness and physico-chemical properties of these compounds were predicted using variety of platforms. No antimicrobial properties were detected even at 1000 μg/mL. Ecotoxicological impact of the compounds against marine bacteria Allivibrio fischeri proved that the 6 out of 11 tested PET-associated compounds may be classified as harmful to aquatic microorganisms, with PET trimer being one of the most toxic. In comparison, most of the compounds were not toxic on human lung fibroblasts (MRC-5) at 200 μg/mL with inhibiting concentration (IC50) values of 30 μg/mL and 50 μg/mL determined for PET dimer and trimer. Only three of these compounds including PET monomer were toxic to nematode Caenorhabditis elegans at high concentration of 500 μg/mL. In terms of the applicative potential, PET dimer can be used as suitable substrate for the screening, identification and characterization of novel PET-depolymerizing enzymes.",
publisher = "Elsevier",
journal = "Chemosphere, ChemosphereChemosphere",
title = "Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases",
pages = "130005",
volume = "275",
doi = "10.1016/j.chemosphere.2021.130005"
}

Đapović, M., Milivojević, D., Ilić-Tomić, T., Lješević, M., Nikolaivits, E., Topakas, E., Maslak, V.,& Nikodinović-Runić, J.. (2021). Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases. in Chemosphere
Elsevier., 275, 130005.
https://doi.org/10.1016/j.chemosphere.2021.130005

Đapović M, Milivojević D, Ilić-Tomić T, Lješević M, Nikolaivits E, Topakas E, Maslak V, Nikodinović-Runić J. Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases. in Chemosphere. 2021;275:130005.
doi:10.1016/j.chemosphere.2021.130005 .

Đapović, Milica, Milivojević, Dušan, Ilić-Tomić, Tatjana, Lješević, Marija, Nikolaivits, Efstratios, Topakas, Evangelos, Maslak, Veselin, Nikodinović-Runić, Jasmina, "Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases" in Chemosphere, 275 (2021):130005,
https://doi.org/10.1016/j.chemosphere.2021.130005 . .

TY  - JOUR
AU  - Đapović, Milica
AU  - Milivojević, Dušan
AU  - Ilić-Tomić, Tatjana
AU  - Ljesević, Marija
AU  - Nikolaivits, Efstratios
AU  - Topakas, Evangelos
AU  - Maslak, Veselin
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1415
AB  - Polyethylene terephthalate (PET) is widely used material and as such became highly enriched in nature. It is generally considered inert and safe plastic, but due to the recent increased efforts to break-down PET using biotechnological approaches, we realized the scarcity of information about structural analysis of possible degradation products and their ecotoxicological assessment. Therefore, in this study, 11 compounds belonging to the group of PET precursors and possible degradation products have been comprehensively characterized. Seven of these compounds including 1-(2-hydroxyethyl)-4methylterephthalate, ethylene glycol bis(methyl terephthalate), methyl bis(2-hydroxyethyl terephtahalate), 1,4-benzenedicarboxylic acid, 1,4-bis[2-[[4-(methoxycarbonyl)benzoyl]oxy]ethyl] ester and methyl tris(2-hydroxyethyl terephthalate) corresponding to mono-, 1.5-, di-, 2,5- and trimer of PET were synthetized and structurally characterized for the first time. In-silico druglikeness and physico-chemical properties of these compounds were predicted using variety of platforms. No antimicrobial properties were detected even at 1000 mg/mL. Ecotoxicological impact of the compounds against marine bacteria Allivibrio fischeri proved that the 6 out of 11 tested PET-associated compounds may be classified as harmful to aquatic microorganisms, with PET trimer being one of the most toxic. In comparison, most of the compounds were not toxic on human lung fibroblasts (MRC-5) at 200 mg/mL with inhibiting concentration (IC50) values of 30 mg/mL and 50 mg/mL determined for PET dimer and trimer. Only three of these compounds including PET monomer were toxic to nematode Caenorhabditis elegans at high concentration of 500 mg/mL. In terms of the applicative potential, PET dimer can be used as suitable substrate for the screening, identification and characterization of novel PET-depolymerizing enzymes.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Chemosphere
T1  - Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases
SP  - 130005
VL  - 275
DO  - 10.1016/j.chemosphere.2021.130005
ER  - 

@article{
author = "Đapović, Milica and Milivojević, Dušan and Ilić-Tomić, Tatjana and Ljesević, Marija and Nikolaivits, Efstratios and Topakas, Evangelos and Maslak, Veselin and Nikodinović-Runić, Jasmina",
year = "2021",
abstract = "Polyethylene terephthalate (PET) is widely used material and as such became highly enriched in nature. It is generally considered inert and safe plastic, but due to the recent increased efforts to break-down PET using biotechnological approaches, we realized the scarcity of information about structural analysis of possible degradation products and their ecotoxicological assessment. Therefore, in this study, 11 compounds belonging to the group of PET precursors and possible degradation products have been comprehensively characterized. Seven of these compounds including 1-(2-hydroxyethyl)-4methylterephthalate, ethylene glycol bis(methyl terephthalate), methyl bis(2-hydroxyethyl terephtahalate), 1,4-benzenedicarboxylic acid, 1,4-bis[2-[[4-(methoxycarbonyl)benzoyl]oxy]ethyl] ester and methyl tris(2-hydroxyethyl terephthalate) corresponding to mono-, 1.5-, di-, 2,5- and trimer of PET were synthetized and structurally characterized for the first time. In-silico druglikeness and physico-chemical properties of these compounds were predicted using variety of platforms. No antimicrobial properties were detected even at 1000 mg/mL. Ecotoxicological impact of the compounds against marine bacteria Allivibrio fischeri proved that the 6 out of 11 tested PET-associated compounds may be classified as harmful to aquatic microorganisms, with PET trimer being one of the most toxic. In comparison, most of the compounds were not toxic on human lung fibroblasts (MRC-5) at 200 mg/mL with inhibiting concentration (IC50) values of 30 mg/mL and 50 mg/mL determined for PET dimer and trimer. Only three of these compounds including PET monomer were toxic to nematode Caenorhabditis elegans at high concentration of 500 mg/mL. In terms of the applicative potential, PET dimer can be used as suitable substrate for the screening, identification and characterization of novel PET-depolymerizing enzymes.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Chemosphere",
title = "Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases",
pages = "130005",
volume = "275",
doi = "10.1016/j.chemosphere.2021.130005"
}

Đapović, M., Milivojević, D., Ilić-Tomić, T., Ljesević, M., Nikolaivits, E., Topakas, E., Maslak, V.,& Nikodinović-Runić, J.. (2021). Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases. in Chemosphere
Pergamon-Elsevier Science Ltd, Oxford., 275, 130005.
https://doi.org/10.1016/j.chemosphere.2021.130005

Đapović M, Milivojević D, Ilić-Tomić T, Ljesević M, Nikolaivits E, Topakas E, Maslak V, Nikodinović-Runić J. Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases. in Chemosphere. 2021;275:130005.
doi:10.1016/j.chemosphere.2021.130005 .

Đapović, Milica, Milivojević, Dušan, Ilić-Tomić, Tatjana, Ljesević, Marija, Nikolaivits, Efstratios, Topakas, Evangelos, Maslak, Veselin, Nikodinović-Runić, Jasmina, "Synthesis and characterization of polyethylene terephthalate (PET) precursors and potential degradation products: Toxicity study and application in discovery of novel PETases" in Chemosphere, 275 (2021):130005,
https://doi.org/10.1016/j.chemosphere.2021.130005 . .

TY  - DATA
AU  - Đapović, Milica
AU  - Milivojević, Dušan
AU  - Ilić-Tomić, Tatjana
AU  - Lješević, Marija
AU  - Nikolaivits, Efstratios
AU  - Topakas, Evangelos
AU  - Maslak, Veselin
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0045653521004744
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1733
PB  - Elsevier
T2  - Chemosphere
T1  - Supplementary data for the article: Djapovic, M.; Milivojevic, D.; Ilic-Tomic, T.; Lješević, M.; Nikolaivits, E.; Topakas, E.; Maslak, V.; Nikodinovic-Runic, J. Synthesis and Characterization of Polyethylene Terephthalate (PET) Precursors and Potential Degradation Products: Toxicity Study and Application in Discovery of Novel PETases. Chemosphere 2021, 275, 130005. https://doi.org/10.1016/j.chemosphere.2021.130005.
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1733
ER  - 

@misc{
author = "Đapović, Milica and Milivojević, Dušan and Ilić-Tomić, Tatjana and Lješević, Marija and Nikolaivits, Efstratios and Topakas, Evangelos and Maslak, Veselin and Nikodinović-Runić, Jasmina",
year = "2021",
publisher = "Elsevier",
journal = "Chemosphere",
title = "Supplementary data for the article: Djapovic, M.; Milivojevic, D.; Ilic-Tomic, T.; Lješević, M.; Nikolaivits, E.; Topakas, E.; Maslak, V.; Nikodinovic-Runic, J. Synthesis and Characterization of Polyethylene Terephthalate (PET) Precursors and Potential Degradation Products: Toxicity Study and Application in Discovery of Novel PETases. Chemosphere 2021, 275, 130005. https://doi.org/10.1016/j.chemosphere.2021.130005.",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1733"
}

Đapović, M., Milivojević, D., Ilić-Tomić, T., Lješević, M., Nikolaivits, E., Topakas, E., Maslak, V.,& Nikodinović-Runić, J.. (2021). Supplementary data for the article: Djapovic, M.; Milivojevic, D.; Ilic-Tomic, T.; Lješević, M.; Nikolaivits, E.; Topakas, E.; Maslak, V.; Nikodinovic-Runic, J. Synthesis and Characterization of Polyethylene Terephthalate (PET) Precursors and Potential Degradation Products: Toxicity Study and Application in Discovery of Novel PETases. Chemosphere 2021, 275, 130005. https://doi.org/10.1016/j.chemosphere.2021.130005.. in Chemosphere
Elsevier..
https://hdl.handle.net/21.15107/rcub_imagine_1733

Đapović M, Milivojević D, Ilić-Tomić T, Lješević M, Nikolaivits E, Topakas E, Maslak V, Nikodinović-Runić J. Supplementary data for the article: Djapovic, M.; Milivojevic, D.; Ilic-Tomic, T.; Lješević, M.; Nikolaivits, E.; Topakas, E.; Maslak, V.; Nikodinovic-Runic, J. Synthesis and Characterization of Polyethylene Terephthalate (PET) Precursors and Potential Degradation Products: Toxicity Study and Application in Discovery of Novel PETases. Chemosphere 2021, 275, 130005. https://doi.org/10.1016/j.chemosphere.2021.130005.. in Chemosphere. 2021;.
https://hdl.handle.net/21.15107/rcub_imagine_1733 .

Đapović, Milica, Milivojević, Dušan, Ilić-Tomić, Tatjana, Lješević, Marija, Nikolaivits, Efstratios, Topakas, Evangelos, Maslak, Veselin, Nikodinović-Runić, Jasmina, "Supplementary data for the article: Djapovic, M.; Milivojevic, D.; Ilic-Tomic, T.; Lješević, M.; Nikolaivits, E.; Topakas, E.; Maslak, V.; Nikodinovic-Runic, J. Synthesis and Characterization of Polyethylene Terephthalate (PET) Precursors and Potential Degradation Products: Toxicity Study and Application in Discovery of Novel PETases. Chemosphere 2021, 275, 130005. https://doi.org/10.1016/j.chemosphere.2021.130005." in Chemosphere (2021),
https://hdl.handle.net/21.15107/rcub_imagine_1733 .

TY  - JOUR
AU  - Nikolaivits, Efstratios
AU  - Dimopoulou, Phaedra
AU  - Maslak, Veselin
AU  - Nikodinović-Runić, Jasmina
AU  - Topakas, Evangelos
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1633
AB  - Plastic waste poses an enormous environmental problem as a result of soil and ocean contamination, causing the release of microplastics that end up in humans through the food web. Enzymatic degradation of plastics has emerged as an alternative to traditional recycling processes. In the present work, we used bioinfomatics tools to discover a gene coding for a putative polyester degrading enzyme (polyesterase). The gene was heterologously expressed, purified and biochemically characterized. Furthermore, its ability to degrade polyethylene terephthalate (PET) model substrates and synthetic plastics was assessed.
T2  - Chemistry Proceedings
T2  - Chemistry Proceedings
T1  - Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics
IS  - 1
SP  - 33
VL  - 2
DO  - 10.3390/ECCS2020-07572
ER  - 

@article{
author = "Nikolaivits, Efstratios and Dimopoulou, Phaedra and Maslak, Veselin and Nikodinović-Runić, Jasmina and Topakas, Evangelos",
year = "2020",
abstract = "Plastic waste poses an enormous environmental problem as a result of soil and ocean contamination, causing the release of microplastics that end up in humans through the food web. Enzymatic degradation of plastics has emerged as an alternative to traditional recycling processes. In the present work, we used bioinfomatics tools to discover a gene coding for a putative polyester degrading enzyme (polyesterase). The gene was heterologously expressed, purified and biochemically characterized. Furthermore, its ability to degrade polyethylene terephthalate (PET) model substrates and synthetic plastics was assessed.",
journal = "Chemistry Proceedings, Chemistry Proceedings",
title = "Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics",
number = "1",
pages = "33",
volume = "2",
doi = "10.3390/ECCS2020-07572"
}

Nikolaivits, E., Dimopoulou, P., Maslak, V., Nikodinović-Runić, J.,& Topakas, E.. (2020). Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics. in Chemistry Proceedings, 2(1), 33.
https://doi.org/10.3390/ECCS2020-07572

Nikolaivits E, Dimopoulou P, Maslak V, Nikodinović-Runić J, Topakas E. Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics. in Chemistry Proceedings. 2020;2(1):33.
doi:10.3390/ECCS2020-07572 .

Nikolaivits, Efstratios, Dimopoulou, Phaedra, Maslak, Veselin, Nikodinović-Runić, Jasmina, Topakas, Evangelos, "Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics" in Chemistry Proceedings, 2, no. 1 (2020):33,
https://doi.org/10.3390/ECCS2020-07572 . .

TY  - JOUR
AU  - Mandić, Mina
AU  - Đokić, Lidija
AU  - Nikolaivits, Efstratios
AU  - Prodanović, Radivoje
AU  - O'Connor, Kevin
AU  - Jeremić, Sanja
AU  - Topakas, Evangelos
AU  - Nikodinović-Runić, Jasmina
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1284
AB  - Laccases are multicopper-oxidases with variety of biotechnological applications. While predominantly used, fungal laccases have limitations such as narrow pH and temperature range and their production via heterologous protein expression is more complex due to posttranslational modifications. In comparison, bacterial enzymes, including laccases, usually possess higher thermal and pH stability, and are more suitable for expression and genetic manipulations in bacterial expression hosts. Therefore, the aim of this study was to identify, recombinantly express, and characterize novel laccases from Pseudomonas spp. A combination of approaches including DNA sequence analysis, N-terminal protein sequencing, and genome sequencing data analysis for laccase amplification, cloning, and overexpression have been used. Four active recombinant laccases were obtained, one each from P. putida KT2440 and P. putida CA-3, and two from P. putida F6. The new laccases exhibited broad temperature and pH range and high thermal stability, as well as the potential to degrade selection of synthetic textile dyes. The best performing laccase was CopA from P. putida F6 which degraded five out of seven tested dyes, including Amido Black 10B, Brom Cresol Purple, Evans Blue, Reactive Black 5, and Remazol Brilliant Blue. This work highlighted species of Pseudomonas genus as still being good sources of biocatalytically relevant enzymes.
PB  - MDPI, Basel
T2  - Catalysts
T1  - Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes
IS  - 7
VL  - 9
DO  - 10.3390/catal9070629
ER  - 

@article{
author = "Mandić, Mina and Đokić, Lidija and Nikolaivits, Efstratios and Prodanović, Radivoje and O'Connor, Kevin and Jeremić, Sanja and Topakas, Evangelos and Nikodinović-Runić, Jasmina",
year = "2019",
abstract = "Laccases are multicopper-oxidases with variety of biotechnological applications. While predominantly used, fungal laccases have limitations such as narrow pH and temperature range and their production via heterologous protein expression is more complex due to posttranslational modifications. In comparison, bacterial enzymes, including laccases, usually possess higher thermal and pH stability, and are more suitable for expression and genetic manipulations in bacterial expression hosts. Therefore, the aim of this study was to identify, recombinantly express, and characterize novel laccases from Pseudomonas spp. A combination of approaches including DNA sequence analysis, N-terminal protein sequencing, and genome sequencing data analysis for laccase amplification, cloning, and overexpression have been used. Four active recombinant laccases were obtained, one each from P. putida KT2440 and P. putida CA-3, and two from P. putida F6. The new laccases exhibited broad temperature and pH range and high thermal stability, as well as the potential to degrade selection of synthetic textile dyes. The best performing laccase was CopA from P. putida F6 which degraded five out of seven tested dyes, including Amido Black 10B, Brom Cresol Purple, Evans Blue, Reactive Black 5, and Remazol Brilliant Blue. This work highlighted species of Pseudomonas genus as still being good sources of biocatalytically relevant enzymes.",
publisher = "MDPI, Basel",
journal = "Catalysts",
title = "Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes",
number = "7",
volume = "9",
doi = "10.3390/catal9070629"
}

Mandić, M., Đokić, L., Nikolaivits, E., Prodanović, R., O'Connor, K., Jeremić, S., Topakas, E.,& Nikodinović-Runić, J.. (2019). Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes. in Catalysts
MDPI, Basel., 9(7).
https://doi.org/10.3390/catal9070629

Mandić M, Đokić L, Nikolaivits E, Prodanović R, O'Connor K, Jeremić S, Topakas E, Nikodinović-Runić J. Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes. in Catalysts. 2019;9(7).
doi:10.3390/catal9070629 .

Mandić, Mina, Đokić, Lidija, Nikolaivits, Efstratios, Prodanović, Radivoje, O'Connor, Kevin, Jeremić, Sanja, Topakas, Evangelos, Nikodinović-Runić, Jasmina, "Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes" in Catalysts, 9, no. 7 (2019),
https://doi.org/10.3390/catal9070629 . .