Zerva, Anastasia

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orcid::0000-0003-0361-7690
  • Zerva, Anastasia (2)
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Author's Bibliography

Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives

Milovanović, Jelena; Gunduz, Miyase Gozde; Zerva, Anastasia; Petković, Milos; Beskoski, Vladimir; Thomaidis, Nikolaos S.; Topakas, Evangelos; Nikodinović-Runić, Jasmina

(MDPI, Basel, 2021)

TY  - JOUR
AU  - Milovanović, Jelena
AU  - Gunduz, Miyase Gozde
AU  - Zerva, Anastasia
AU  - Petković, Milos
AU  - Beskoski, Vladimir
AU  - Thomaidis, Nikolaos S.
AU  - Topakas, Evangelos
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1442
AB  - We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively coloured products were detected in all biocatalytic reactions using laccase from Trametes versicolor (TvLacc), possibly due to the presence of conjugated chromophores formed in products after oxidation. The NMR assessment confirmed that the oxidation product of DHP1 was its corresponding pyridine-bearing tetrahydroquinoline derivative. Laccase from Bacillus subtillis (BacillusLacc) was the most efficient enzyme for this group of substrates using HPLC assessment. Overall, it could be concluded that DHP2 and DHP5, bearing catecholic structures, were easily oxidized by all tested laccases, while DHP3 and DHP6 containing electron-withdrawing nitro-groups are not readily oxidized by laccases. DHP4 with decahydroacridine moiety consisting of three condensed six-membered rings that contribute not only to the volume but also to the higher redox potential of the substrate rendered this compound not to be biotransformed with any of the mentioned enzymes. Overall, we showed that multiple analytical approaches are needed in order to assess biocatalytical reactions.
PB  - MDPI, Basel
T2  - Catalysts
T1  - Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives
IS  - 6
VL  - 11
DO  - 10.3390/catal11060727
ER  - 
@article{
author = "Milovanović, Jelena and Gunduz, Miyase Gozde and Zerva, Anastasia and Petković, Milos and Beskoski, Vladimir and Thomaidis, Nikolaos S. and Topakas, Evangelos and Nikodinović-Runić, Jasmina",
year = "2021",
abstract = "We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively coloured products were detected in all biocatalytic reactions using laccase from Trametes versicolor (TvLacc), possibly due to the presence of conjugated chromophores formed in products after oxidation. The NMR assessment confirmed that the oxidation product of DHP1 was its corresponding pyridine-bearing tetrahydroquinoline derivative. Laccase from Bacillus subtillis (BacillusLacc) was the most efficient enzyme for this group of substrates using HPLC assessment. Overall, it could be concluded that DHP2 and DHP5, bearing catecholic structures, were easily oxidized by all tested laccases, while DHP3 and DHP6 containing electron-withdrawing nitro-groups are not readily oxidized by laccases. DHP4 with decahydroacridine moiety consisting of three condensed six-membered rings that contribute not only to the volume but also to the higher redox potential of the substrate rendered this compound not to be biotransformed with any of the mentioned enzymes. Overall, we showed that multiple analytical approaches are needed in order to assess biocatalytical reactions.",
publisher = "MDPI, Basel",
journal = "Catalysts",
title = "Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives",
number = "6",
volume = "11",
doi = "10.3390/catal11060727"
}
Milovanović, J., Gunduz, M. G., Zerva, A., Petković, M., Beskoski, V., Thomaidis, N. S., Topakas, E.,& Nikodinović-Runić, J.. (2021). Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives. in Catalysts
MDPI, Basel., 11(6).
https://doi.org/10.3390/catal11060727
Milovanović J, Gunduz MG, Zerva A, Petković M, Beskoski V, Thomaidis NS, Topakas E, Nikodinović-Runić J. Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives. in Catalysts. 2021;11(6).
doi:10.3390/catal11060727 .
Milovanović, Jelena, Gunduz, Miyase Gozde, Zerva, Anastasia, Petković, Milos, Beskoski, Vladimir, Thomaidis, Nikolaos S., Topakas, Evangelos, Nikodinović-Runić, Jasmina, "Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives" in Catalysts, 11, no. 6 (2021),
https://doi.org/10.3390/catal11060727 . .
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Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)

Zerva, Anastasia; Simić, Stefan; Topakas, Evangelos; Nikodinović-Runić, Jasmina

(MDPI, Basel, 2019)

TY  - JOUR
AU  - Zerva, Anastasia
AU  - Simić, Stefan
AU  - Topakas, Evangelos
AU  - Nikodinović-Runić, Jasmina
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1227
AB  - There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society's increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.
PB  - MDPI, Basel
T2  - Catalysts
T1  - Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)
IS  - 12
VL  - 9
DO  - 10.3390/catal9121023
ER  - 
@article{
author = "Zerva, Anastasia and Simić, Stefan and Topakas, Evangelos and Nikodinović-Runić, Jasmina",
year = "2019",
abstract = "There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society's increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.",
publisher = "MDPI, Basel",
journal = "Catalysts",
title = "Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)",
number = "12",
volume = "9",
doi = "10.3390/catal9121023"
}
Zerva, A., Simić, S., Topakas, E.,& Nikodinović-Runić, J.. (2019). Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019). in Catalysts
MDPI, Basel., 9(12).
https://doi.org/10.3390/catal9121023
Zerva A, Simić S, Topakas E, Nikodinović-Runić J. Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019). in Catalysts. 2019;9(12).
doi:10.3390/catal9121023 .
Zerva, Anastasia, Simić, Stefan, Topakas, Evangelos, Nikodinović-Runić, Jasmina, "Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)" in Catalysts, 9, no. 12 (2019),
https://doi.org/10.3390/catal9121023 . .
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