Loncar, Nikola

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orcid::0000-0002-3420-973X
  • Loncar, Nikola (1)
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Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines

Simić, Stefan; Jeremić, Sanja; Đokić, Lidija; Bozić, Nataša; Vujcić, Zoran; Loncar, Nikola; Senthamaraikannan, Ramsankar; Babu, Ramesh; Opsenica, Igor M.; Nikodinović-Runić, Jasmina

(New York : Elsevier Science Inc, 2020)

TY  - JOUR
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Bozić, Nataša
AU  - Vujcić, Zoran
AU  - Loncar, Nikola
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh
AU  - Opsenica, Igor M.
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1406
AB  - Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7-24 h with good yields (70-99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 degrees C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.
PB  - New York : Elsevier Science Inc
T2  - Enzyme and Microbial Technology
T1  - Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
VL  - 132
DO  - 10.1016/j.enzmictec.2019.109411
ER  - 
@article{
author = "Simić, Stefan and Jeremić, Sanja and Đokić, Lidija and Bozić, Nataša and Vujcić, Zoran and Loncar, Nikola and Senthamaraikannan, Ramsankar and Babu, Ramesh and Opsenica, Igor M. and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7-24 h with good yields (70-99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 degrees C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.",
publisher = "New York : Elsevier Science Inc",
journal = "Enzyme and Microbial Technology",
title = "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines",
volume = "132",
doi = "10.1016/j.enzmictec.2019.109411"
}
Simić, S., Jeremić, S., Đokić, L., Bozić, N., Vujcić, Z., Loncar, N., Senthamaraikannan, R., Babu, R., Opsenica, I. M.,& Nikodinović-Runić, J.. (2020). Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology
New York : Elsevier Science Inc., 132.
https://doi.org/10.1016/j.enzmictec.2019.109411
Simić S, Jeremić S, Đokić L, Bozić N, Vujcić Z, Loncar N, Senthamaraikannan R, Babu R, Opsenica IM, Nikodinović-Runić J. Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology. 2020;132.
doi:10.1016/j.enzmictec.2019.109411 .
Simić, Stefan, Jeremić, Sanja, Đokić, Lidija, Bozić, Nataša, Vujcić, Zoran, Loncar, Nikola, Senthamaraikannan, Ramsankar, Babu, Ramesh, Opsenica, Igor M., Nikodinović-Runić, Jasmina, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" in Enzyme and Microbial Technology, 132 (2020),
https://doi.org/10.1016/j.enzmictec.2019.109411 . .
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