Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
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2020
Authors
Simić, StefanJeremić, Sanja
Đokić, Lidija
Bozić, Nataša
Vujcić, Zoran
Loncar, Nikola
Senthamaraikannan, Ramsankar
Babu, Ramesh
Opsenica, Igor M.
Nikodinović-Runić, Jasmina
Article (Published version)
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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.
Keywords:
Whole-cell biocatalysis / Laccase / Immobilization / Bacterial nanocellulose / 1,4-dihydropyridinesSource:
Enzyme and Microbial Technology, 2020, 132Publisher:
- New York : Elsevier Science Inc
Funding / projects:
- Microbial diversity study and characterization of beneficial environmental microorganisms (RS-MESTD-Basic Research (BR or ON)-173048)
- Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-MESTD-Basic Research (BR or ON)-172048)
- The synthesis of aminoquinoline-based antimalarials and botulinum neurotoxin A inhibitors (RS-MESTD-Basic Research (BR or ON)-172008)
DOI: 10.1016/j.enzmictec.2019.109411
ISSN: 0141-0229
PubMed: 31731971
WoS: 000504531500015
Scopus: 2-s2.0-85070994303
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Institution/Community
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .