Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
Samo za registrovane korisnike
2020
Autori
Simić, StefanJeremić, Sanja
Đokić, Lidija
Božić, Nataša
Vujčić, Zoran
Lončar, Nikola L.
Senthamaraikannan, Ramsankar
Babu, Ramesh P.
Opsenica, Igor
Nikodinović-Runić, Jasmina
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 °C. In addition, evidence has been provided that multicopper oxidase CueO from t...he 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.
Ključne reči:
1,4-dihydropyridines / Bacterial nanocellulose / Immobilization / Laccase / Whole-cell biocatalysisIzvor:
Enzyme and Microbial Technology, 2020, 132Finansiranje / projekti:
- Izučavanje mikrobiološkog diverziteta i karakterizacija korisnih sredinskih mikroorganizama (RS-MESTD-Basic Research (BR or ON)-173048)
- Proizvodnja, izolovanje i karakterizacija enzima i malih molekula i njihova primena u rastvornom i imobilizovanom obliku u biotehnologiji hrane, biogorivima i zaštititi životne sredine (RS-MESTD-Basic Research (BR or ON)-172048)
- Sinteza aminohinolina i njihovih derivata kao antimalarika i inhibitora botulinum neurotoksina A (RS-MESTD-Basic Research (BR or ON)-172008)
Napomena:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3357
DOI: 10.1016/j.enzmictec.2019.109411
ISSN: 0141-0229
WoS: 000504531500015
Scopus: 2-s2.0-85070994303
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Simić, Stefan AU - Jeremić, Sanja AU - Đokić, Lidija AU - Božić, Nataša AU - Vujčić, Zoran AU - Lončar, Nikola L. AU - Senthamaraikannan, Ramsankar AU - Babu, Ramesh P. AU - Opsenica, Igor AU - Nikodinović-Runić, Jasmina PY - 2020 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3356 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 °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. 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 Božić, Nataša and Vujčić, Zoran and Lončar, Nikola L. and Senthamaraikannan, Ramsankar and Babu, Ramesh P. and Opsenica, Igor 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 °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.", 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., Božić, N., Vujčić, Z., Lončar, N. L., Senthamaraikannan, R., Babu, R. P., Opsenica, I.,& 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, 132. https://doi.org/10.1016/j.enzmictec.2019.109411
Simić S, Jeremić S, Đokić L, Božić N, Vujčić Z, Lončar NL, Senthamaraikannan R, Babu RP, Opsenica I, 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, Božić, Nataša, Vujčić, Zoran, Lončar, Nikola L., Senthamaraikannan, Ramsankar, Babu, Ramesh P., Opsenica, Igor, 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 . .