Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines

[Display omitted] •Bacillus laccase and whole-cells expressing it oxidized selected 1,4-dihydropyridines.•Whole-cell biocatalyst was stable after 1-month storage at 4 °C.•Multicopper oxidase CueO from the expression host enhanced the oxidation activity.•Laccase based biocatalysts were immobilized on...

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Published in:Enzyme and microbial technology 2020-01, Vol.132, p.109411-109411, Article 109411
Main Authors: Simić, Stefan, Jeremic, Sanja, Djokic, Lidija, Božić, Nataša, Vujčić, Zoran, Lončar, Nikola, Senthamaraikannan, Ramsankar, Babu, Ramesh, Opsenica, Igor M., Nikodinovic-Runic, Jasmina
Format: Article
Language:English
Subjects:
1,4-dihydropyridines
Bacillus - enzymology
Bacterial nanocellulose
Biocatalysis
Dihydropyridines - metabolism
Enzymes, Immobilized - metabolism
Hydrogen-Ion Concentration
Immobilization
Laccase
Laccase - metabolism
Oxidation-Reduction
Temperature
Whole-cell biocatalysis
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Summary:[Display omitted] •Bacillus laccase and whole-cells expressing it oxidized selected 1,4-dihydropyridines.•Whole-cell biocatalyst was stable after 1-month storage at 4 °C.•Multicopper oxidase CueO from the expression host enhanced the oxidation activity.•Laccase based biocatalysts were immobilized on bacterial nanocellulose. 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.
ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2019.109411