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

Authors: Stefan Simić; Sanja Jeremic; Lidija Djokic; Nataša Božić; Zoran Vujčić; Nikola Lončar; Ramsankar Senthamaraikannan; +3 Authors

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

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.

Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3357]

Countries
Serbia, Serbia, Netherlands
Subjects by Vocabulary

Microsoft Academic Graph classification: Multicopper oxidase medicine.disease_cause Biotransformation medicine Bacillus licheniformis Escherichia coli Trametes versicolor Laccase biology Chemistry Substrate (chemistry) biology.organism_classification Combinatorial chemistry Biocatalysis

Keywords

HANTZSCH 1,4-DIHYDROPYRIDINES, Dihydropyridines, 1, Bacillus, Bioengineering, Applied Microbiology and Biotechnology, Biochemistry, BACILLUS-LICHENIFORMIS, Immobilization, AROMATIZATION, HANTZSCH 1, 1,4-dihydropyridines, 4-DIHYDROPYRIDINES, MULTICOPPER OXIDASE, Whole-cell biocatalysis, DERIVATIVES, Laccase, Temperature, AMINES, Hydrogen-Ion Concentration, Enzymes, Immobilized, ONE-POT SYNTHESIS, Bacterial nanocellulose, CELLULOSE, Biocatalysis, NANOCELLULOSE, Oxidation-Reduction, Biotechnology

61 references, page 1 of 7

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
views
OpenAIRE UsageCountsViews provided by UsageCounts
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