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

• 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
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2019.109411

[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.