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Article

Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT

by
Jorge Sánchez-SanMartín
2,
Sebastián L. Márquez
2,
Giannina Espina
2,*,
Rodrigo Cortés-Antiquera
1,
Junsong Sun
3 and
Jenny M. Blamey
1,2,*
1
Facultad de Química y Biología, Universidad de Santiago de Chile, Alameda 3363, Santiago 9170022, Chile
2
Fundación Biociencia, José Domingo Cañas 2280, Santiago 7750132, Chile
3
Green Chemical Engineering Technology R&D Center, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Haike Road 99, Shanghai 201210, China
*
Authors to whom correspondence should be addressed.
Biomolecules 2024, 14(3), 369; https://doi.org/10.3390/biom14030369
Submission received: 20 February 2024 / Revised: 10 March 2024 / Accepted: 11 March 2024 / Published: 19 March 2024
(This article belongs to the Special Issue Recent Advances in Laccases and Laccase-Based Bioproducts)

Abstract

Laccases are industrially relevant enzymes that have gained great biotechnological importance. To date, most are of fungal and mesophilic origin; however, enzymes from extremophiles possess an even greater potential to withstand industrial conditions. In this study, we evaluate the potential of a recombinant spore-coat laccase from the thermoalkaliphilic bacterium Bacillus sp. FNT (FNTL) to biodegrade antibiotics from the tetracycline, β-lactams, and fluoroquinolone families. This extremozyme was previously characterized as being thermostable and highly active in a wide range of temperatures (20–90 °C) and very versatile towards several structurally different substrates, including recalcitrant environmental pollutants such as PAHs and synthetic dyes. First, molecular docking analyses were employed for initial ligand affinity screening in the modeled active site of FNTL. Then, the in silico findings were experimentally tested with four highly consumed antibiotics, representatives of each family: tetracycline, oxytetracycline, amoxicillin, and ciprofloxacin. HPLC results indicate that FNTL with help of the natural redox mediator acetosyringone, can efficiently biodegrade 91, 90, and 82% of tetracycline (0.5 mg mL−1) in 24 h at 40, 30, and 20 °C, respectively, with no apparent ecotoxicity of the products on E. coli and B. subtilis. These results complement our previous studies, highlighting the potential of this extremozyme for application in wastewater bioremediation.
Keywords: wastewater bioremediation; pharmaceutical pollutants; antibiotics; tetracyclines; fluoroquinolone; β-lactam; docking; extremozyme; oxidoreductase; spore-coat laccase wastewater bioremediation; pharmaceutical pollutants; antibiotics; tetracyclines; fluoroquinolone; β-lactam; docking; extremozyme; oxidoreductase; spore-coat laccase

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MDPI and ACS Style

Sánchez-SanMartín, J.; Márquez, S.L.; Espina, G.; Cortés-Antiquera, R.; Sun, J.; Blamey, J.M. Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT. Biomolecules 2024, 14, 369. https://doi.org/10.3390/biom14030369

AMA Style

Sánchez-SanMartín J, Márquez SL, Espina G, Cortés-Antiquera R, Sun J, Blamey JM. Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT. Biomolecules. 2024; 14(3):369. https://doi.org/10.3390/biom14030369

Chicago/Turabian Style

Sánchez-SanMartín, Jorge, Sebastián L. Márquez, Giannina Espina, Rodrigo Cortés-Antiquera, Junsong Sun, and Jenny M. Blamey. 2024. "Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT" Biomolecules 14, no. 3: 369. https://doi.org/10.3390/biom14030369

APA Style

Sánchez-SanMartín, J., Márquez, S. L., Espina, G., Cortés-Antiquera, R., Sun, J., & Blamey, J. M. (2024). Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic Bacterium Bacillus sp. FNT. Biomolecules, 14(3), 369. https://doi.org/10.3390/biom14030369

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