Elucidating the bioremediation potential of laccase and peroxidase enzymes from Bacillus ligniniphilus L1 in antibiotic degradation: A computationally guided study

Bioresour Technol. 2024 Dec:413:131520. doi: 10.1016/j.biortech.2024.131520. Epub 2024 Sep 23.

Abstract

This study showcased the antibiotic degradation abilities of laccase and catalase-peroxidase from Bacillus ligniniphilus L1, an extremophile, against 18 common antibiotics using computationally guided approach. Molecular docking and simulation identified six enzyme-antibiotic complexes for laccase and four for catalase-peroxidase, demonstrating significant binding affinity and stability. Enzyme activity assays corroborated computational results, indicating both enzymes could degrade all tested antibiotics with varying efficiencies. L1 laccase outperformed commercial laccase against five antibiotics, notably vancomycin, levofloxacin, tobramycin, linezolid, and rifamycin, with enhanced degradation potential upon ABTS addition. Catalase-peroxidase from L1 exhibited superior degradation efficiency over commercial peroxidase against vancomycin, linezolid, tobramycin, and clindamycin. Overall, this study underscores the computational approach's utility in understanding enzyme-mediated antibiotic degradation, offering insights into environmental contaminant remediation.

Keywords: Biodegradation; Extremozymes; Molecular docking; Molecular dynamic simulations.

MeSH terms

  • Anti-Bacterial Agents* / metabolism
  • Bacillus* / enzymology
  • Biodegradation, Environmental*
  • Laccase* / chemistry
  • Laccase* / metabolism
  • Molecular Docking Simulation*
  • Peroxidase / metabolism
  • Peroxidases / metabolism

Substances

  • Laccase
  • Anti-Bacterial Agents
  • Peroxidase
  • Peroxidases