Izvorni znanstveni članak

https://doi.org/10.2478/aiht-2026-77-4001

Potential of Bacillus paramycoides hydrolase to degrade propiconazole

Muhammad Naveed ; University of Central Punjab Faculty of Science and Technology, Department of Biotechnology, Lahore, Pakistan 2 Jiangsu University, Biofuels Institute; School of the Environment and Safety Engineering, Zhenjiang, China
Maida Salah Ud Din ; University of Central Punjab Faculty of Science and Technology, Department of Biotechnology, Lahore, Pakistan
Tariq Aziz orcid.org/0000-0003-0905-8076 ; University of Ioannina Arta, Department of Agriculture, Laboratory of Animal Health, Hygiene and Food Quality, Arta, Greece
Rida Naveed orcid.org/0000-0002-2440-4187 ; University of Central Punjab Faculty of Science and Technology, Department of Biotechnology, Lahore, Pakistan
Daochen Zhu ; Jiangsu University, Biofuels Institute; School of the Environment and Safety Engineering, Zhenjiang, China
Maha Alharbi ; Princess Nourah bint Abdulrahman University College of Science, Department of Biology, Riyadh, Saudi Arabia
Ashwag Shami ; Princess Nourah bint Abdulrahman University College of Science, Department of Biology, Riyadh, Saudi Arabia

Sažetak

Propiconazole is a widely used synthetic fungicide that has raised deep environmental and toxicological concerns due to its persistence and bioactivity. In this study, we investigated the potential of a facultative anaerobic, Gram-positive, rod-shaped bacterium, Bacillus paramycoides to degrade propiconazole by elucidating the functional role of its hydrolase enzyme in silico. The hydrolase was characterized with the FASTA sequence to determine its physicochemical properties, stability, and conserved functional domains. Homology modelling was performed and the predicted structure validated using a Ramachandran plot and ERRAT analysis, yielding an overall quality score of 93.6 %. Eleven propiconazole-related compounds, including parent molecules and degradation products (e.g. hispor, propiconazole TP1, propiconazole TP2, and propiconazole-d7) were retrieved from the PubChem database and subjected to molecular docking using PyRx. Docking analysis revealed stable enzyme-substrate interactions, with the highest binding affinity of -6.8 kcal/mol observed for native hydrolase complexes. Site-directed mutagenesis was subsequently performed, and mutant structures were evaluated for structural stability and functional integrity. The mutated hydrolase exhibited an improved binding affinity of -7.4 kcal/mol, indicating enhanced substrate interaction. Molecular dynamics simulations using the AMBER force field further confirmed the structural stability, binding consistency, and functional reliability of the enzyme-ligand complexes. Overall, these quantitative findings support the potential of B. paramycoides hydrolase as a stable, non-virulent, and efficient candidate for environmentally sustainable bioremediation of propiconazole, with relevance to environmental and occupational toxicology.

Ključne riječi

bioremediation; environmental toxicology; hydrolase enzymes; molecular docking; propiconazole degradation

Hrčak ID:

345665

URI

https://hrcak.srce.hr/345665

Datum izdavanja:

23.3.2026.

Podaci na drugim jezicima: hrvatski

Posjeta: 217 *