| Autor: |
Coelho, Glauciane Danusa, Silva, Marco Antônio, de Melo Pinheiro, Maria Alice, Nadvorny, Daniela, Costa Amador, Vinicius, Maia, Rafael Trindade |
| Zdroj: |
Journal of Biomolecular Structure and Dynamics; May 2024, Vol. 42 Issue: 7 p3802-3813, 12p |
| Abstrakt: |
AbstractLaccase is a superfamily of ligninolytic enzymes known to degrade a wide variety of xenobiotics, including synthetic dyes. Congo Red (CR) has a diazo dye function, carcinogenic and mutagenic potential, and is currently applied in clinical analysis. The objective of this work was to produce and characterize the crude extract of Lentinus sp. in semi-solid fermentation (FSS) and perform in vitroand in silicostudies to assess the potential of the crude extract to discolor the CR dye. Laccase activity was determined using ABTS as substrate and characterized. The in vitrodiscoloration was carried out using experimental design 22at room temperature and monitored at 340 nm for 24h. Molecular docking and molecular dynamics simulations were performed between laccase and CR. The maximum laccase activity production was 29.63 U L−1with six days of FSS. The optimal temperature and pH were 50 °C and 3.0, respectively. Discoloration of the CR dye was obtained only in tests containing CuSO4. Laccase formed stable complexes with the dye, presenting negative binding energy values ranging from −70.94 to −63.16 kcal mol−1and the occurrence of seven hydrogen bonds. Molecular dynamics results showed the stability of the system (RMSD ranging from 1.0 to 2.5 Ä) and protein-ligand interaction along simulation. RMSF values pointed residues at the end of chains A (residues 300 to 305, 480 to 500) and B (residues 650 to 655 and 950 to 1000) as the most flexible regions of the laccase. This study highlighted the enzymatic action in the bioremediation of CR in vitroin agreement with the in silicosimulations that demonstrate the enzyme potential.Communicated by Ramaswamy H. Sarma |
| Databáze: |
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