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In silico and in vitro assays suggests Congo red dye degradation by a Lentinus sp. laccase enzyme.
Coelho, Glauciane Danusa; Silva, Marco Antônio; de Melo Pinheiro, Maria Alice; Nadvorny, Daniela; Costa Amador, Vinicius; Maia, Rafael Trindade.
Afiliación
  • Coelho GD; Center for Sustainable Development of the Semi-Arid, Academic Unit of Biotechnology Engineering, Federal University of Campina Grande, Sumé, Paraiba, Brazil.
  • Silva MA; Center for Water Resources and Environmental Studies, University of São Paulo, São Carlos School of Engineering, São Carlos, São Paulo, Brazil.
  • de Melo Pinheiro MA; Post-Graduation in Materials Sciences, Center for Exact and Natural Sciences, Federal University of Pernambuco, Recife, Pernambuco, Brazil.
  • Nadvorny D; Department of Pharmaceutical Sciences, Federal University of Pernambuco, Recife, Pernambuco, Brazil.
  • Costa Amador V; Post-Graduation in Biological Science, Federal University of Pernambuco, Recife, Pernambuco, Brazil.
  • Maia RT; Center for Sustainable Development of the Semi-Arid, Academic Unit of Biotechnology Engineering, Federal University of Campina Grande, Sumé, Paraiba, Brazil.
J Biomol Struct Dyn ; 42(7): 3802-3813, 2024 Apr.
Article en En | MEDLINE | ID: mdl-37254291
Laccase 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 vitro and in silico studies 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 vitro discoloration was carried out using experimental design 22 at 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-1 with 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-1 and 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 vitro in agreement with the in silico simulations that demonstrate the enzyme potential.Communicated by Ramaswamy H. Sarma.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Rojo Congo / Lentinula Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Rojo Congo / Lentinula Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido