In silico and in vitro assays suggests Congo red dye degradation by a Lentinus sp. laccase enzyme.

Please use this identifier to cite or link to this item: http://dspace.sti.ufcg.edu.br:8080/jspui/handle/riufcg/37515

Title:	In silico and in vitro assays suggests Congo red dye degradation by a Lentinus sp. laccase enzyme.
Other Titles:	Ensaios in silico e in vitro sugerem degradação do corante vermelho Congo por uma enzima lacase Lentinus sp.
???metadata.dc.creator???:	COELHO, Glauciane Danusa. SILVA, Marco A.ntônio PINHEIRO, Maria Alice de Melo. NADVORNY, Daniela. AMADOR, Vinicius Costa. MAIA, Rafael Trindade.
Keywords:	Laccase enzyme;Lentinus sp.;Corante vermelho;Ensaio in vitro;Basidiomycete;Bioprocesses;Bioremediation;Ligninolytic enzyme;Molecular docking;Molecular dynamics;Enzima lacase;Enzima ligninolítica;Ancoragem molecular;Dinâmica molecular
Issue Date:	2023
Publisher:	Universidade Federal de Campina Grande
Citation:	COELHO, Glauciane Danusa; SILVA, Marco Antônio; PINHEIRO, Maria Alice de Melo; NADVORNY, Daniela; AMADOR, Vinicius Costa; MAIA, Rafael Trindade. In silico and in vitro assays suggests Congo red dye degradation by a Lentinus sp. laccase enzyme. Journal of Biomolecular Structure & Dynamics, v. 40, p. 1-12, 2023. Disponível em: http://dspace.sti.ufcg.edu.br:8080/jspui/handle/riufcg/37515
???metadata.dc.description.resumo???:	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 €A) 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.
Keywords:	Laccase enzyme Lentinus sp. Corante vermelho Ensaio in vitro Basidiomycete Bioprocesses Bioremediation Ligninolytic enzyme Molecular docking Molecular dynamics Enzima lacase Enzima ligninolítica Ancoragem molecular Dinâmica molecular
???metadata.dc.subject.cnpq???:	Microbiologia.
URI:	http://dspace.sti.ufcg.edu.br:8080/jspui/handle/riufcg/37515
Appears in Collections:	Artigos Científicos - CDSA

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