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

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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.	pt_BR
dc.publisher.country	Brasil	pt_BR
dc.publisher.initials	UFCG	pt_BR
dc.subject.cnpq	Microbiologia.	pt_BR
dc.title	In silico and in vitro assays suggests Congo red dye degradation by a Lentinus sp. laccase enzyme.	pt_BR
dc.date.issued	2023
dc.identifier.uri	http://dspace.sti.ufcg.edu.br:8080/jspui/handle/riufcg/37515
dc.date.accessioned	2024-08-27T22:13:32Z
dc.date.available	2024-08-27
dc.date.available	2024-08-27T22:13:32Z
dc.type	Artigo de Periódico	pt_BR
dc.subject	Laccase enzyme	pt_BR
dc.subject	Lentinus sp.	pt_BR
dc.subject	Corante vermelho	pt_BR
dc.subject	Ensaio in vitro	pt_BR
dc.subject	Basidiomycete	pt_BR
dc.subject	Bioprocesses	pt_BR
dc.subject	Bioremediation	pt_BR
dc.subject	Ligninolytic enzyme	pt_BR
dc.subject	Molecular docking	pt_BR
dc.subject	Molecular dynamics	pt_BR
dc.subject	Enzima lacase	pt_BR
dc.subject	Enzima ligninolítica	pt_BR
dc.subject	Ancoragem molecular	pt_BR
dc.subject	Dinâmica molecular	pt_BR
dc.rights	Acesso Aberto	pt_BR
dc.creator	COELHO, Glauciane Danusa.
dc.creator	SILVA, Marco A.ntônio
dc.creator	PINHEIRO, Maria Alice de Melo.
dc.creator	NADVORNY, Daniela.
dc.creator	AMADOR, Vinicius Costa.
dc.creator	MAIA, Rafael Trindade.
dc.publisher	Universidade Federal de Campina Grande	pt_BR
dc.language	eng	pt_BR
dc.title.alternative	Ensaios in silico e in vitro sugerem degradação do corante vermelho Congo por uma enzima lacase Lentinus sp.	pt_BR
dc.identifier.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	pt_BR