Structural study and molecular docking insights into laccase-mediated dye degradation

Industrial wastewater often contains harmful dyes, posing significant environmental challenges. This study used computational tools to investigate the interactions between the low-degradability Azo dye, Reactive Blue 19, and laccase enzyme from two fungi species, Lentinus sp. WR2 and Trametes versic...

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Main Authors: Yatindra Kumar, Hirdya Ramesh, Kalpana Dhabade, Manju Shahare, Bhawna Kalra
Format: Article
Language:English
Published: Elsevier 2024-12-01
Series:Sustainable Chemistry for the Environment
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Online Access:http://www.sciencedirect.com/science/article/pii/S2949839224001184
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author Yatindra Kumar
Hirdya Ramesh
Kalpana Dhabade
Manju Shahare
Bhawna Kalra
author_facet Yatindra Kumar
Hirdya Ramesh
Kalpana Dhabade
Manju Shahare
Bhawna Kalra
author_sort Yatindra Kumar
collection DOAJ
description Industrial wastewater often contains harmful dyes, posing significant environmental challenges. This study used computational tools to investigate the interactions between the low-degradability Azo dye, Reactive Blue 19, and laccase enzyme from two fungi species, Lentinus sp. WR2 and Trametes versicolor, as well as the protein Xyn5B (GH30) from Bacillus sp. BP7. Physiochemical characterization indicated acidic properties for Lentinus sp. WR2 and T. versicolor, while basic characteristics for Bacillus sp. BP7. Secondary structure (SOPMA analysis) revealed that most laccases had random coiling, enhancing protein flexibility. The negative GRAVY index revealed favorable water interaction for Lentinus sp. WR2 and Bacillus sp. BP7. The ERRAT plot validated the laccase 3D structure. The molecular docking results were compared using active site prediction and docking score. Lentinus sp. WR2 is linked with Reactive Blue 19 through a single residual amino acid THR 168; T. versicolor is linked through GLY 101, TRP 98, and TRP 512; and Bacillus sp. BP7 exhibited four linkages: VAL 262, TYR 263, TRP 117, and THR 260. The molecular docking results showed that Xyn5B demonstrated laccase activity and bound effectively with Reactive Blue 19, outperforming a commonly used fungal laccase in dye degradation. These findings enhance our understanding of enzyme-substrate interactions and highlight the potential of Xyn5B in eco-friendly dye degradation.
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spelling doaj-art-113a1d64aec0474d97cb0070338b0a362025-08-20T02:30:39ZengElsevierSustainable Chemistry for the Environment2949-83922024-12-01810017510.1016/j.scenv.2024.100175Structural study and molecular docking insights into laccase-mediated dye degradationYatindra Kumar0Hirdya Ramesh1Kalpana Dhabade2Manju Shahare3Bhawna Kalra4Department of Life Sciences and Biotechnology, Chhatrapati Shivaji Maharaj University, Panvel, Navi Mumbai, Maharashtra 410206, IndiaDepartment of Life Sciences and Biotechnology, Chhatrapati Shivaji Maharaj University, Panvel, Navi Mumbai, Maharashtra 410206, IndiaDepartment of Life Sciences and Biotechnology, Chhatrapati Shivaji Maharaj University, Panvel, Navi Mumbai, Maharashtra 410206, IndiaDepartment of Life Sciences and Biotechnology, Chhatrapati Shivaji Maharaj University, Panvel, Navi Mumbai, Maharashtra 410206, IndiaDepartment of Genetics and Plant Breeding, FASC, SGT University, Budhera, Gurugram, Haryana 122505, India; Corresponding author.Industrial wastewater often contains harmful dyes, posing significant environmental challenges. This study used computational tools to investigate the interactions between the low-degradability Azo dye, Reactive Blue 19, and laccase enzyme from two fungi species, Lentinus sp. WR2 and Trametes versicolor, as well as the protein Xyn5B (GH30) from Bacillus sp. BP7. Physiochemical characterization indicated acidic properties for Lentinus sp. WR2 and T. versicolor, while basic characteristics for Bacillus sp. BP7. Secondary structure (SOPMA analysis) revealed that most laccases had random coiling, enhancing protein flexibility. The negative GRAVY index revealed favorable water interaction for Lentinus sp. WR2 and Bacillus sp. BP7. The ERRAT plot validated the laccase 3D structure. The molecular docking results were compared using active site prediction and docking score. Lentinus sp. WR2 is linked with Reactive Blue 19 through a single residual amino acid THR 168; T. versicolor is linked through GLY 101, TRP 98, and TRP 512; and Bacillus sp. BP7 exhibited four linkages: VAL 262, TYR 263, TRP 117, and THR 260. The molecular docking results showed that Xyn5B demonstrated laccase activity and bound effectively with Reactive Blue 19, outperforming a commonly used fungal laccase in dye degradation. These findings enhance our understanding of enzyme-substrate interactions and highlight the potential of Xyn5B in eco-friendly dye degradation.http://www.sciencedirect.com/science/article/pii/S2949839224001184LaccaseReactive blue 19Lentinus sp. WR2Trametes versicolorBacillus sp. BP7Molecular docking
spellingShingle Yatindra Kumar
Hirdya Ramesh
Kalpana Dhabade
Manju Shahare
Bhawna Kalra
Structural study and molecular docking insights into laccase-mediated dye degradation
Sustainable Chemistry for the Environment
Laccase
Reactive blue 19
Lentinus sp. WR2
Trametes versicolor
Bacillus sp. BP7
Molecular docking
title Structural study and molecular docking insights into laccase-mediated dye degradation
title_full Structural study and molecular docking insights into laccase-mediated dye degradation
title_fullStr Structural study and molecular docking insights into laccase-mediated dye degradation
title_full_unstemmed Structural study and molecular docking insights into laccase-mediated dye degradation
title_short Structural study and molecular docking insights into laccase-mediated dye degradation
title_sort structural study and molecular docking insights into laccase mediated dye degradation
topic Laccase
Reactive blue 19
Lentinus sp. WR2
Trametes versicolor
Bacillus sp. BP7
Molecular docking
url http://www.sciencedirect.com/science/article/pii/S2949839224001184
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AT hirdyaramesh structuralstudyandmoleculardockinginsightsintolaccasemediateddyedegradation
AT kalpanadhabade structuralstudyandmoleculardockinginsightsintolaccasemediateddyedegradation
AT manjushahare structuralstudyandmoleculardockinginsightsintolaccasemediateddyedegradation
AT bhawnakalra structuralstudyandmoleculardockinginsightsintolaccasemediateddyedegradation