Sulphonated azo dye decolorization by Alcaligenes faecalis subsp. phenolicus MB207: Insights from laboratory and computational analysis.
Azo dyes
Bacteria
Bioremediation
Congo red
Methyl orange
Molecular docking
Journal
Biophysical chemistry
ISSN: 1873-4200
Titre abrégé: Biophys Chem
Pays: Netherlands
ID NLM: 0403171
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
received:
01
01
2022
revised:
14
03
2022
accepted:
20
03
2022
pubmed:
10
4
2022
medline:
7
6
2022
entrez:
9
4
2022
Statut:
ppublish
Résumé
Microbial decolorization of azo dyes, mediated by an enzymatic mechanism is an intricate cost-effective, and eco-friendly treatment method of genotoxic azo pollutants. Scientists are on the constant lookout for microbes, enzymes, and mechanisms that could aid remediation of the environment at a fast pace. Alcaligenes faecalis subsp. phenolicus MB207 is one such bacteria, consisting of azoreductase (AzoR) and laccase/multicopper oxidase enzyme responsible for sulphonated mono-azo dye (Methyl orange) and di-azo dye (Congo red) degradation. AzoR degrades dyes by a ping-pong setup while multicopper oxidase achieves this through a non-specified radical approach. We have coupled experimental analysis with bioinformatics for deciphering intricacies of this procedure in tiny scale enzymatic machines of this biotope. The degradation assays were followed by molecular docking of the enzyme-substrate complexes. Key anchoring bonds were detected and mapped H-bonding, electron exchange, ionic interactions, as well as hydrophobic interactions, provided insights into dye-enzyme and NADH-enzyme binding. This study establishes a foundation of the molecular basis of dye interaction with azoR and multicopper oxidase in A. facealis subsp. phenolicus MB207.
Identifiants
pubmed: 35397247
pii: S0301-4622(22)00048-5
doi: 10.1016/j.bpc.2022.106806
pii:
doi:
Substances chimiques
Amlodipine Besylate, Olmesartan Medoxomil Drug Combination
0
Azo Compounds
0
Coloring Agents
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
106806Informations de copyright
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