Elucidation of the decolorization of Congo Red by Trametes versicolor laccase in presence of ABTS through cyclic voltammetry.


Journal

Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761

Informations de publication

Date de publication:
Apr 2020
Historique:
received: 20 06 2019
revised: 23 12 2019
accepted: 31 12 2019
entrez: 10 3 2020
pubmed: 10 3 2020
medline: 2 10 2020
Statut: ppublish

Résumé

The azo dye Congo red is heavily used in textile industries and is actively present in the wastewater run-offs. Its structural complexity and physical characteristics make it resistant to the physicochemical treatments employed by the industry. Over time, application of the enzyme laccase has proved to be quite useful due to its ability to oxidize and eventually decolorize the dye. Moreover, the use of ABTS as the electron mediator also helps in enhancing the oxidizing capability of the enzyme with congo red. The present study involves establishing the role of the individual components i.e. laccase, ABTS and the dye, in the LMS electrochemically. Congo red doesn't have any form of electrochemical activity by itself, but the enzyme brings about a substantial change by increasing the rate of reduction. The effect of ABTS, though same, is concentration-dependent. For LMS, laccase helps in bringing about the rate of reduction much faster in the presence of the mediator, initiating the decolorization of the dye.

Identifiants

pubmed: 32146934
pii: S0141-0229(19)30245-5
doi: 10.1016/j.enzmictec.2019.109507
pii:
doi:

Substances chimiques

Azo Compounds 0
Benzothiazoles 0
Fungal Proteins 0
Sulfonic Acids 0
2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid 28752-68-3
Congo Red 3U05FHG59S
Laccase EC 1.10.3.2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

109507

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Auteurs

Rituparna Saha (R)

Department of Biotechnology, JIS University, Agarpara, West Bengal 700109, India; Department of Biochemistry, University of Calcutta, Ballygunge, West Bengal 700019, India.

Mainak Mukhopadhyay (M)

Department of Biotechnology, JIS University, Agarpara, West Bengal 700109, India. Electronic address: mainak.mukhopadhyay12@gmail.com.

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Classifications MeSH