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Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator

A multicopper oxidase (IOX) produced by Iodidimonas sp. Q-1 has high catalytic efficiency for iodide (I(−)) oxidation to form molecular iodine (I(2)). In this study, the potential capacity of IOX for decolorization of recalcitrant dyes was determined. Although IOX did not decolorize any dyes in the...

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Autores principales: Taguchi, Taro, Ebihara, Kyota, Yanagisaki, Chihiro, Yoshikawa, Jun, Horiguchi, Hirofumi, Amachi, Seigo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928188/
https://www.ncbi.nlm.nih.gov/pubmed/29712927
http://dx.doi.org/10.1038/s41598-018-25043-1
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author Taguchi, Taro
Ebihara, Kyota
Yanagisaki, Chihiro
Yoshikawa, Jun
Horiguchi, Hirofumi
Amachi, Seigo
author_facet Taguchi, Taro
Ebihara, Kyota
Yanagisaki, Chihiro
Yoshikawa, Jun
Horiguchi, Hirofumi
Amachi, Seigo
author_sort Taguchi, Taro
collection PubMed
description A multicopper oxidase (IOX) produced by Iodidimonas sp. Q-1 has high catalytic efficiency for iodide (I(−)) oxidation to form molecular iodine (I(2)). In this study, the potential capacity of IOX for decolorization of recalcitrant dyes was determined. Although IOX did not decolorize any dyes in the absence of redox mediator, significant decolorization of Orange G, Indigo Carmine, Amido Black, and Remazol Brilliant Blue R (RBBR) was observed in the presence of iodide. Addition of 0.1 mM iodide was sufficient to decolorize a total of 3 mM Indigo Carmine, suggesting that iodide functions as a mediator. Such mediator-like function of iodide was not observed in commercially available fungal laccases. The IOX-iodide decolorization system showed much alkaline pH optima of 5.5–6.5 and stronger salt tolerance than fungal laccases did. In addition, actual wastewater discharged from a dyeing factory could be decolorized more than 50% by the system. Since iodide is naturally occurring, non-toxic, and cheaper than common synthetic mediators, the IOX-iodide system is potentially more advantageous than fungal laccase-mediator systems for decolorization of recalcitrant dyes.
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spelling pubmed-59281882018-05-07 Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator Taguchi, Taro Ebihara, Kyota Yanagisaki, Chihiro Yoshikawa, Jun Horiguchi, Hirofumi Amachi, Seigo Sci Rep Article A multicopper oxidase (IOX) produced by Iodidimonas sp. Q-1 has high catalytic efficiency for iodide (I(−)) oxidation to form molecular iodine (I(2)). In this study, the potential capacity of IOX for decolorization of recalcitrant dyes was determined. Although IOX did not decolorize any dyes in the absence of redox mediator, significant decolorization of Orange G, Indigo Carmine, Amido Black, and Remazol Brilliant Blue R (RBBR) was observed in the presence of iodide. Addition of 0.1 mM iodide was sufficient to decolorize a total of 3 mM Indigo Carmine, suggesting that iodide functions as a mediator. Such mediator-like function of iodide was not observed in commercially available fungal laccases. The IOX-iodide decolorization system showed much alkaline pH optima of 5.5–6.5 and stronger salt tolerance than fungal laccases did. In addition, actual wastewater discharged from a dyeing factory could be decolorized more than 50% by the system. Since iodide is naturally occurring, non-toxic, and cheaper than common synthetic mediators, the IOX-iodide system is potentially more advantageous than fungal laccase-mediator systems for decolorization of recalcitrant dyes. Nature Publishing Group UK 2018-04-30 /pmc/articles/PMC5928188/ /pubmed/29712927 http://dx.doi.org/10.1038/s41598-018-25043-1 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Taguchi, Taro
Ebihara, Kyota
Yanagisaki, Chihiro
Yoshikawa, Jun
Horiguchi, Hirofumi
Amachi, Seigo
Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title_full Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title_fullStr Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title_full_unstemmed Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title_short Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator
title_sort decolorization of recalcitrant dyes by a multicopper oxidase produced by iodidimonas sp. q-1 with iodide as a novel inorganic natural redox mediator
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928188/
https://www.ncbi.nlm.nih.gov/pubmed/29712927
http://dx.doi.org/10.1038/s41598-018-25043-1
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