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Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes
Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the productio...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7272029/ https://www.ncbi.nlm.nih.gov/pubmed/32497077 http://dx.doi.org/10.1371/journal.pone.0229968 |
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author | Sayyed, R. Z. Bhamare, H. M. Sapna, Marraiki, Najat Elgorban, Abdallah M. Syed, Asad El-Enshasy, Hesham Ali Dailin, Daniel J. |
author_facet | Sayyed, R. Z. Bhamare, H. M. Sapna, Marraiki, Najat Elgorban, Abdallah M. Syed, Asad El-Enshasy, Hesham Ali Dailin, Daniel J. |
author_sort | Sayyed, R. Z. |
collection | PubMed |
description | Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO(4) was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes. |
format | Online Article Text |
id | pubmed-7272029 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-72720292020-06-12 Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes Sayyed, R. Z. Bhamare, H. M. Sapna, Marraiki, Najat Elgorban, Abdallah M. Syed, Asad El-Enshasy, Hesham Ali Dailin, Daniel J. PLoS One Research Article Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO(4) was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system.Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes. Public Library of Science 2020-06-04 /pmc/articles/PMC7272029/ /pubmed/32497077 http://dx.doi.org/10.1371/journal.pone.0229968 Text en © 2020 Sayyed et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Sayyed, R. Z. Bhamare, H. M. Sapna, Marraiki, Najat Elgorban, Abdallah M. Syed, Asad El-Enshasy, Hesham Ali Dailin, Daniel J. Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title | Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title_full | Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title_fullStr | Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title_full_unstemmed | Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title_short | Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes |
title_sort | tree bark scrape fungus: a potential source of laccase for application in bioremediation of non-textile dyes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7272029/ https://www.ncbi.nlm.nih.gov/pubmed/32497077 http://dx.doi.org/10.1371/journal.pone.0229968 |
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