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A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye
A novel extracellular laccase enzyme produced from Spirulina platensis CFTRI was purified by ultrafiltration, cold acetone precipitation, anion exchange and size exclusion chromatography with 51.5% recovery and 5.8 purification fold. The purified laccase was a monomeric protein with molecular mass o...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5383238/ https://www.ncbi.nlm.nih.gov/pubmed/28384218 http://dx.doi.org/10.1371/journal.pone.0175144 |
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author | Afreen, Sumbul Shamsi, Tooba Naz Baig, Mohd Affan Ahmad, Nadeem Fatima, Sadaf Qureshi, M. Irfan Hassan, Md. Imtaiyaz Fatma, Tasneem |
author_facet | Afreen, Sumbul Shamsi, Tooba Naz Baig, Mohd Affan Ahmad, Nadeem Fatima, Sadaf Qureshi, M. Irfan Hassan, Md. Imtaiyaz Fatma, Tasneem |
author_sort | Afreen, Sumbul |
collection | PubMed |
description | A novel extracellular laccase enzyme produced from Spirulina platensis CFTRI was purified by ultrafiltration, cold acetone precipitation, anion exchange and size exclusion chromatography with 51.5% recovery and 5.8 purification fold. The purified laccase was a monomeric protein with molecular mass of ~66 kDa that was confirmed by zymogram analysis and peptide mass fingerprinting. The optimum pH and temperature of the enzyme activity was found at 3.0 and 30°C using ABTS as substrate but the enzyme was quite stable at high temperature and alkaline pH. The laccase activity was enhanced by Cu+2, Zn+2 and Mn+2. In addition, the dye decolorization potential of purified laccase was much higher in terms of extent as well as time. The purified laccase decolorized (96%) of anthraquinonic dye Reactive blue- 4 within 4 h and its biodegradation studies was monitored by UV visible spectra, FTIR and HPLC which concluded that cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. |
format | Online Article Text |
id | pubmed-5383238 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-53832382017-05-03 A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye Afreen, Sumbul Shamsi, Tooba Naz Baig, Mohd Affan Ahmad, Nadeem Fatima, Sadaf Qureshi, M. Irfan Hassan, Md. Imtaiyaz Fatma, Tasneem PLoS One Research Article A novel extracellular laccase enzyme produced from Spirulina platensis CFTRI was purified by ultrafiltration, cold acetone precipitation, anion exchange and size exclusion chromatography with 51.5% recovery and 5.8 purification fold. The purified laccase was a monomeric protein with molecular mass of ~66 kDa that was confirmed by zymogram analysis and peptide mass fingerprinting. The optimum pH and temperature of the enzyme activity was found at 3.0 and 30°C using ABTS as substrate but the enzyme was quite stable at high temperature and alkaline pH. The laccase activity was enhanced by Cu+2, Zn+2 and Mn+2. In addition, the dye decolorization potential of purified laccase was much higher in terms of extent as well as time. The purified laccase decolorized (96%) of anthraquinonic dye Reactive blue- 4 within 4 h and its biodegradation studies was monitored by UV visible spectra, FTIR and HPLC which concluded that cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Public Library of Science 2017-04-06 /pmc/articles/PMC5383238/ /pubmed/28384218 http://dx.doi.org/10.1371/journal.pone.0175144 Text en © 2017 Afreen 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 Afreen, Sumbul Shamsi, Tooba Naz Baig, Mohd Affan Ahmad, Nadeem Fatima, Sadaf Qureshi, M. Irfan Hassan, Md. Imtaiyaz Fatma, Tasneem A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title | A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title_full | A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title_fullStr | A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title_full_unstemmed | A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title_short | A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye |
title_sort | novel multicopper oxidase (laccase) from cyanobacteria: purification, characterization with potential in the decolorization of anthraquinonic dye |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5383238/ https://www.ncbi.nlm.nih.gov/pubmed/28384218 http://dx.doi.org/10.1371/journal.pone.0175144 |
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