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A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

PloS one, 2017-04, Vol.12 (4), p.e0175144-e0175144 [Peer Reviewed Journal]

COPYRIGHT 2017 Public Library of Science ;COPYRIGHT 2017 Public Library of Science ;2017 Afreen et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2017 Afreen et al 2017 Afreen et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0175144 ;PMID: 28384218

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Title:
A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye
Author: Afreen, Sumbul ; Shamsi, Tooba Naz ; Baig, Mohd Affan ; Ahmad, Nadeem ; Fatima, Sadaf ; Qureshi, M Irfan ; Hassan, Md Imtaiyaz ; Fatma, Tasneem
Permyakov, Eugene A.
Subjects: Acetone ; Acrylamide ; Adsorption ; Algae ; Ammonium ; Analysis ; Anthraquinones ; Aquatic organisms ; Bacteria ; Bagasse ; Biodegradation ; Biofuels ; Biology and Life Sciences ; Biomass ; Biotechnology ; Biotransformation ; Cadmium ; Catalysis ; Cbl protein ; Cell culture ; Cellulose ; Chemical degradation ; Chemicals ; Chromatography ; Chromatography, Gel ; Coloring Agents - chemistry ; Copper ; Cosmetics ; Cultivation ; Cyanobacteria ; Cyanobacteria - enzymology ; Degradation ; Dissolved oxygen ; Dyes ; Dyes and dyeing ; E coli ; Effluent treatment ; Electrophoresis, Polyacrylamide Gel ; Environmental impact ; Enzymes ; Fungi ; Glycoproteins ; Hydrogen-Ion Concentration ; Laboratories ; Laccase - isolation & purification ; Laccase - metabolism ; Lignin ; Monomers ; Oxidation ; Pigmentation ; Polycyclic aromatic hydrocarbons ; Purification ; Redox potential ; Research and Analysis Methods ; Spectrophotometry, Ultraviolet ; Spectroscopy, Fourier Transform Infrared ; Spirulina platensis ; Studies ; Temperature ; Temperature effects ; Wastewater
Is Part Of: PloS one, 2017-04, Vol.12 (4), p.e0175144-e0175144
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.
Publisher: United States: Public Library of Science
Language: English
Identifier: ISSN: 1932-6203
EISSN: 1932-6203
DOI: 10.1371/journal.pone.0175144
PMID: 28384218
Source: GFMER Free Medical Journals
MEDLINE
PubMed Central
Public Library of Science (PLoS)
ProQuest Central
DOAJ Directory of Open Access Journals

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A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

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