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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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ABSTRACT

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.

No MeSH data available.


HPLC chromatogram (a) Reactive Blue 4 control (b) Laccase treated Reactive Blue 4
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pone.0175144.g011: HPLC chromatogram (a) Reactive Blue 4 control (b) Laccase treated Reactive Blue 4

Mentions: The HPLC analysis of control dye (Reactive blue 4) showed the presence of one major peak at retention time of 1.190 min with concentration of 10.575 mgml-1 covering the peak area of 535398649 (Fig 11A). After the dye decolorization process, there was major peak observed at retention time 1.190 but the peak area of dye was decreased 11848018 and the formation of completely different two minor peaks (by products) at retention times of 1.480 mins and 2.79 minswere observed (Fig 11B). The concentration of reactive blue 4 retained after decolorization was 1.106 mgml-1 which clearly support the biodegradation of RB4. The HPLC chromatogram of Reactive Blue 4 (control) suggested that similar results were presented during a HPLC follow-up of dye biodegradation [18, 62].


A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye
HPLC chromatogram (a) Reactive Blue 4 control (b) Laccase treated Reactive Blue 4
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5383238&req=5

pone.0175144.g011: HPLC chromatogram (a) Reactive Blue 4 control (b) Laccase treated Reactive Blue 4
Mentions: The HPLC analysis of control dye (Reactive blue 4) showed the presence of one major peak at retention time of 1.190 min with concentration of 10.575 mgml-1 covering the peak area of 535398649 (Fig 11A). After the dye decolorization process, there was major peak observed at retention time 1.190 but the peak area of dye was decreased 11848018 and the formation of completely different two minor peaks (by products) at retention times of 1.480 mins and 2.79 minswere observed (Fig 11B). The concentration of reactive blue 4 retained after decolorization was 1.106 mgml-1 which clearly support the biodegradation of RB4. The HPLC chromatogram of Reactive Blue 4 (control) suggested that similar results were presented during a HPLC follow-up of dye biodegradation [18, 62].

View Article: PubMed Central - PubMed

ABSTRACT

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.

No MeSH data available.