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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.


Effect of organic solvents on the activity of purified laccase was measured using ABTS as asubstrate.Values are mean of triplicates ± S.E
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pone.0175144.g007: Effect of organic solvents on the activity of purified laccase was measured using ABTS as asubstrate.Values are mean of triplicates ± S.E

Mentions: In present study, effect of organic solvent like ethanol, acetonitrile, methanol, DMF and DMSO was observed for the characterization of laccase (Fig 7). The order of relative was Ethanol (96.36%) > Acetonitrile (91.80%) > Methanol (82.54%) > DMF (58.76%) > DMSO (42.26%) with respect to control (100%). Similar results were reported in Cerrena sp. HYB07 and Ganoderma fornicatum [55– 56]. It was also reported that organic solvents inhibit laccase activity by promoting protein unfolding [57]. DMF and DMSO increase relative laccase activity in Thermobifida fusca which was contrary to result obtained in our study [58].


A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye
Effect of organic solvents on the activity of purified laccase was measured using ABTS as asubstrate.Values are mean of triplicates ± S.E
© Copyright Policy
Related In: Results  -  Collection

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

pone.0175144.g007: Effect of organic solvents on the activity of purified laccase was measured using ABTS as asubstrate.Values are mean of triplicates ± S.E
Mentions: In present study, effect of organic solvent like ethanol, acetonitrile, methanol, DMF and DMSO was observed for the characterization of laccase (Fig 7). The order of relative was Ethanol (96.36%) > Acetonitrile (91.80%) > Methanol (82.54%) > DMF (58.76%) > DMSO (42.26%) with respect to control (100%). Similar results were reported in Cerrena sp. HYB07 and Ganoderma fornicatum [55– 56]. It was also reported that organic solvents inhibit laccase activity by promoting protein unfolding [57]. DMF and DMSO increase relative laccase activity in Thermobifida fusca which was contrary to result obtained in our study [58].

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.