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Purification and Biochemical Characterization of Trametes hirsuta CS5 Laccases and Its Potential in Decolorizing Textile Dyes as Emerging Contaminants
Summary
Three laccase isoforms from Trametes hirsuta CS5 were purified and characterized, with the ThII isoform showing the highest catalytic efficiency; all isoforms effectively decolorized synthetic textile dyes, supporting their potential as eco-friendly biocatalysts for treating dye-containing wastewater.
This study explores the purification, characterization, and application of laccases from Trametes hirsuta CS5 for degrading synthetic dyes as models of emerging contaminants. Purification involved ion exchange chromatography, molecular exclusion, and chromatofocusing, identifying th ree laccase isoforms: ThIa, ThIb, and ThII. Characterization included determining pH and temperature stability, kinetic parameters (Km, Kcat), and inhibition constants (Ki) for inhibitors like NaN3, SDS, TGA, EDTA, and DMSO, using 2,6-DMP and guaiacol as substrates. ThII exhibited the highest catalytic efficiency, with the lowest Km and highest Kcat. Optimal activity was observed at pH 3.5 and 55 °C. Decolorization tests with nine dyes showed that ThII and ThIa were particularly effective against Acid Red 44, Orange II, Indigo Blue, Brilliant Blue R, and Remazol Brilliant Blue R. ThIb displayed higher activity towards Crystal Violet and Acid Green 27. Among substrates, guaiacol showed the highest Kcat, while 2,6-DMP was preferred overall. Inhibitor studies revealed NaN3 as the most potent inhibitor. These results demonstrate the significant potential of T. hirsuta CS5 laccases, especially ThIa and ThII, as biocatalysts for degrading synthetic dyes and other xenobiotics. Their efficiency and stability under acidic and moderate temperature conditions position them as promising tools for sustainable wastewater treatment and environmental remediation.
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