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<p>Laccases (EC 1.10.3.2) are promising biocatalysts for textile wastewater treatment. Here, we identified a novel laccase, TpLcc3, from <i>Trametes polyzona</i> MUCL 38443, heterologously expressed it in <i>Pichia pastoris</i>, and evaluated its biochemical properties and dye-removal performance in citrate buffer (CB) and a simplified simulated industrial dyebath effluent (DB). The glycosylated recombinant enzyme (rTpLcc3) exhibited maximal activity at 70&#xa0;°C and pH 3.0, broad pH tolerance (pH 4.0–8.0 at 25–30&#xa0;°C), and substantial thermal stability with half-lives of 187&#xa0;min at 50&#xa0;°C and 19&#xa0;min at 70&#xa0;°C. rTpLcc3 showed high catalytic efficiency toward ABTS (k<sub>cat</sub>/K<sub>m</sub> = 576.76 µM⁻¹ s⁻¹), placing it among high-performing fungal laccases. rTpLcc3&#xa0;alone effectively decolorized azo dyes-Acid Black 194 (AB194) and Bismarck Brown, with AB194 showing the highest removal in CB (71.39 ± 6.16%) and DB (42.17 ± 5.69%). Mediator supplementation markedly enhanced decolorization, with ABTS enabling rapid, complete removal of AB194, and &gt; 90% removal of Malachite Green in both matrices. Across dye classes, ABTS and syringaldehyde were the most effective mediators in CB (72.4 ± 21.8% and 71.4 ± 28.3% mean decolorization, respectively), while ABTS remained superior in DB (80.1 ± 27.8%). Notably, the TpLcc3/mediator systems significantly reduced cytotoxicity of Malachite Green and Crystal Violet while no increase in cytotoxicity was observed for the remaining dyes under the tested conditions.</p>

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Characterization and application potential of a robust recombinant laccase rTpLcc3 from Trametes polyzona for textile dye decolorization

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月26日

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  • Öznur Pehlivan-Günaydın,
  • Ayfer Dilara Bayezit,
  • Dicle Malaymar Pinar,
  • Orkun Pinar,
  • İdil Arslan-Alaton,
  • Ayten Yazgan-Karataş

摘要

Laccases (EC 1.10.3.2) are promising biocatalysts for textile wastewater treatment. Here, we identified a novel laccase, TpLcc3, from Trametes polyzona MUCL 38443, heterologously expressed it in Pichia pastoris, and evaluated its biochemical properties and dye-removal performance in citrate buffer (CB) and a simplified simulated industrial dyebath effluent (DB). The glycosylated recombinant enzyme (rTpLcc3) exhibited maximal activity at 70 °C and pH 3.0, broad pH tolerance (pH 4.0–8.0 at 25–30 °C), and substantial thermal stability with half-lives of 187 min at 50 °C and 19 min at 70 °C. rTpLcc3 showed high catalytic efficiency toward ABTS (kcat/Km = 576.76 µM⁻¹ s⁻¹), placing it among high-performing fungal laccases. rTpLcc3 alone effectively decolorized azo dyes-Acid Black 194 (AB194) and Bismarck Brown, with AB194 showing the highest removal in CB (71.39 ± 6.16%) and DB (42.17 ± 5.69%). Mediator supplementation markedly enhanced decolorization, with ABTS enabling rapid, complete removal of AB194, and > 90% removal of Malachite Green in both matrices. Across dye classes, ABTS and syringaldehyde were the most effective mediators in CB (72.4 ± 21.8% and 71.4 ± 28.3% mean decolorization, respectively), while ABTS remained superior in DB (80.1 ± 27.8%). Notably, the TpLcc3/mediator systems significantly reduced cytotoxicity of Malachite Green and Crystal Violet while no increase in cytotoxicity was observed for the remaining dyes under the tested conditions.