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<p>Laccases are valuable industrial enzymes with applications across various fields. While heterologous expression in <i>Pichia pastoris</i> is a common strategy, current approaches face limitations in yield, stability, and catalytic efficiency against recalcitrant agrochemicals. In this study, we sequenced and annotated the first high-quality genome of <i>Cerrena unicolor</i> strain GC.u01 (30.95&#xa0;Mb, 8,089 genes), revealing a unique laccase gene family comprising nine members. Structural analysis revealed novel catalytic motifs in Lac2, which was successfully expressed in P. <i>pastoris</i> GS115 through codon optimization, yielding a novel recombinant enzyme (70&#xa0;kDa) with exceptional pH stability (retaining &gt; 80% activity at pH 3.0–8.0 for 24&#xa0;h) and thermotolerance (&gt; 60% activity at 40&#xa0;°C), surpassing most reported fungal laccases. Notably, Lac2 demonstrated unprecedented degradation efficiency for azoxystrobin (96.2) and phoxim (30.7%)—the first report of a <i>Cerrena unicolor</i> laccase degrading these pesticides—achieving significantly higher rates than previously described laccases under similar conditions. This study integrates genome mining, enzyme engineering, and functional validation to establish a new paradigm for developing robust biocatalysts against recalcitrant agrochemicals. These unique characteristics of Lac2 suggest the potential of this enzyme in biotechnological and industrial applications.</p>

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Exploration and heterologous expression of laccase genes and pesticide degradation ability of laccases from Cerrena unicolor GC.u01

  • 期刊论文

  • 发表日期：

    2025年6月4日

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  • Jie Chu,
  • Xiaoxiao Zhang,
  • Ruihong Sun,
  • Yuanqiang Lv,
  • Zhuran Hu,
  • Wenjuan Zhang,
  • Xiaoran Shen,
  • Yanhua Huang

摘要

Laccases are valuable industrial enzymes with applications across various fields. While heterologous expression in Pichia pastoris is a common strategy, current approaches face limitations in yield, stability, and catalytic efficiency against recalcitrant agrochemicals. In this study, we sequenced and annotated the first high-quality genome of Cerrena unicolor strain GC.u01 (30.95 Mb, 8,089 genes), revealing a unique laccase gene family comprising nine members. Structural analysis revealed novel catalytic motifs in Lac2, which was successfully expressed in P. pastoris GS115 through codon optimization, yielding a novel recombinant enzyme (70 kDa) with exceptional pH stability (retaining > 80% activity at pH 3.0–8.0 for 24 h) and thermotolerance (> 60% activity at 40 °C), surpassing most reported fungal laccases. Notably, Lac2 demonstrated unprecedented degradation efficiency for azoxystrobin (96.2) and phoxim (30.7%)—the first report of a Cerrena unicolor laccase degrading these pesticides—achieving significantly higher rates than previously described laccases under similar conditions. This study integrates genome mining, enzyme engineering, and functional validation to establish a new paradigm for developing robust biocatalysts against recalcitrant agrochemicals. These unique characteristics of Lac2 suggest the potential of this enzyme in biotechnological and industrial applications.