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<p><i>Bacillus</i> sp. DL-5 isolated in the present study produced an extracellular laccase capable of degrading textile dyes known to cause pollution. A 20- fold increase in the enzyme yield was achieved under statistically optimized conditions 400&#xa0;µM copper sulfate, 200&#xa0;µM magnesium sulphate, 0.6&#xa0;g yeast extract and 150&#xa0;µM vanillic acid. The enzyme was purified using standard chromatographic techniques and was found to be a molecular weight of 32&#xa0;kDa. The enzyme was found to be optimally active at 50&#xa0;°C and retained 76% of activity for 4&#xa0;h. The enzyme was found to be stable in presence of most of the metal ions and was inhibited by the known laccase inhibitors maximum inhibition was achieved by β-mercaptoethanol. The enzyme was able to degraded the various textile dyes even without using the laccase mediator. Maximum degradation of 60% was achieved with malachite green, optimization led to 78.64% degradation with an enzyme dose of 6&#xa0;IU mL<sup>1</sup> at 55&#xa0;°C and pH 8.5 within 3&#xa0;h. The results indicate that laccase DL-5 is a promising biocatalyst for textile wastewater treatment, offering an eco-friendly approach for textile industry.</p>

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Bacterial laccase-mediated biodegradation of malachite green dye: a green solution to environmental pollution

  • 期刊论文

  • 发表日期：

    2025年6月1日

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  • Kumud Sharma,
  • Aditi Sharma,
  • Deepti Goyal,
  • Sunena Jassal,
  • Naveen Gupta

摘要

Bacillus sp. DL-5 isolated in the present study produced an extracellular laccase capable of degrading textile dyes known to cause pollution. A 20- fold increase in the enzyme yield was achieved under statistically optimized conditions 400 µM copper sulfate, 200 µM magnesium sulphate, 0.6 g yeast extract and 150 µM vanillic acid. The enzyme was purified using standard chromatographic techniques and was found to be a molecular weight of 32 kDa. The enzyme was found to be optimally active at 50 °C and retained 76% of activity for 4 h. The enzyme was found to be stable in presence of most of the metal ions and was inhibited by the known laccase inhibitors maximum inhibition was achieved by β-mercaptoethanol. The enzyme was able to degraded the various textile dyes even without using the laccase mediator. Maximum degradation of 60% was achieved with malachite green, optimization led to 78.64% degradation with an enzyme dose of 6 IU mL1 at 55 °C and pH 8.5 within 3 h. The results indicate that laccase DL-5 is a promising biocatalyst for textile wastewater treatment, offering an eco-friendly approach for textile industry.