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<p>This study investigates the enzymatic degradation of hydroquinone, a model phenolic pollutant, using free and immobilized <i>Pleurotus ostreatus</i> ARC280 laccase. Initial one-factor-at-a-time experiments identified optimal single parameters: pH 7.0, 0.153 U enzyme, 100&#xa0;µg substrate, and 50&#xa0;°C. Response Surface Methodology (RSM) was subsequently employed for multivariate optimization, refining these values to pH 6.84, 0.184 U laccase, 150&#xa0;µg hydroquinone, and 35&#xa0;°C for maximum degradation efficiency. The immobilized laccase demonstrated superior operational stability and reusability, retaining significant activity across multiple catalytic cycles. These results underscore the efficacy of both free and immobilized laccase as robust, sustainable biocatalysts. The study concludes that immobilized <i>Pl. ostreatus</i> laccase is a highly promising candidate for developing innovative and eco-friendly bioremediation strategies for phenolic pollutants.</p>

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Evaluation of Pleurotus ostreatus ARC280 laccase potential in hydroquinone enzymatic degradation as an environmental biotechnology approach: statistical optimization and immobilization

  • 期刊论文

  • 发表日期：

    2026年7月15日

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  • Shahd Y. Elmazahy,
  • Abdelmageed M. Othman

摘要

This study investigates the enzymatic degradation of hydroquinone, a model phenolic pollutant, using free and immobilized Pleurotus ostreatus ARC280 laccase. Initial one-factor-at-a-time experiments identified optimal single parameters: pH 7.0, 0.153 U enzyme, 100 µg substrate, and 50 °C. Response Surface Methodology (RSM) was subsequently employed for multivariate optimization, refining these values to pH 6.84, 0.184 U laccase, 150 µg hydroquinone, and 35 °C for maximum degradation efficiency. The immobilized laccase demonstrated superior operational stability and reusability, retaining significant activity across multiple catalytic cycles. These results underscore the efficacy of both free and immobilized laccase as robust, sustainable biocatalysts. The study concludes that immobilized Pl. ostreatus laccase is a highly promising candidate for developing innovative and eco-friendly bioremediation strategies for phenolic pollutants.