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<p>The present study focused on the enhanced biodegradation of phenol as a toxic compound using peroxidases extracted from agricultural wastes (skin peels of luffa and jicama plants) mediated bioprocess under H<sub>2</sub>O<sub>2</sub>-infusion. The extracted crude luffa peroxidase (LP) and jicama peroxidase (JP) showed enzyme activities of 1.4 ± 0.2 U/mL and 1.6 ± 0.1 U/mL, respectively. LP achieved a phenol removal efficiency exceeding 95% at H₂O₂ concentrations between 6–8&#xa0;mM and pH 7, whereas JP achieved 94.5% removal at pH 7, with minimal impact from variations in H₂O₂ concentrations. Maximum removal efficiencies for both peroxidases were observed at an enzyme loading of 1.5&#xa0;mL. LP demonstrated effective removal within a temperature range of 25&#xa0;°C to 30&#xa0;°C, while JP maintained functionality up to 40&#xa0;°C. The optimum reaction times were determined to be 16&#xa0;h for LP and 13&#xa0;h for JP. LP exhibited high preservation of enzyme activity during storage, with no significant fluctuations observed, while JP’s enzyme activity decreased to approximately 40% of its initial value, accompanied by a notable decline in phenol elimination efficiency by day 42. First-order kinetic analysis of enzyme activity yielded reaction rate constants of 1.18&#xa0;h<sup>−1</sup> for LP and 1.21&#xa0;h<sup>−1</sup> for JP, with JP demonstrating superior storage stability compared to LP.</p>

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Sustainable biodegradation of phenol using peroxidases extracted from local agricultural wastes

  • 期刊论文

  • 发表日期：

    2026年2月5日

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  • Tung Chiong,
  • Sie Yon Lau,
  • Michael K. Danquah,
  • Murat Yılmaz

摘要

The present study focused on the enhanced biodegradation of phenol as a toxic compound using peroxidases extracted from agricultural wastes (skin peels of luffa and jicama plants) mediated bioprocess under H2O2-infusion. The extracted crude luffa peroxidase (LP) and jicama peroxidase (JP) showed enzyme activities of 1.4 ± 0.2 U/mL and 1.6 ± 0.1 U/mL, respectively. LP achieved a phenol removal efficiency exceeding 95% at H₂O₂ concentrations between 6–8 mM and pH 7, whereas JP achieved 94.5% removal at pH 7, with minimal impact from variations in H₂O₂ concentrations. Maximum removal efficiencies for both peroxidases were observed at an enzyme loading of 1.5 mL. LP demonstrated effective removal within a temperature range of 25 °C to 30 °C, while JP maintained functionality up to 40 °C. The optimum reaction times were determined to be 16 h for LP and 13 h for JP. LP exhibited high preservation of enzyme activity during storage, with no significant fluctuations observed, while JP’s enzyme activity decreased to approximately 40% of its initial value, accompanied by a notable decline in phenol elimination efficiency by day 42. First-order kinetic analysis of enzyme activity yielded reaction rate constants of 1.18 h−1 for LP and 1.21 h−1 for JP, with JP demonstrating superior storage stability compared to LP.