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<p>Laccase is an environmentally friendly biocatalyst widely used in wastewater treatment, the food industry, and biosensors. However, free laccase is susceptible to environmental factors such as pH and temperature. Immobilizing it on nanomaterials can significantly mitigate these issues. This approach also enhances the reusability of laccase, demonstrating broad application prospects. Four different morphologies of MnO<sub>2</sub> were compared, with δ-MnO<sub>2</sub> (sheet) demonstrating the most effective immobilization effect as a carrier. Under conditions of pH=5, 30&#xa0;°C, and laccase concentration of 1&#xa0;mg/L, the reaction achieves optimal immobilization after 4&#xa0;h of adsorption. Characterization of δ-MnO<sub>2</sub> and immobilized laccase was performed using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The enzymatic properties of immobilized laccase were also investigated. The results indicate that the optimal temperature for immobilized laccase is 75&#xa0;°C, with an optimal pH of 3. Compared to free laccase, stability has been significantly enhanced. Furthermore, even after 30&#xa0;days of storage at −4 °C the relative enzyme activity of the immobilized laccase remained as high as 74.51%. The kinetic constants demonstrate that immobilized laccase not only enhances the maximum reaction rate but also significantly improves substrate affinity. Compared to free laccase, the relative enzyme activity of MnO<sub>2</sub>-immobilized laccase (MnO<sub>2</sub>@Lac) is significantly enhanced. This may be attributed to the synergistic effect between MnO<sub>2</sub> nanoparticles and laccase during substrate conversion. This study creates favorable conditions for the further application of immobilized laccase in the treatment of organic pollutants.</p>

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Preparation, characterization, and enzymatic properties of laccase immobilized on MnO2 nanoparticles via adsorption method

  • 期刊论文

  • 发表日期：

    2026年1月21日

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  • Wanlei Yue,
  • Xin Wang,
  • Zixin Gao,
  • Jiale Zhang,
  • Jia Bao,
  • Mengqin Yao

摘要

Laccase is an environmentally friendly biocatalyst widely used in wastewater treatment, the food industry, and biosensors. However, free laccase is susceptible to environmental factors such as pH and temperature. Immobilizing it on nanomaterials can significantly mitigate these issues. This approach also enhances the reusability of laccase, demonstrating broad application prospects. Four different morphologies of MnO2 were compared, with δ-MnO2 (sheet) demonstrating the most effective immobilization effect as a carrier. Under conditions of pH=5, 30 °C, and laccase concentration of 1 mg/L, the reaction achieves optimal immobilization after 4 h of adsorption. Characterization of δ-MnO2 and immobilized laccase was performed using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The enzymatic properties of immobilized laccase were also investigated. The results indicate that the optimal temperature for immobilized laccase is 75 °C, with an optimal pH of 3. Compared to free laccase, stability has been significantly enhanced. Furthermore, even after 30 days of storage at −4 °C the relative enzyme activity of the immobilized laccase remained as high as 74.51%. The kinetic constants demonstrate that immobilized laccase not only enhances the maximum reaction rate but also significantly improves substrate affinity. Compared to free laccase, the relative enzyme activity of MnO2-immobilized laccase (MnO2@Lac) is significantly enhanced. This may be attributed to the synergistic effect between MnO2 nanoparticles and laccase during substrate conversion. This study creates favorable conditions for the further application of immobilized laccase in the treatment of organic pollutants.