article · Scientific Reports
This research evaluates the immobilisation of laccase enzyme extracted from the fungus Agaricus bisporus using calcium alginate beads, achieving an entrapped immobilisation yield of 91.95 percent. Both the free and immobilised enzymes achieved their highest activity at an optimum temperature of 60 degrees Celsius. While free laccase lost almost all activity after 30 minutes at 70 and 80 degrees Celsius, the immobilised enzyme retained approximately 60 percent and 40 percent of its activity under identical conditions. Adding magnesium sulphate enhanced enzymatic activity, reaching over 113 percent relative activity at a concentration of 10 millimolar. Using a central composite design approach, optimal degradation of Cibacron D-Blue SGL dye occurred at pH 6.0 with the mediator hydroxybenzotriazole. Testing demonstrated that the immobilised enzyme efficiently decolorises the dye across repeated operational cycles.
Industrial dyes are frequent environmental pollutants that are challenging to remove from wastewater. Using enzymes to break down these chemicals is an environmentally friendly alternative, but free enzymes are often fragile and cannot be reused. Immobilising laccase in calcium alginate significantly improves its heat tolerance and allows it to be used repeatedly, making biological treatment of dye-contaminated water more practical and robust.
This work is relevant to wastewater treatment operators and textile manufacturers seeking sustainable dye remediation processes. The findings demonstrate effective dye decolorisation and reusability across multiple cycles in laboratory settings. Because the research focuses on laboratory-scale characterisation and statistical optimisation via response surface methodology, it represents early-stage development that requires testing at larger volumes and in real industrial effluent before commercial adoption is feasible.
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In the current study, calcium alginate was used as a carrier for Agaricus bisporus CU13 laccase immobilization, with an immobilization yield of the entrapped laccase of 91.95%. Free and immobilized enzymes showed their best enzyme activity at 60 °C as an optimum temperature. Free laccase was nearly completely inactivated at high temperatures (70 and 80 °C C) after 30 min, whereas the immobilized form retained around 60 and 40% of its activity after 30 min at the same temperatures. The metal ion of MgSO<sub>4</sub> showed the best impact on the Agaricus bisporus laccase activity with a relative activity of 113.1 and 106.8% at concentrations of 10 mM and 2.5 mM, respectively. The best Cibacron D-Blue SGL dye degradation by laccase enzyme was obtained at pH 6.0, 0.354 U of laccase, and 100 mg/L of dye using hydroxybenzotriazole (HBT; 1 mM) as a mediator. Optimization ramps obtained from the central composite design (CCD) approach indicate that the rate at which the laccase enzyme decolorizes dye has increased significantly when the concentrations of the enzyme, and HBT increased, whereas dye concentration decreased. Finally, the immobilized enzyme was found to be efficient in decolorizing Cibacron D-Blue SGL dye in the presence of HBT as a mediator for different cycles.
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DOI: 10.1038/s41598-024-82310-0
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