Improvement of Laccase Activity Via Covalent Immobilization over Mesoporous Silica Coated Magnetic Multiwalled Carbon Nanotubes for the Discoloration of Synthetic Dyes

Due to its environmental friendliness and biodegradable ability, the enzymatic decolorization of azo dyes is the best option. However, the free enzyme suffers from various limitations, including poor stability, no repeatable use, and a high expense, which is the key drawback for its practical use. In this analysis, the laccase enzyme was immobilized in mesoporous silica coated magnetic multiwalled carbon nanotubes (Fe3O4-MWCNTs@SiO2) by a glutaraldehyde cross-linker to create an easily separable and stable enzyme. Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and energy-dispersive X-ray spectroscopy (EDX) were used to characterize the as-synthesized Fe3O4-MVVCNTs@SiO2. Laccase immobilized in Fe3O4-MWCNTs@SiO2 showed a good improvement in temperature, pH, and storage stability. Moreover, the operational stability of the biocatalyst was improved, retaining 87% of its original activity even after 10 cycles of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) oxidation. The biocatalysts were applied for the decolorization of selected azo dyes without a mediator, and up to 99% of Eriochrome Black T (EBT), 98% of Acid Red 88 (AR 88), and 66% of Reactive Black 5 (RB5) were decolorized. Based on these properties, the biocatalysts can be potentially utilized in various environmental and industrial applications.

Automated summary

Immobilizing laccase enzyme in mesoporous silica coated magnetic multiwalled carbon nanotubes can enhance stability and operational stability, allowing for efficient dye decolorization without a mediator. This method shows potential applications in environmental and industrial settings.