Sorption-assisted surface conjugation: a way to stabilize laccase enzyme

Area of Science:

• Biotechnology
• Environmental Science
• Materials Science

Background:

• Enzyme immobilization on solid surfaces enhances stability and activity under harsh conditions.
• Laccases are multicopper enzymes crucial for oxidizing aromatic compounds, with applications in wastewater treatment.
• Developing effective enzyme immobilization techniques is key for environmental remediation tools.

Purpose of the Study:

• To develop and characterize a novel method for immobilizing laccase from Coriolopsis polyzona onto fumed silica nanoparticles.
• To evaluate the efficiency of this immobilization method compared to other nanoparticle types.
• To assess the long-term stability and activity of the immobilized laccase in real wastewater.

Main Methods:

• Immobilization of laccase onto amino-modified fumed silica nanoparticles via sorption and glutaraldehyde cross-linking.
• Characterization of the nanoparticulate material using scanning electron microscopy and Brunauer-Emmett-Teller surface area analysis.
• Long-term stability assays in real wastewater, comparing immobilized laccase to free laccase.

Main Results:

• A novel immobilization method using fumed silica nanoparticles was successfully developed.
• The method resulted in significant surface structure and area modifications of the nanoparticles.
• Immobilized laccase demonstrated drastically improved long-term stability, retaining 77% activity in real wastewater over 1 month, compared to 2.5% for free laccase.

Conclusions:

• The novel immobilization technique using fumed silica nanoparticles effectively enhances laccase stability and longevity.
• This method offers a promising solution for developing robust enzymatic tools for micropollutant elimination in wastewater.
• Fumed silica nanoparticles are superior supports for laccase immobilization compared to spherical nanoparticles produced via the Stöber method.