Laccase catalytic activity shielded by SiO₂ nanostructured materials: an in vitro and in silico approach

Abstract

This study investigates the enhancement of enzymatic catalytic performance by immobilizing laccase on various nanostructured mesoporous silica materials (SBA-15, MCF, and MSU-F). The activity of immobilized laccase was evaluated under different hydrothermal, pH, and solvent conditions, with laccase@MSU-F showing a three-fold increase in stability. Laccase immobilized on these materials demonstrated stability in a pH range of 4.5 to 10.0, while free laccase was inactivated at pH higher than 7. Molecular dynamics simulations revealed that electrostatic interactions and protective confinement effects contribute to the improved stability of immobilized laccase. Overall, the findings suggest that nanomaterials can enhance the operational stability and recovery of enzymes.

Communicated by Ramaswamy H. Sarma

Keywords:

• Laccase
• mesoporous silica
• immobilization
• molecular dynamics
• catalytic stability

Disclosure Statement

The authors declare that there are no competing interests.

Additional information

Funding

This research was funded by the Universidad Nacional Autónoma de Mexico (UNAM) with a PAPIIT-IG200320 and LANCAD-UNAM-DGTIC-286 grants. AVL acknowledges the National Supercomputing Center- IPICYT for the computational resources supported in this research through grant TKII-AMVL001, as well as MSc. Emanuel Villafán de la Torre for technical support on Huitzilin academic cluster. JIWR acknowledge CONACYT Scholarship 28572. The authors acknowledge technical support of MSc. Aldo Rodriguez Guerrero, Maria I. Perez (writing assistant), Eloísa Aparicio and David Domínguez (Spectroscopy Laboratory), Francisco Ruiz (TEM), Jaime Mendoza (sample preparation) and Israel Gradilla (SEM).