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; catalytic stability; immobilization; mesoporous silica; molecular dynamics.