Catalytic activity in organic solvents and stability of immobilized enzymes depend on the pore size and surface characteristics of mesoporous silica

An enzyme, horseradish peroxidase (HRP), was adsorbed in the manner of the single immersion method on the silica mesoporous materials FSM-16, MCM-41, and SBA-15 with various pore diameters from 27 to 92 Angstrom, and their en zymatic activities in an organic solvent and the thermal stabilities were s tudied. FSM-16 and MCM-41 showed a larger amount of adsorption of HRP than SBA-15 or silica gel when the pore sizes were larger than the 50 Angstrom. The increased enzyme adsorption capacity may be due to the surface characte ristics of FSM-16 and MCM-41, which would be consistent with the observed l arger adsorption capacity of cationic pigment compared with anionic pigment for these materials. The immobilized HRP on FSM-16 and MCM-41 with pore di ameter 50 Angstrom showed the highest enzymatic activity in an organic tolu ene and thermal stability in aqueous solution at the temperature of 70 degr eesC. The immobilized enzymes on the other mesoporous materials including l arge or small pore sized FSM-16 showed lower enzymatic activity in an organ ic solvent and thermal stability. Both surface character and size matching between pore sizes and the molecular diameters of HRP were important in ach ieving high enzymatic activity in organic solvent and high thermal stabilit y.