Enhancement in adsorption and catalytic activity of enzymes immobilized on phosphorus- and calcium-modified MCM-41.

摘要: An oxidative enzyme, horseradish peroxidase (HRP), was immobilized on phosphorus- and/or calcium-modified MCM-41 mesoporous silicas with suitable pore diameters. Structural analyses by means of XRD and nitrogen adsorption confirmed that the P- Ca-modified materials retained their structural quality even after modification or enzyme immobilization. Detailed studies behaviors characterization using FT-IR spectroscopy zeta potential measurements revealed P Ca atoms attached silica surface provided increased uptake HRP molecules, which is attributable to more negatively charged strong interatomic interactions between these functional groups enzyme. In particular, P-modified showed an improved capacity in a short period over wide pH range without denaturation protein structure, largest 154 mg/g. Furthermore, higher enzymatic activity reusability oxidation 1,2-diaminobenzene organic solvent at temperature 37 °C than parent MCM-41. This enhancement can be related integrity loaded molecules P-MCM-41 surface. work thus demonstrates bearing provide environment for