Elevating enzyme activity through the immobilization of horseradish peroxidase onto periodic mesoporous organosilicas

Abstract

Horseradish peroxidase (HRP) is immobilized on periodic mesoporous organosilicas (PMO) for the first time, and the enzyme activity improved, especially on MI100, prepared with 100% organic silica precursor, the enzyme activity is enhanced 110% compared with free HRP in solution. Besides, the stability of immobilized HRP to lower pH values or the denaturing agent urea is enhanced, resulting from interfacial activation of the enzyme when it is attached to a surface filled with organic groups and hydrophobic parts. The thermal stability of immobilized HRP on PMO is also increased and, moreover, the HRP immobilized samples can be reusable for many cycles.