The silica-coated chitosan particle from a layer-by-layer approach for pectinase immobilization

We investigate the enzymatic activity of pectinase adsorbed on a novel type of colloidal particles. The colloidal stability is not impeded by the adsorbed proteins despite the fact that up to 247.8 mg of enzyme is adsorbed per gram of the carrier particles. Various characteristics of immobilized pectinase such as the pH stability, thermal stability, and storage stability were valuated. The immobilized pectinase revealed acceptable pH stability over a broad experimental range. The activity of immobilized pectinase adsorbed onto these particles is analyzed in terms of the Michaelis–Menten parameters. The Michaelis constant Km differs only slightly from the Km value of the native enzyme when the amount of adsorbed enzyme is raised despite the high local concentration of immobilized enzymes.