Immobilization of horseradish peroxidase in cross-linked phyllosilicates: conditions and characterizations

An innovative immobilization procedure was developed for intercalation of e nzymes into dispersed phyllosilicates which were cross-linked with silicate s resulting from the hydrolysis of tetramethyl orthosilicate, Donor:hydroge n-peroxide oxidoreductase intercalative immobilized in the cross-linked phy llosilicate exhibited a similar or higher activity than the free enzyme. Th e kinetic properties of peroxidase were unaffected by intercalative immobil ization. Different factors, including drying methods, particle size, surfac e cations of the phyllosilicate and ratio of phyllosilicate to tetramethyl orthosilicate, were investigated to optimize immobilization conditions. The immobilized peroxidase exhibited similar kinetic properties to the free en zyme and good storage stability.