Abstract
An innovative immobilization procedure was developed for intercalation of enzymes into dispersed phyllosilicates which were cross-linked with silicates resulting from the hydrolysis of tetramethyl orthosilicate. Donor:hydrogen-peroxide oxidoreductase intercalative immobilized in the cross-linked phyllosilicate exhibited a similar or higher activity than the free enzyme. The kinetic properties of peroxidase were unaffected by intercalative immobilization. Different factors, including drying methods, particle size, surface 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 enzyme and good storage stability.
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