Immobilization of horseradish peroxidase in cross-linked phyllosilicates: conditions and characterizations.
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.[1]References
- Immobilization of horseradish peroxidase in cross-linked phyllosilicates: conditions and characterizations. Shen, S., Tu, S.I. Biotechnol. Appl. Biochem. (1999) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg