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Fabrication of a Silica Coating on Magnetic γ-Fe2O3Nanoparticles by an Immobilized Enzyme.
- Source :
-
Chemistry of Materials . May2008, Vol. 20 Issue 11, p3567-3573. 7p. - Publication Year :
- 2008
-
Abstract
- Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe 2O 3) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe 2O 3surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe 2O 3nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR) 4. Functionalization of the magnetic nanoparticles and the architecture of the SiO 2-coated γ-Fe 2O 3nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy. [ABSTRACT FROM AUTHOR]
- Subjects :
- *BIOMOLECULE analysis
*IMMOBILIZED enzymes
*SILICON compounds
*POLYMERS
Subjects
Details
- Language :
- English
- ISSN :
- 08974756
- Volume :
- 20
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Chemistry of Materials
- Publication Type :
- Academic Journal
- Accession number :
- 33049564
- Full Text :
- https://doi.org/10.1021/cm7029954