| Abstract
| - Maghemite (γ-Fe2O3) nanoparticles were functionalized using a multifunctional coblock polymer to immobilize silicatein, a protein involved in biomineralization of marine silica sponges. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica.
- Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe2O3) 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-Fe2O3 surface 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-Fe2O3 nanoparticles. 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 SiO2-coated γ-Fe2O3 nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy.
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