Covalent immobilization of glutamate dehydrogenase (GDH) onto activated Si/SiO2 supports was analyzed by both at. force microscopy (AFM) and an enzymic assay. When the concn. of 3-aminopropyltriethoxysilane used in the first derivatization step of the silicon surface was decreased, the specific enzymic activity also decreased, whereas the mean roughness increased. Thus, the activity of immobilized GDH is critically dependent on the conditions for surface derivatization, and is inversely correlated with surface roughness.
Characterization of glutamate dehydrogenase immobilization on silica surface by atomic force microscopy and kinetic analyses
VASAPOLLO, Giuseppe;RINALDI, Rosaria;MAFFIA, Michele
2005-01-01
Abstract
Covalent immobilization of glutamate dehydrogenase (GDH) onto activated Si/SiO2 supports was analyzed by both at. force microscopy (AFM) and an enzymic assay. When the concn. of 3-aminopropyltriethoxysilane used in the first derivatization step of the silicon surface was decreased, the specific enzymic activity also decreased, whereas the mean roughness increased. Thus, the activity of immobilized GDH is critically dependent on the conditions for surface derivatization, and is inversely correlated with surface roughness.File in questo prodotto:
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