Characterization of glutamate dehydrogenase immobilization on silica surface by atomic force microscopy and kinetic analyses

Authors :: Michele Maffia
G. Vasapollo
Laura Blasi
Ross Rinaldi
Luigia Longo
Raffaele Acierno
T. Rizzello
R. Cingolani
Blasi, L.
Longo, L.
Vasapollo, Giuseppe
Cingolani, R.
Rinaldi, Rosaria
Rizzello, T.
Acierno, R.
Maffia, Michele
Blasi, L
Longo, L
Vasapollo, G
Cingolani, Roberto
Rizzello, T
Acierno, R
Source :: Enzyme and microbial technology 36 (2005): 818–823. doi:10.1016/j.enzmictec.2005.01.014, info:cnr-pdr/source/autori:Laura Blasi; Luigia Longo; Giuseppe Vasapollo; Roberto Cignolani; Rosaria Rinaldi; Tonia Rizzello; Raffaele Acierno; Michele Maffia/titolo:Characterization of glutamate dehydrogenase immobilization on silica surface by atomic force microscopy and kinetic analyses/doi:10.1016%2Fj.enzmictec.2005.01.014/rivista:Enzyme and microbial technology/anno:2005/pagina_da:818/pagina_a:823/intervallo_pagine:818–823/volume:36
Publication Year :: 2005
Publisher :: Elsevier BV, 2005.
Abstract: Covalent immobilization of glutamate dehydrogenase (GDH) onto activated Si/SiO 2 supports was analyzed by both atomic force microscopy (AFM) and an enzymatic assay. When the concentration of 3-aminopropyltriethoxysilane used in the first derivatization step of the silicon surface was decreased, the specific enzymatic 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.

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