INFIQC   05475
INSTITUTO DE INVESTIGACIONES EN FISICO- QUIMICA DE CORDOBA
Unidad Ejecutora - UE
artículos
Título:
Interaction of D-Amino Acid Oxidase with Carbon Nanotubes: Implications in the Design of Biosensors
Autor/es:
MARIA F. MORA; CARLA E. GIACOMELLI; CARLOS D. GARCIA
Revista:
ANALYTICAL CHEMISTRY
Editorial:
American Chemical Society
Referencias:
Lugar: Washington; Año: 2009 vol. 81 p. 1016 - 1022
ISSN:
0003-2700
Resumen:
We have investigated the interaction of D-amino acid oxidase (DAAO) with single-walled carbon nanotubes (CNT) by spectroscopic ellipsometry. Dynamic adsorption experiments were performed at different experimental conditions. In addition, the activity of the enzyme adsorbed at different conditions was studied. Our results indicate that DAAO can be adsorbed to CNT at different pH values and concentrations by a combination of hydrophobic and electrostatic interactions. Considering that the highest enzymatic activity was obtained by adsorbing the protein at pH 5.7 and 0.1 mg·mL-1, our results indicate that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. oxidase (DAAO) with single-walled carbon nanotubes (CNT) by spectroscopic ellipsometry. Dynamic adsorption experiments were performed at different experimental conditions. In addition, the activity of the enzyme adsorbed at different conditions was studied. Our results indicate that DAAO can be adsorbed to CNT at different pH values and concentrations by a combination of hydrophobic and electrostatic interactions. Considering that the highest enzymatic activity was obtained by adsorbing the protein at pH 5.7 and 0.1 mg·mL-1, our results indicate that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. D-amino acid oxidase (DAAO) with single-walled carbon nanotubes (CNT) by spectroscopic ellipsometry. Dynamic adsorption experiments were performed at different experimental conditions. In addition, the activity of the enzyme adsorbed at different conditions was studied. Our results indicate that DAAO can be adsorbed to CNT at different pH values and concentrations by a combination of hydrophobic and electrostatic interactions. Considering that the highest enzymatic activity was obtained by adsorbing the protein at pH 5.7 and 0.1 mg·mL-1, our results indicate that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity. ·mL-1, our results indicate that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity.