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.