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Search results (43 of 88)

Rational co-immobilization of bi-enzyme cascades on porous supports and their applications in bio-redox reactions with insitu recycling of soluble cofactors

2012
PUBLICACIONES
ChemCatChem, .
In bio-redox cascade reactions that are immobilized on porous supports...

Design of activated carbon–clay composites for effluent decontamination.

2012
Microporous and Mesoporous Materials
Adsorption offers an efficient technology for removing volatile organi...

Spectral response and stability of In2S3 as visible light-active photocatalyst

2012
Raquel Lucena García, Fernando Fresno García, J. C. Conesa
Catalysis Communications

Materiales MOF para el almacenamiento de hidrógeno

2012
M.A. Orcajo , J. A. Botas , Guillermo Calleja , Manuel Sánchez Sánchez
Anales de Química
The study of sorbent materials having prominent textural properties ga...

Combined ATR-SEIRAS and EC-STM Study of the Immobilization of Laccase on Chemically Modified Au Electrodes

2012
Cristina Vaz Dominguez, Marcos Pita Martínez, Antonio López de Lacey, Sergey Shleev , Ángel Cuesta Ciscar
Journal of Physical Chemistry CThe successive steps of laccase immobilization on chemically modified Au electrodes were monitored using ATR-SEIRAS and in situ STM. Successful covalent immobilization of the enzyme on Au electrodes modified by a mixed aminophenyl-mercaptohexanol adlayer and on Au electrodes modified by a 4-aminothiophenyl SAM via a Schiff base reaction followed by the formation of amide bonds is revealed by the emergence of the corresponding bands in the ATR-SEIRA spectra, and an enzyme coverage on aminophenyl-mercaptohexanol-modified Au electrodes of about (7.27 ± 1.93) × 1011 laccase units per cm2 was calculated from STM images. The small differences between the ATR-SEIRA spectra of the enzyme immobilized on aminophenyl-mercaptohexanol-modified Au electrodes and the ATR-SEIRA spectra of the enzyme immobilized on 4-aminothiophenyl-modified Au electrodes are attributed to a different orientation of the immobilized enzyme due to the presence on the surface of aminophenyl-mercaptohexanol-modified Au electrodes of OH functional groups that favor an orientation of laccase with the Cu T1 center of the enzyme facing the electrode surface, thus, allowing a high activity for direct electrocatalysis of the ORR at low overpotentials.
The successive steps of laccase immobilization on chemically modif...
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