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

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

Use of different templates on SAPO-34 synthesis: Effect on the acidity and catalytic activity in the MTO reaction

Teresa Álvaro Muñoz, Carlos Márquez Álvarez, Enrique Sastre
Catalysis Today
SAPO-34 molecular sieves have been synthesized with different structur...

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

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

Materiales MOF para el almacenamiento de hidrógeno

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

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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