High Redox Potential Cathode Based on Laccase Covalently Attached to Gold Electrode
A new strategy for oriented covalent immobilization of Trametes hirsuta laccase on gold electrodes is presented. The strategy is based on the gold surface modification with a mixed monolayer of an aromatic diazonium salt derivative and 6-mercapto-1-hexanol for further use as scaffold for the enzyme’...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2011 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/54208 |
| Acceso en línea: | http://hdl.handle.net/10261/54208 |
| Access Level: | acceso abierto |
| Palabra clave: | Laccase Gold Biocathode Diazonium salt Direct electron transfer |
| Sumario: | A new strategy for oriented covalent immobilization of Trametes hirsuta laccase on gold electrodes is presented. The strategy is based on the gold surface modification with a mixed monolayer of an aromatic diazonium salt derivative and 6-mercapto-1-hexanol for further use as scaffold for the enzyme’s covalent linkage. This strategy offers a variety of advantages such as high stability and laccase-friendly support morphology, which turns it into a suitable metal-enzyme interface. Conditions aiming at optimum orientation for direct electron transfer (DET) via the T1 copper site were studied. Current density values up to 40 μA·cm-2 were measured for the electrocatalytic reduction of O2 in absence of redox mediators. This strategy is a big step forward in the development of laccase-modified gold electrodes for bioelectrocatalytic reduction of O2. |
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