Obtención y purificación de extractos de la enzima monóxido de carbono deshidrogenasa de Oligotropha carboxidovorans (cepa OM 5) con actividad de oxidación de monóxido de carbono detectable electroquímicamente por medio de un microelectrodo de platin
Extracts of the enzyme carbon monoxide dehydrogenase capable to oxidize carbon monoxide to CO2 were obtained from the carboxidotrophic bacteria Oligotropha carboxidovorans OM5 cultivated under aerobic conditions in a mineral medium saturated with CO. The extracts were obtained disrupting cells by so...
- Autores:
-
Cuervo, Raúl A.
Hurtado, Clara
Gómez, Diana M.
Benítez, Neyla
Torres, Walter
Larmat, Fernando E.
Bravo, Enrique
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2006
- Institución:
- Universidad Autónoma de Occidente
- Repositorio:
- RED: Repositorio Educativo Digital UAO
- Idioma:
- spa
- OAI Identifier:
- oai:red.uao.edu.co:10614/245
- Acceso en línea:
- http://hdl.handle.net/10614/245
- Palabra clave:
- Oligotropha carboxidovorans cepa OM5
Monóxido de carbono
Electroquímica
Carbon monoxide
Electrochemistry
Dehydrogenases
- Rights
- openAccess
- License
- Derechos Reservados - Universidad Autónoma de Occidente
| Summary: | Extracts of the enzyme carbon monoxide dehydrogenase capable to oxidize carbon monoxide to CO2 were obtained from the carboxidotrophic bacteria Oligotropha carboxidovorans OM5 cultivated under aerobic conditions in a mineral medium saturated with CO. The extracts were obtained disrupting cells by sonication and purification by molecular size-exclusion chromatography and ion-exchange chromatography. The enzymatic activity of the extracts was measured using methylene blue as an artificial electronic acceptor in the oxidation of the CO to CO2. Crude and purified extracts showed enzymatic activity detectable by spectrophotometry. The maximum grade of purification obtained was 200 times and specific enzymatic activities were achieved in the range from 0.01 to 2.0 mU/mg of protein. Electrochemical assays using a platinum microelectrode and methylene blue as an electronic mediator showed an increase of the anodic current when the substrate carbon monoxide was added to the cell that contained the enzymatic extract. These results encourage the construction of an electrochemical biosensor for the detection of carbon monoxide using enzymatic extracts obtained from carboxidotrophic bacteria. |
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