Study on extraction, purification and characterization of a novel peroxidase from white Spanish broom (Cytisus multiflorus)
Peroxidases (EC 1.11.1.7) are a large group of enzymes widely distributed in the plant kingdom. The present work describes a study on the isolation, purification and some features of a novel peroxidase from white Spanish broom (Cytisus multiflorus), a tree legume very abundant in the northern half o...
| Autores: | , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Fecha de publicación: | 2016 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/144106 |
| Acceso en línea: | http://hdl.handle.net/10261/144106 |
| Access Level: | acceso abierto |
| Palabra clave: | peroxidase protein purification Cytisus multiflorus Chromatography |
| Sumario: | Peroxidases (EC 1.11.1.7) are a large group of enzymes widely distributed in the plant kingdom. The present work describes a study on the isolation, purification and some features of a novel peroxidase from white Spanish broom (Cytisus multiflorus), a tree legume very abundant in the northern half of Spain and Portugal. Optimal conditions are proposed for enzyme extraction, removal of phenolic compounds and enzyme purification by consecutive hydrophobic, ion-exchange and size-exclusion chromatographies. Peroxidase from Cytisus multiflorus (CMP) was found to have a molecular weight of 49 kDa. The spectrum of CMP showed a Soret band at 403 nm with a Rz factor of 3.3. Substrate specificity and the effect of some variables on the activity of CMP with guaiacol as cosubstrate have also been investigated. |
|---|