Protein phosphatase inhibition assays for okadaic acid detection in shellfish: matrix effects, applicability and comparison with LC-MS/MS analysis
The applicability of the protein phosphatase inhibition assay (PPIA) to the determination of okadaic acid (OA) and its acyl derivatives in shellfish samples has been investigated, using a recombinant PP2A and a commercial one. Mediterranean mussel, wedge clam, Pacific oyster and flat oyster have bee...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión borrador |
| Fecha de publicación: | 2012 |
| País: | España |
| Institución: | Institut de Recerca i Tecnologia Agroalimentàries (IRTA) |
| Repositorio: | IRTA Pubpro. Open Digital Archive |
| OAI Identifier: | oai:repositori.irta.cat:20.500.12327/4497 |
| Acceso en línea: | http://hdl.handle.net/20.500.12327/4497 |
| Access Level: | acceso abierto |
| Palabra clave: | Toxines marines Espectrometria de Mases Cromatografia Líquida |
| Sumario: | The applicability of the protein phosphatase inhibition assay (PPIA) to the determination of okadaic acid (OA) and its acyl derivatives in shellfish samples has been investigated, using a recombinant PP2A and a commercial one. Mediterranean mussel, wedge clam, Pacific oyster and flat oyster have been chosen as model species. Shellfish matrix loading limits for the PPIA have been established, according to the shellfish species and the enzyme source. A synergistic inhibitory effect has been observed in the presence of OA and shellfish matrix, which has been overcome by the application of a correction factor (0.48). Finally, Mediterranean mussel samples obtained from Rı´a de Arousa during a DSP closure associated to Dinophysis acuminata, determined as positive by the mouse bioassay, have been analysed with the PPIAs. The OA equivalent contents provided by the PPIAs correlate satisfactorily with those obtained by liquid chromatography–tandem mass spectrometry (LC–MS/MS). |
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