| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 4545516 | Harmful Algae | 2012 | 8 Pages |
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 Ría 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).
► We evaluate the applicability of a protein phosphatase inhibition assay (PPIA). ► We compare a recombinant PP2A with a commercial one. ► We establish mussel, wedge clam, Pacific oyster and flat oyster charge limits. ► We observe a synergistic effect of okadaic acid in the presence of shellfish matrix. ► We determine okadaic acid equivalent contents in mussel samples.
