NDLI: A Simple Colorimetric Enzymatic-Assay for Okadaic Acid Detection Based on the Immobilization of Protein Phosphatase 2A in Sol-Gel

Content Provider	Springer Nature Link
Author	Hayat, Akhtar Barthelmebs, Lise Marty, Jean Louis
Copyright Year	2011
Abstract	Okadaic acid (OA), a lipophilic toxin, is produced by Dinophysis and Prorocentrum, and causes diarrheic shellfish poisoning to humans. The mechanism of OA action is based on the reversible inhibition of protein phosphatase type 2A (PP2A) by the toxin. Therefore, this inhibition could be used to develop assay for OA detection. In this work, a colorimetric test based on the PP2A inhibition was developed for OA detection. PP2A from GTP and Millipore was immobilized on silica sol-gel, and the detection was performed. A limit of detection of 0.29 and 1.14 μg/L was respectively observed for enzyme from GTP and Millipore. The immobilization technique provided a tool to preserve the enzymatic activity, which is very unstable in solution. The PP2A immobilized sol-gel exhibited a storage stability of near 5 months, when microtiter plate with enzyme-immobilized polymer was kept at −18C°. The combination of the simplicity of the colorimetric method, along with long storage stability achieved by sol-gel immobilization, demonstrated the potentiality of this technique to be used for commercial purpose.
Starting Page	47
Ending Page	56
Page Count	10
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	166
Issue Number	1
e-ISSN	15590291
Language	English
Publisher	Humana Press Inc
Publisher Date	2011-10-08
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Okadaic acid Protein phosphatase 2A Sol gel Storage test Colorimetric enzymatic-assay Biochemistry Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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