Biopolym. Cell. 2016; 32(4):271-278.
Molecular and Cell Biotechnologies
Inhibition of immobilized acetylcholinesterase by aflatoxin B1 in a potentiometric biosensor
1, 2, 3Stepurska K. V., 2Korobko M. I., 1Arkhypova V. M., 1, 2Soldatkin O. O., 3Lagarde F., 1, 2Soldatkin A. P., 1, 2Dzyadevych S. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Institute of High Technologies,
    Taras Shevchenko National University of Kyiv
    2, korp.5, Pr. Akademika Hlushkova, Kyiv, Ukraine, 03022
  3. University Claude Bernard Lyon 1, Institute of Analytical Sciences, UMR5280 CNRS/UCBL/ENS,
    5, rue de la Doua, Villeurbanne, France, 69100


Aim. To identify a type of inhibition of immobilized acetylcholinesterase by aflatoxin B1. Methods. A bioselective element of the potentiometric biosensor was created using acetylcholinesterase, which was covalently immobilized on the surface of the pH-FET sensor by glutaraldehyde crosslinking with bovine serum albumin. Results. Optimal conditions for the potentiometric biosensor operation such as pH-optimum of the enzyme action and its inhibition were defined. An apparent Michaelis constant, as well as a maximum initial reaction rate of immobilized acetylcholinesterase as a part of the biosensor were determined. The type of reversible inhibition of immobilized acetylcholinesterase by aflatoxin B1 in potentiometric biosensor was identified by using a new graphical “degree of inhibition” method and the obtained result was confirmed with one of the tradi-tional methods, such as the Lineweaver-Burk plot. Conclusions. This study helps to understand the mechanisms of enzyme inhibition in biosensors and brings the biosensor implementation closer.
Keywords: biosensor, immobilized acetylcholinesterase, type of inhibition, aflatoxin B1, potentiometric transducer


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