Abstract
The affinity of mushroom tyrosinase for alternariol (AOH) and alternariol monomethyl ether (AME), mycotoxins of the Alternaria alternata genus, is verified both spectroscopically and electrochemically. Commercial enzyme and fresh mushroom tissue were employed for electrochemical measurements. The results presented here demonstrate, for the first time, that both AME and AOH are substrates for mushroom tyrosinase. The kinetic parameters were evaluated from Eadie–Hofstee plots. The analytical performance was also evaluated in the detection limits 2.4×10 −5 and 1.9×10 −5 M for AME and AOH, respectively, with a linear range up to 1.8×10 −4 and 2.0×10 −4 M for the same analytes. It is concluded that the enzyme has relatively good affinities for both substrates, which is a promising result for developing an enzymatic biosensor.
Published Version
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