Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS.

In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by AChE and releases electrons, making it possible to measure current values in accordance with the amount of substrate using LAAS. When KCl solution was used as the supporting electrolyte and an Ag/AgCl reference electrode as the counter electrode, a correlation between substrate concentration and reaction was confirmed in the range of 1 μM–10 mM. Malathion was then used as an inhibitor of AChE. Malathion phosphorylates and inactivates AChE, which prevents substrate hydrolysis and is expected to decrease the current value. Experimental results showed a decrease in sensor response correlated with inhibitor concentration. [ABSTRACT FROM AUTHOR]