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.

中文翻译：

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使用二维电化学传感器 LAAS 测量乙酰胆碱酯酶

在本研究中，我们使用光可寻址电流传感器 (LAAS) 测量乙酰胆碱酯酶 (AChE) 的酶活性，这是一种电化学传感器，可以轻松测量多个样品的氧化还原电流值。乙酰硫代胆碱（ATCh）用作底物。ATCh被AChE水解并释放电子，从而可以使用LAAS测量与底物量相应的电流值。当使用 KCl 溶液作为支持电解质、Ag/AgCl 参比电极作为对电极时，底物浓度与反应之间的相关性在 1 μM–10 mM 范围内得到证实。随后马拉硫磷被用作AChE抑制剂。马拉硫磷会磷酸化并灭活 AChE，从而防止底物水解并有望降低电流值。实验结果表明传感器响应的降低与抑制剂浓度相关。