Analytical Chemistry Department, Faculty of Sciences, University of Burgos, Pza, Misael Bañuelos s/n, 09001 Burgos, Spain.
Sci Total Environ. 2012 Jun 1;426:346-50. doi: 10.1016/j.scitotenv.2012.03.042. Epub 2012 Apr 13.
An amperometric assay based on acetylcholinesterase (AChE) inactivation has been developed for the monitoring of permethrin using a screen-printed three-electrode system. The enzyme AChE catalyzes the hydrolysis of acetylthiocholine to thiocholine, which can be electrochemically oxidized. The presence of permethrin inhibits the AChE activity, resulting in a lower thiocholine production and thus, a decrease in the amperometric oxidation current. Immobilization of AChE was performed by cross-linking giving a capability of detection of 8.1±0.4 μM. Repeatability and reproducibility of the developed AChE biosensor were also calculated, yielding values of 9.6% (n=4) and 5.4% (n=5), respectively related to the slopes of the calibration curves performed in the range from 6.2 up to 41 μM. The method was successfully applied to the determination of permethrin content in a commercial lice gel.
基于乙酰胆碱酯酶 (AChE) 失活的电流测定法已被开发出来,用于通过丝网印刷三电极系统监测氯菊酯。酶 AChE 催化乙酰硫代胆碱的水解生成硫代胆碱,后者可电化学氧化。氯菊酯的存在抑制 AChE 活性,导致硫代胆碱生成减少,因此,电流的安培氧化也随之减少。通过交联使 AChE 固定化,检测能力为 8.1±0.4 μM。还计算了所开发的 AChE 生物传感器的重复性和再现性,在 6.2 至 41 μM 的范围内进行校准曲线的斜率时,其值分别为 9.6%(n=4)和 5.4%(n=5)。该方法成功地应用于测定市售 lice gel 中的氯菊酯含量。