DETERMINATION OF ACETYLCHOLINESTERASE (AChE) ENZYME ACTIVITY IN LOCAL INSECTS

This article examines the activity and kinetics of the enzyme acetylcholinesterase (AChE), which catalyzes the hydrolysis of acetylcholine (ACh), using the example of Moroccan and Vokhinsk locusts (Gampsocleis buergeri). Enzyme activity was determined using the Ellman method. High-quality reagents (Sigma Aldrich), such as phosphate buffer solution, ACh substrate, and Ellman reagent, were used in the experiments. Optical density was determined using a spectrophotometric method. Based on the data obtained, the kinetics of acetylcholinesterase enzyme activity in insects was studied. It was found that the Michaelis-Menten constant (Km) and the maximum reaction rate (Vmax) for the Vokhinsk locust are Km = 6.05•10-5 and Vmax = 5.4•10-6, while for Moroccan locusts these values are Km = 1.06•10-4 and Vmax = 7.84•10-6, which was determined by constructing a Lineweaver-Burk plot. A comparative analysis showed that the metabolic rate of the Vakh locust is more intense than that of the Moroccan locust, which is confirmed by the reaction rate values and the Michaelis-Menten constant.