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Kinetics of ultrasonic inactivation of peroxidase in aqueous solutions

The kinetics of the inactivation of horse-radish peroxidase in a 0.01 M phosphate citrate buffer (pH 5.4) under the action of high-frequency (2.64 MHz) ultrasound with a power input of 1 W/cm 2 was studied over a temperature range from 35.5 to 55.0°C and a concentration range from 10 to 100 nM and described by apparent first-order rate constants: k i n (total inactivation), k* i n (thermal inactivation), and k u s i n (ultrasound inactivation). These rate constants were demonstrated to be dependent on the temperature and pH value. As the concentration of peroxidase increases from 10 to 100 nM, the value of k i n changes only slightly, while k* i n decreases significantly. Poly(2-aminodisulfide-4-nitrophenol) and poly(gallic acid disulfide) cause a significant decrease in the degree of US inactivation of peroxidase: the presence of these compounds in micromolar concentrations completely stops the inactivation at 45°C. This result suggests that the HO and HO . 2 free radicals, which are generated by US cavitation, play the main role in the inactivation of the enzyme. Both these polysulfides of substituted phenols also cause a decrease in k* i n at 45°C.