Abstract
Alcohol dehydrogenase, lysozyme, and catalase were assayed after exposure to cavitating 20 kHz ultrasound for varying times. Catalase was little affected, but alcohol dehydrogenase and lysozyme were both inactivated at an exponential rate. The rate of enzyme inactivation decreased with increasing protein concentration and was inhibited by the presence of 2-mercaptoethanol. The presence of stainless steel in the sonication vessel accelerated enzyme inactivation. On the basis of the results obtained, it is suggested that the mechanism of inactivation is chemical rather than mechanical, and a comparison is made between the rate of inactivation and the yield of free radicals as measured with a radiochemical dosimeter. Suggestions are offered to minimize the sonochemical effects on proteins isolated from cells with an ultrasonic disintegrator.
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