The effect of cavitating 22 kHz ultrasound on aqueous solutions of hyd
rogen peroxide-consuming enzymes, catalase and peroxidases, both plant
(horseradish peroxidase) and animal (lactoperoxidase) was studied. Ca
talase did not undergo inactivation during sonication, whereas activit
y of peroxidases decreased with increased duration of sonication. It i
s suggested, basing on the absorption spectra, that some conformationa
l changes occur in peroxidases upon sonolysis. It is concluded from th
e experiments with free radical scavengers that partial enzyme inactiv
ation and modification has not a chemical but a mechanical basis.