Аннотация:Low‐frequency electromagnetic fields, induced by alternating current, are known to
influence physicochemical properties and functioning of enzymes, including their catalytic activity.
Herein, by using atomic force microscopy (AFM) and spectrophotometry analysis in parallel, we have
investigated how the incubation near an autotransformer operated at 50 Hz influences the
physicochemical properties of horseradish peroxidase (HRP). We have found that 30 min incubation
of the enzyme above the coil of a loaded autotransformer enhances a disaggregation of HRP on mica
and the number of adsorbed enzyme particles by two orders of magnitude in comparison with the
control sample. And most interestingly, the incubation of HRP above the switched‐off transformer
for the same period of time has been found to cause a disaggregation of the enzyme, An increase in
the activity of HRP against ABTS has been observed in the both cases. We hope that the interesting
effects reported will emphasize the importance of consideration of the influence of low‐frequency
electromagnetic fields on enzymes in the design of laboratory and industrial equipment intended for
operation with enzyme systems.