Interaction of sodium bis(2‐ethylhexyljt) sulfosuccinate (AOT) with catalase and horseradish peroxidase in an aqueous solution and in the reverse micelles of AOT/n‐heptane

Abstract

Some properties of catalase and horseradish peroxidase entrapped into reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane with those in an aqueous solution of AOT are compared. Secondary structure of catalase significantly changes and activity is completely lost in the presence of aqueous micellar solution of AOT. In AOT/n-heptane reverse micelles secondary structure of catalase does not change. AOT has no effect on horseradish peroxidase in aqueous solution. On the other hand slight changes in secondary structure of horseradish peroxidase in AOT/n-heptane reverse micelles appear. It is concluded that electrostatic interactions between catalase or horseradish peroxidase with AOT molecule at neutral pH are not the main factor determining reactivity of investigated enzymes in reverse micelles.