STABILITY AND STABILIZATION OF RECOMBINANT PEROXIDASE IN REVERSED MICELLES

Stability of recombinant peroxidase lacking carbohydrate residues on t he surface of the protein molecule has been characterized in reversed micelles of Aerosol OT in octane, The enzyme stability was found to de pend on the surfactant hydration degree (w(0) = [H2O]/[AOT]). Residual activity after 1 h incubation dropped to zero at w(0) = 7 but was 54% at w(0) 25. However, the residual activity levels at all values of hy dration degree were definitely low compared to that of glycosylated wi ld-type horseradish peroxidase. The stability of the enzyme apparently depends on the presence of carbohydrate residues, Stabilization of re combinant peroxidase in reversed micellar system involved sugar-contai ning co-surfactants such as Tweens and Spans is proposed. As an exampl e, addition of 1 mM Span 80 (1% relative to AOT concentration) increas ed the recombinant peroxidase stability up to that of wild-type peroxi dase.