DIMERIZATION OF RECOMBINANT HORSERADISH-PEROXIDASE IN A REVERSED MICELLAR SYSTEM

Recombinant horseradish peroxidase reactivated from E. coil inclusion bodies was studied in a reversed micellar system of AOT in octane. The ability of the recombinant enzyme, in contrast to native horseradish peroxidase, to form a dimeric structure was found. The existence of th e dimer was proved by results of sedimentation analysis. Dimer/monomer ratio in the enzyme-containing micelles and dimer catalytic activity were found to depend on the substrate used (pyrogallol, guaiacol, o-di anisidine, o-phenylenediamine). Computer modelling was used to describ e possible structures of the dimeric recombinant horseradish peroxidas e.