Actividades dihidrodiol-deshidrogenasa en Mucor circinelloides YR-1 aislada de suelo contaminado con petróleo

Abstract

After the growth of cells of strain YR-1 of Mucor circinelloides with naphthalene as sole carbon source, the presence of five different 1, 2-dihydroxi-1, 2-dihydro-naphthalenediol dehydrogenase activities were revealed by electrophoretic zymograms using (+)-cis-1(R), 2(s)-dihydroxi-1, 2-dihydronaphthalene as substrate and NADP⁺ as electron acceptor. The bands NDD1, NDD3 and NDD5 showing the highest intensity in the zymograms and by their relative electrophoretic mobilities, were purified to homogeneity by means of sequen­tial steps of electrophoresis-electroelution to know both, the molecular weight and the number of subunits that conform each activity band. The results show molecular weights of 98.64 kDa, 48.37 kDa and 102.45 kDa for the subunit of each protein band respectively. We conclude that these activities there are not enzymatic isoforms conformed by the same proteic subunit, the native enzymes have a homopolymeric structure and they do not share any protomeric subunit.