[Particularities of alkane oxidation in Rhodococcus erythropolis EK-1 strain--producer of surface-active substances]

Abstract

The hexadecane oxidation of Rhodococcus erythropolls EK-1 was established to be catalyzed by the alkane hydroxylase complex containing Fe-S proteid rubredoxin. Alkane hydroxylase activity was increased twice in the presence of 10 mg/l iron ions in the cultivation medium. Sodium ions were shown to be an activator of alkane hydroxylase. Four types of alcohol dehydrogenases (NAD, NADP, pyrroloquinoline quinone and N,N-dimethyll-4-nitrosoaniline-dependent enzymes) were found in hexadecane-grown cells of R. erythropolis EK-1. The obtained data are the basis for the improvement of surface active substances technology.