Key enzymes of glycerol metabolism were detected in the cells of surfactants producers Rhodococcus erythropolis IMV Ac-5017 and Acinetobacter calcaaceticus IMV B-7241 grown on glycerol. It has been established that in the both strains glycerol catabolism to dihydroxyacetonephosphate (the intermediate of glycolysis) may be performed in two ways: through glycerol-3-phosphate (glycerol kinase activity 740-840 nmol min(-1) mg(-1) of protein) and through dihydroxyacetone. Glycerol oxidation to dihydroxyacetone in the strains IMV B-7241 and Ac-5017 is catalised by pyrrholo-quinolinquinone-dependent glycerol dehydrogenases and nitroso-N,N-dimethylaniline-dependent alcohol dehydrogenases. Both glyoxylate cycle and phosphoenol pyruvate(PEP)-carboxylase function as anaplerotic paths in R. erythropolis IMV Ac-5017, and only PEP-carboxylase reaction (1045 +/- 52 nmol min(-1) mg(-1) of proteins) functions in A. calcoaceticus IMV B-7241. The data obtained serve as the basis for theoretical calculations of optimal molar ratio of concentrations of energetically nonequivalent substrates for intensifying the surfactants synthesis on their mixture.
