ABSTRACT
The feasibility of electrosynthesis involving the use of biocatalysts has been demonstrated in a model reaction of hydrocortisone oxidation to prednisolone catalyzed by Arthrobacter globiformis cells. Electrochemical regeneration of phenazine methosulfate, an artificial electron acceptor, was performed, using electrodes made of different materials. Transformation products were analyzed by high performance liquid chromatography.
Subject(s)
Steroids/biosynthesis , Arthrobacter/metabolism , Catalysis , ElectrochemistryABSTRACT
Experiments were carried out to study the effect of polymerization conditions and polyacrylamide gel structure on the enzyme activity of Mycobacterium phlei immobilized cells degrading sterols to C19-steroids. The modified sterol 4-chlostene-3(O-carboxymethyl)oxime was used as substrate. The polymerization conditions (the number of the cells incorporated and the reaction temperature) significantly affected the ability of the immobilized cells to degrade the sterol side chain. The monomer contact produced no negative effect on the cellular enzymic activity. The following conditions of immobilization and transformation appear to be optimal: cell incorporation into 10% gel, monomer (AA:MBA) ratio 95:5, polymerization temperature 2-8 degrees C, polymerization mixture biomass 40 mg/ml, granule size about 1 mm. Enzymic activity can be substantially increased via cell incubation in the nutrient medium.
Subject(s)
Acrylic Resins/pharmacology , Mycobacterium phlei/enzymology , Mycobacterium/enzymology , Sterols/metabolism , Biotransformation/drug effects , Fermentation/drug effects , Mycobacterium phlei/drug effects , Structure-Activity Relationship , TemperatureABSTRACT
A method is described for obtaining epiprednisolone and its 21-acetate by means of microbiological 1,2-dehydration by a culture of Mycobacterium globiforme 193. The substrate, epihydrocortisone or its 21-acetate, is added in the form of a microcrystalline suspension at a concentration of 25-100 g/liter medium.
Subject(s)
Hydrocortisone/analogs & derivatives , Hydrocortisone/metabolism , Mycobacterium/metabolism , Crystallography , Prednisolone/analogs & derivatives , Prednisolone/biosynthesisABSTRACT
The process of transformation of microcystalline acetate cortisone by two mycobacteria (Mycobacterium album and Mycobacterium globiforme) has been studied. Optimal conditions for the process have been established: amount of biomass of both cultures, concentration of the initial substrate and required concentration of the surfactant--antifoamsilane. The anzymic activity of the cultures reaches maximum if the following three requirements are met: utilization of cells separated from the medium, substrate in the microcrystalline state and surfactant of the antifoamsilane type.
