[Study of the carbohydrate metabolic enzyme activity of Act. noursei]

Activity of aldolase and threosophosphate dehydrogenase, transketolase and phosphogluconate dehydrogenase in Act. noursei, strain 153 and its inactive mutant 149 was studied comparatively. The enzyme activity of the inactive mutant was investigated in the absence of the antibiotic production and under conditions of reduced biosynthesis of nystatin in this strain after addition of the fermentation broth filtrate of the inactive mutant 369 to the medium. The activity of the enzymes of the hexosomonophosphate metabolic pathway in the active strain 153 of Act. noursei was 2-4 times higher than that of the inactive mutant 149. The activity of the enzymes of the hexosomonophosphate metabolic pathways increased and reached the level of the enzyme of the active mutant. The high level of the enzyme activity of the hexosomonophosphate glycolysis pathway is probably one of the necessary conditions for nystatin production.