Effect of culture conditions on synthesis of L-asparaginase by Escherichia coli A-1.
The nutritional requirements and culture conditions affecting biosynthesis of L-asparaginase in a mutant of Escherichia coli HAP designated strain A-1 were studied. Asparaginase activity was increased by  the addition of L-glutamic acid, L-glutamine, or commercial-grade monosodium glutamate. The rate of enzyme synthesis was dependent on the interaction between the pH of the culture and the amount of oxygen dissolved in the medium. A critical oxygen transfer rate essential for asparaginase formation was identified, and a fermentation procedure is described in which enzyme synthesis is controlled by aeration rate. Enhancement of L-asparaginase activity by monosodium glutamate was inhibited by the presence of glucose, culture pH, chloramphenicol, and oxygen dissolved in the fermentation medium.
D001215:Asparaginase / Q000096:biosynthesis*; D002701:Chloramphenicol / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D005285:Fermentation; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D010101:Oxygen Consumption
D005971:Glutamates; D005973:Glutamine; D002701:Chloramphenicol; D001215:Asparaginase; D005947:Glucose