L-Asparaginase II was synthesized at constant rates by Escherichia coli under
anaerobic conditions. The enzyme was produced optimally by bacteria grown
between pH 7 and 8 at 37 C. Although some enzyme was formed aerobically, between
100 and 1,000 times more asparaginase II was produced during anaerobic
growth in media enriched with high concentrations of a variety of amino acids.
Bacteria grown under these conditions should provide a rich starting material for
the large-scale production of the enzyme. No single amino acid specifically induced
the synthesis of the asparaginase, nor did L-asparagine, even when it was used as
the only source of nitrogen. The enzyme was produced at lower rates in the presence
of sugars; glucose was the most inhibitory.