Production and properties of asparaginase from a new Erwinia sp.

Asparaginase production by a mesophilic strain of Erwinia sp. was examined; the maximum of activity was found at 40 degrees C and pH 8.5. Among the various carbon sources, mannitol was shown to be the best for production of activity. Inorganic nitrogen sources were better than the organic ones. The enzyme activity was not inhibited by 10 mmol/L metal ions (Na+, K+, Mg2+, Ca2+, Ba2+, Co2+, Ni2+, Zn2+); the activity was strongly inhibited by addition of EDTA. L-Arginine, DL-alanine, L-asparagine and L-glutamine stimulated the L-asparaginase production by 3.9, 1.7, 4.3 and 4.0 fold, respectively. The combination of L-arginine, L-asparagine and L-glutamine synergistically stimulated the asparaginase up to 5.8 fold.