[Purification of microbial asparaginases by the aid of affinity chromatography]

Asparaginases from Escherichia coli and Erwinia caratovora were isolated and purified by column chromatography with a specific sorbent (sepharose, covalently bound to N-alpha-(6-aminohexyl)-D-asparagine). Homogenous asparaginase from E. coli was isolated by one-step procedure, while the enzyme from Er. carotovara was 50-60-fold purified. Asparaginase from Mycobacterium n. sp. was found not to bind with the specific sorbent.