In the 60's and 70's of the last century many researchers were trying to purify L-Asparaginase II among others from Escherichia coli B. L-Asparaginase is an enzyme which shows anti-tumor activity, specific to acute lymphatic leukemia. Therefore, it became of great interest to pharmaceutical industry, medical and clinical research and it has been and is still used in therapeutic applications. The purity, stability and the conservation of the enzymatic activity of L-Asparaginase are the basic factors to be aware of. Recombinant E. coli BL21Gold (DE3) pET11a-ansB was used to overproduce L-Asparaginase II in higher quantities. To enhance the purity and to preserve the activity of L-Asparaginase crystallization represents a promising process which usually yields in very high quality (purity) and even high quantity. Crystallization of L-Asparaginase has already been done in past research but besides some patents there are no original references describing that process in details. Based on that literature available lab scale experiments on the purification by crystallization were successfully performed. Successfully crystallized L-Asparaginase from recombinant E. coli BL21Gold (DE3) pET11a-ansB by 1) 17percent of PEG_(6000) and 2) 50percent Methanol which shows different crystal shapes and different crystal sizes.
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