Published in Scientific Bulletin. Series F. Biotechnologies, Vol. XXIV
Written by Georgiana MICU, Florentina ISRAEL-ROMING, Călina Petruța CORNEA
L-asparaginase is a hydrolase able to mediate the cleavage reaction of the amide bond from asparagine to ammonia and aspartate. This hydrolysis reaction plays a very important role in the medicine, bringing the solution to diseases considered incurable such as acute lymphoblastic leukemia (ALL), malignant diseases of the lymphoid system, different lymphomas, being a treatment used in chemotherapy schemes. Despite the adverse effects that it can trigger in the body, L-asparaginase remains the main treatment for such diseases. It is well known that microorganisms, mainly bacteria, are able to produce important quantities of L-asparaginase. However, the level of this enzyme need to be improved in order to reduce the costs, and this could be realized both by identification of new microbial producers or optimization of the production technologies. Moreover, the new sources of L-asparaginase must be free of glutaminase and urease activity, these enzymes being involved in the side effects of enzymatic treatment of ALL. For this reason, the identification of new sources of L-asparaginase, free of glutaminase as well as urease, remains an important goal for researches in domain. The present review aims to discuss the microbial sources of L-asparaginase, the methods used for screening new microbial strains isolated from different sources able to produce large quantities of L-asparaginase, the molecular aspects of the main enzyme producers, as well as the characteristics of enzymes and their applications.
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