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Type: Artigo
Title: Therapeutic L-asparaginase: Upstream, Downstream And Beyond
Author: Lopes
Andre Moreni; de Oliveira-Nascimento
Laura; Ribeiro
Artur; Tairum
Carlos Abrunhosa
Jr.; Breyer
Carlos Alexandre; de Oliveira
Marcos Antonio; Monteiro
Gisele; de Souza-Motta
Cristina Maria; Magalhaes
Perola de Oliveira; Farias Avendano
Jorge Gonzalo; Cavaco-Paulo
Artur Manuel; Mazzola
Priscila Gava; Rangel-Yagui
Carlota de Oliveira; Sette
Lara Duraes; Converti
Attilio; Pessoa
Abstract: l-asparaginase (l-asparagine amino hydrolase, E.C. is an enzyme clinically accepted as an antitumor agent to treat acute lymphoblastic leukemia and lymphosarcoma. It catalyzes l-asparagine (Asn) hydrolysis to l-aspartate and ammonia, and Asn effective depletion results in cytotoxicity to leukemic cells. Microbial l-asparaginase (ASNase) production has attracted considerable attention owing to its cost effectiveness and eco-friendliness. The focus of this review is to provide a thorough review on microbial ASNase production, with special emphasis to microbial producers, conditions of enzyme production, protein engineering, downstream processes, biochemical characteristics, enzyme stability, bioavailability, toxicity and allergy potential. Some issues are also highlighted that will have to be addressed to achieve better therapeutic results and less side effects of ASNase use in cancer treatment: (a) search for new sources of this enzyme to increase its availability as a drug; (b) production of new ASNases with improved pharmacodynamics, pharmacokinetics and toxicological profiles, and (c) improvement of ASNase production by recombinant microorganisms. In this regard, rational protein engineering, directed mutagenesis, metabolic flux analysis and optimization of purification protocols are expected to play a paramount role in the near future.
Subject: Acute Lymphoblastic Leukemia
Antineoplastic Activity
Microbial L-asparaginase Production
Editor: Taylor & Francis Inc
Citation: Critical Reviews In Biotechnology . Taylor & Francis Inc, v. 37, p. 82 - 99, 2017.
Rights: fechado
Identifier DOI: 10.3109/07388551.2015.1120705
Date Issue: 2017
Appears in Collections:Unicamp - Artigos e Outros Documentos

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