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Expression of L-asparaginase from Erwinia chrysanthemi in cell-free protein synthesis technology

Grant number: 18/15041-8
Support type:Scholarships in Brazil - Master
Effective date (Start): November 01, 2018
Effective date (End): September 30, 2020
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Cooperation agreement: Coordination of Improvement of Higher Education Personnel (CAPES)
Principal researcher:Gisele Monteiro
Grantee:Guilherme Meira Lima
Home Institution: Faculdade de Ciências Farmacêuticas (FCF). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated research grant:13/08617-7 - Production of extracellular L-asparaginase: from bioprospecting to the engineering of an antileukemic biopharmaceutical, AP.TEM
Associated scholarship(s):19/09354-6 - Directed evolution of L-asparaginase for improving in vivo stability, BE.EP.MS

Abstract

L-Asparaginase (L-ASNase) is an important biopharmaceutical used for the treatment of acute lymphoblastic leukemia. Since L-ASNase is a biological product isolated from bacteria, extensive purification steps are necessary to obtain a pure preparation, which in turn, negatively impacts the costs related to its manufacturing. More economical and efficient alternatives to obtain this bioproduct are therefore required. In this context, we propose to evaluate the possibility to use cell-free protein synthesis systems in order to obtain a pure Erwinia chrysanthemi recombinant L-ASNase. The technology consists in the use of cellular extracts and energetic substrates capable of expressing recombinant proteins in vitro, thus dispensing the use of living cells in the process. The technology has demonstrated high protein expression efficiency, it is scalable to different reaction volumes and the open environment allows for greater process control and immediate evaluation of protein expression levels achieved. The expression of L-ASNase in this technology would simplify its biotechnological process and facilitate the study and characterization of novel forms of the enzyme, in addition to contributing to the improvement and advancement of cell-free protein synthesis technology within the biopharmaceutical industry.

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