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Fibrinolytic protease aqueous two-phase systems extractive fermentation

Thiago Pajeú Nascimento, Amanda Emmanuelle Sales, Camila Souza Porto, Romero Marcos Pedrosa Brandão, Galba Maria de Campos-Takaki, José Antônio Couto Teixeira, Tatiana Souza Porto, Ana Lúcia Figueiredo Porto, Attilio Converti
A fibrinolytic protease from M. subtilissimus UCP 1262 was recovered and partially purified by polyethylene glycol (PEG)/sodium sulfate aqueous two-phase systems (ATPS). The simultaneous influence of PEG molar mass, PEG concentration and sulfate concentration on the enzyme recovery was first investigated using a 2(3) full factorial design, and the Response Surface Methodology used to identify the optimum conditions for enzyme extraction by ATPS. Once the best PEG molar mass for the process had been selected (6000g/mol), a two-factor central composite rotary design was applied to better evaluate the effects of the other two independent variables...
July 1, 2016: Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Amanda Emmanuelle Sales, Fabiana América Silva Dantas de Souza, José Antônio Teixeira, Tatiana Souza Porto, Ana Lúcia Figueiredo Porto
Fibrinolytic proteases are enzymes that degrade fibrin; these enzymes are a promising alternative for thrombolytic therapy, and microorganisms produce them. The aim of this study was to evaluate the optimum conditions for the integrated production and purification of fibrinolytic protease from Bacillus sp. UFPEDA 485. Extractive fermentation was carried out in a culture medium containing soybean flour and by adding polyethylene glycol (PEG) and Na2SO4 according to a 2(3) experimental design. In all assays, the enzyme preferentially partitioned to the bottom phase (K < 1), with an optimum activity of 835 U ml(-1) in the bottom phase (salt-rich phase)...
August 2013: Applied Biochemistry and Biotechnology
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