Lignin Peroxidase from Streptomyces viridosporus T7A: Enzyme Concentration Using Ultrafiltration |
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Authors: | Leda M F Gottschalk Elba P S Bon Ronaldo Nobrega |
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Institution: | (1) Departamento de Bioquímica, IQ, CT, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21949-900, Brazil;(2) Programa de Engenharia Química, COPPE, CT, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil |
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Abstract: | It is well known that lignin degradation is a key step in the natural process of biomass decay whereby oxidative enzymes such
as laccases and high redox potential ligninolytic peroxidases and oxidases play a central role. More recently, the importance
of these enzymes has increased because of their prospective industrial use for the degradation of the biomass lignin to increase
the accessibility of the cellulose and hemicellulose moieties to be used as renewable material for the production of fuels
and chemicals. These biocatalysts also present potential application on environmental biocatalysis for the degradation of
xenobiotics and recalcitrant pollutants. However, the cost for these enzymes production, separation, and concentration must
be low to permit its industrial use. This work studied the concentration of lignin peroxidase (LiP), produced by Streptomyces viridosporus T7A, by ultrafiltration, in a laboratory-stirred cell, loaded with polysulfone (PS) or cellulose acetate (CA) membranes with
molecular weight cutoffs (MWCO) of 10, 20, and 50 KDa. Experiments were carried out at 25 °C and pH 7.0 in accordance to the
enzyme stability profile. The best process conditions and enzyme yield were obtained using a PS membrane with 10 KDa MWCO,
whereby it was observed a tenfold LiP activity increase, reaching 1,000 U/L and 90% enzyme activity upholding. |
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Keywords: | Streptomyces viridosporus Lignin peroxidase Ultrafiltration Enzyme concentration Enzyme stability |
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