Authors: Leda M F Gottschalk Elba P S Bon Ronaldo Nobrega
Publish Date: 2008/03/20
Volume: 147, Issue: 1-3, Pages: 23-32
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 laboratorystirred 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 70 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 1000 U/L and 90 enzyme activity upholding
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