Volume- 2
Issue- 6
Year- 2015
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Dr. Pascoal José Gaspar Júnior , MsC. Camila de Melo Silva , Dr. Félix Gonçalves de Siqueira , Nilo Sobreira Silva, Dra. Fernanda Silva Torres Dr. Daniel Moreira dos Santos, MsC. Lucas Vieira de Faria , MsC. Géssyca Paula de Alvarenga Soares , Ana Paula Resende Pinto , Juraci Lourenço Teixeira , Dr. Sérgio Marangoni, Dra. Maria Elena de Lima
Screening strategies for the production of fungal holocellulases aims at obtaining enzymes that hydrolyze the lignocellulosic material from plant biomass, increasing the viability of cellulosic ethanol production. The present study evaluates the potential of Penicillium simplicissimum and Penicillium corylophilum to produce holocellulases from commercial and lignocellulosic substrates. These fungi were grown in a supplementary medium with 1.0% lignocellulosic substrate, at pH 7.0, at 108 spores.mL-1 . The supernatant was filtered and the enzyme activities were evaluated. P. simplicissimum xylanase activity on linseed substrate, after 72 and 120 h (3.8 and 3.9 IU.mL-1 , respectively), showed the highest values among all the enzymes tested. The lyophilized crude extract, after 72 h of incubation, was submitted to two chromatographic steps (gel filtration and anion exchange). A third chromatographic step using a reversed phase column, followed by mass spectrometry analyses, showed a pool of lowmolecular-weight xylanases (18831 Da). The specific xylanase activity increased considerably after anionexchange chromatography purification, from 3x10-3 atv.mg-1 to 19.2 atv.mg-1 . Maximum enzyme activity was observed with 0.5% xylan and 0.04% xylose as carbon sources. Optimum pH and temperature for xylanase activity were 4.0 and 50°C, respectively. In conclusion, the fungal strains Penicillium simplicissimum and Penicillium corylophilum are potential sources for the production of different enzymes in several lignocellulosic substrates derived from oil plants. Moreover, we purified and partially characterized a pool of xylanase enzymes from P. simplicissimum that show promising industrial application.
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Departamento de BioquÃmica, Universidade de Campinas, e Departamento de Biologia, Centro Universitário de Formiga, Formiga, MG, Brazil;
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