Abstract
The objective of this work is to investigate the utilization of two abundant agricultural residues in Brazil for the production and application of cellulolytic enzymes. Different materials obtained after pretreatment of sugarcane bagasse, as well as pure synthetic substrates, were considered for cellulase production by Penicillium funiculosum. The best results for FPase (354 U L−1) and β-glucosidase (1,835 U L−1) production were observed when sugarcane bagasse partially delignified cellulignin (PDC) was used. The crude extract obtained from PDC fermentation was then partially characterized. Optimal temperatures for cellulase action ranged from 52 to 58°C and pH values of around 4.9 contributed to maximum enzyme activity. At 37°C, the cellulases were highly stable, losing less than 15% of their initial activity after 23 h of incubation. There was no detection of proteases in the P. funiculosum extract, but other hydrolases, such as endoxylanases, were identified (147 U L−1). Finally, when compared to commercial preparations, the cellulolytic complex from P. funiculosum showed more well-balanced amounts of β-glucosidase, endo- and exoglucanase, resulting in the desired performance in the presence of a lignocellulosic material. Cellulases from this filamentous fungus had a higher glucose production rate (470 mg L−1 h−1) when incubated with corn cob than with Celluclast®, GC 220® and Spezyme® (312, 454 and 400 mg L−1 h−1, respectively).
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Acknowledgments
To Dr. Alexandre Soares dos Santos, Marcela C. Ferreira, Juliana C. Cruz, Daniele F. Carvalho, Kelly C. N. R. Pedro and Roberto Maeda, for their technical assistance. We are also grateful to the Brazilian Council for Research (CNPq), the Rio de Janeiro State Foundation for Science and Technology (FAPERJ), and the Brazilian Petroleum Company (PETROBRAS) for financial support.
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de Castro, A.M., de Albuquerque de Carvalho, M.L., Leite, S.G.F. et al. Cellulases from Penicillium funiculosum: production, properties and application to cellulose hydrolysis. J Ind Microbiol Biotechnol 37, 151–158 (2010). https://doi.org/10.1007/s10295-009-0656-2
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DOI: https://doi.org/10.1007/s10295-009-0656-2