By Adam E. Golan
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Extra resources for Cellulase: Types and Action, Mechanism, and Uses (Biotechnology in Agriculture, Industry and Medicine)
1987]. The expression of catalytically active cellulases in E. coli is generally achieved at low levels due to the absence of post-translational modifications such as the glycosylation and to the intracellular accumulation of the recombinant enzymes. Most of the cellulase genes bear a signal peptide that is not well recognized by the E. coli expression system. This often lowers the production level of the recombinant proteins or even impairs their expression. The thermostable cellulase Cel12A from Rhodothermus marinus, which contains in its sequence a highly hydrophobic putative signal peptide, when cloned in E.
2008]. Analyses and annotation of the genomes of T. atroviride and T. jgipsf. html), are still in progress. The Fungus Acremonium cellulolyticus, isolated in 1987, is known to be a potent producer of cellulases as T. reesei, even if many cellulases and β-glucosidases have not been as well characterized as those produced by T. , 2007]. Since enzymatic saccharification using cellulases has proven to be a powerful method in the production of bioethanol, a comparison between cellulase activity from the two fungi against three lignocellulosic materials (eucalyptus, Douglas fir wood chip and rice straw) has been performed by Fujii et al.
0 and 50°C, respectively. 5) and at temperatures below 55 °C. It retained only 60% activity after incubation at 60°C for 1 h. The newly isolated endoglucanase from A. glaucus XC9 shares common characteristics with those from industrial cellulaseproducing Fungi, such as A. niger and T. reesei suggesting its possible use in industry. , 2010]. Several substrates were generated after different pretreatment of sugar cane bagasse, and they were 22 A. Morana, L. Maurelli, E. Ionata et al. used as carbon source for Penicillium funiculosum growth.