The present study demonstrates the production and characterization of recombinant thermostable
cellulase from this hyperthermophile and the utilization of this
cellulase for paper de-inking process.
We have previously produced recombinant thermostable phytase and now we have characterized the
cellulase.
Both fresh or wilted forages were then treated as follows: control (untreated), Acremonium
cellulase (AC, Meiji Seika Pharma Co., Ltd, Tokyo, Japan): AC 0.0025%, AC 0.005%, AC 0.01%, Trichoderma
cellulase (TC, Meiji Seika Pharma Co., Ltd, Japan): TC 0.0025%, TC 0.005%, and TC 0.01%.
Kudanga & Mewenje (2005) found a higher growth in some filamentous fungi on CMC medium due to the ability of CMC to act as an indirect inducer of
cellulase production.
Enzymatic hydrolysis of the alkali-pretreated straw (2 M NOH-treated biomass) was carried out in a tube with a 30 ml reaction volume using Cellic CTec2
cellulase. 10% (w/v) pretreated biomass was soaked in phosphate buffer (pH 6.0) containing the
cellulase with 10~50 FPU (filter paper unit) per gram of dry biomass.
Taken together, these results showed that, although the
cellulase gene expression profile is similar during T.
Enzymes included
cellulase (15000 U/g; Fine Chemical Research Institute, Tianjin City, China), saccharifying enzyme (100000 U/g; Beijing Aoboxing Biotechnology, LLC), phytase (5000 U/g), and pectinase (10000 U/g; Shandong Sukahan Bio-technology Co., Ltd.).
The results indicate that Trichoderma viride produces three
cellulase enzymes i.e.
Singhania, Sukumaran, and Pandey (2007) obtained total
cellulase activity of 0.17 U [g.sup.-1] after 5 days of culture, using T.
The growing interest in
cellulase production has been focused in improving the process economics of various biotechnological industries [7].