- 1) Jeewon, L., Biological conversion of lignocellulosic biomass to ethanol. J. Biotechnol., 56, 1–24 (1997).
- 2) Zaldivar, J., Nielsen, J., and Olsson, L., Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl. Microbiol. Biotechnol., 56, 17–34 (2001).
- 3) Palmqvist, E., and Hahn-Hagerdal, B., Fermentation of lignocellulosic hydrolysates II: inhibition and mechanisms of inhibition. Bioresour. Technol., 74, 25–33 (2000).
- 4) Klinke, H. B., Thomsen, A. B., and Ahring, B. K., Inhibition of ethanol-producing yeast and bacteria by degradation products produced during pre-treatment of biomass. Appl. Microbiol. Biotechnol., 16, 10–26 (2004).
- 5) Kanda, T., Wakabayashi, K., and Nisizawa, K., Purification and properties of an endo-cellulase of Avicelase type from Irpex lacteus (Polyporus tulipiferae). J. Biochem., 79, 977–988 (1976).
- 6) Kanda, T., Nakakubo, S., Wakabayashi, K., and Nisizawa, K., Purification and properties of and exo-cellulase of Avicelase type from a wood-rotting fungus Irpex lacteus (Polyporus tulipiferae). J. Biochem., 84, 1217–1226 (1978).
- 7) Hamada, N., Ishikawa, K., Fuse, N., Kodaira, R., Shimosaka, M., Amano, Y., Kanda, T., and Okazaki, M., Purification, characterization and gene analysis of exo-cellulase II (Ex-2) from the white rot basidiomycete Irpex lacteus. J. Biosci. Bioeng., 87, 442–451 (1999).
- 8) Toda, H., Takada, S., Amano, Y., Kanda, T., Okazaki, M., and Shimosaka, M., Cloning of a cellobiohydrolase I cDNA from the white rot fungus Irpex lacteus MC-2 and its expression in Aspergillus oryzae. J. Appl. Glycosci., 52, 23–26 (2005).
- 9) Toda, H., Takada, S., Oda, M., Amano, Y., Kanda, T., Okazaki, M., and Shimosaka, M., Gene cloning of an endoglucanase from the basidiomycete Irpex lacteus and its expression in Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem., 69, 1262–1269 (2005).
- 10) Somogyi, M., Notes on sugar determination. J. Biol. Chem., 195, 19 (1952).
- 11) Nelson, N., A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem., 153, 375 (1944).
- 12) Sambrook, J., and Russell, W. D., “Molecular Cloning, a Laboratory Manual” 3rd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor (2001).
- 13) Garber, R. C., and Yoder, O. C., Isolation of DNA from filamentous fungi and separation into nuclear, mitochondrial, ribosomal, and plasmid components. Anal. Biochem., 135, 416 (1983).
- 14) Mandels, M., and Reese, E. T., Induction of cellulase in Trichoderma viride as influenced by carbon source and metals. J. Bacteriol., 73, 269–278 (1957).
- 15) Balance, D. J., Sequences important for gene expression in filamentous fungi. Yeast, 2, 229–236 (1986).
- 16) Hoffren, A. M., Teeri, T. T., and Telemen, O., Molecular dynamics simulation of fungal cellulose-binding domains: differences in molecular rigidity but a preserved cellulose binding surface. Protein Eng., 8, 443–450 (1995).
- 17) Uzcategui, E., Johansson, G., Ek, B., and Pettersson, G., The 1,4-β-D-glucan glucanohydrolases from Phanerochaete chrysosporium: re-assessment of their significance in cellulose degradation mechanisms. J. Biotechnol., 21, 143–160 (1991).
- 18) Wood, T. M., and McCras, S. I., The cellulase of Penicillium pinophilum: synergism between enzyme components in solubilizing cellulose with special reference to the involvement of two immunologically distinct cellobiohydrolases. Biochem. J., 234, 93–99 (1986).
- 19) Wood, T. M., McCrae, S. I., and Bhat, K. M., The mechanism of fungal cellulase action: synergism between enzyme components of Penicillium pinophilum cellulase in solubilizing hydrogen bond-ordered cellulose. Biochem. J., 260, 37–43 (1989).
- 20) Boisset, C., Fraschini, C., Schulein, M., Henrissat, B., and Chanzy, H., Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A. Appl. Environ. Microbiol., 66, 1444–1452 (2000).
- 21) Varrot, A., Hastrup, S., Schulein, M., and Davies, G. J., Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 Å resolution. Biochem. J., 337, 297–304 (1999).
- 22) Davies, G. J., Brzozowski, A. M., Dauter, M., Varrot, A., and Schulein, M., Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 Å resolution. Biochem. J., 348, 201–207 (2000).
- 23) Zou, J., Kleywegt, G. J., Stahlberg, J., Driguez, H., Nerinckx, W., Claeyssens, M., Koivula, A., Teeri, T. T., and Jones, T. A., Crystallographic evidence for substrate ring distortion and protein conformation changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei. Structure Fold. Des., 7, 1035–1045 (1999).
- 24) von Ossowski, I., Stahlberg, J., Koivula, A., Piens, K., Becker, D., Boer, H., Harle, R., Harris, M., Divne, C., Mahdi, S., Zhao, Y., Driguez, H., Claeyssens, M., Sinnott, M. L., and Teeri, T. T., Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A: a comparison with Phanerochaete chrysosporium Cel7D. J. Mol. Biol., 333, 817–829 (2003).
Bioscience, Biotechnology, and Biochemistry
Volume 72, 2008 - Issue 12