151
Views
6
CrossRef citations to date
0
Altmetric
Original Articles

Cloning, Sequencing, and Heterologous Expression of a Cellobiohydrolase cDNA from the Basidiomycete Corticium rolfsii

, , , &
Pages 1319-1326 | Received 24 Dec 2002, Accepted 12 Mar 2003, Published online: 22 May 2014

  • 1) Sasaki, H., Kurosawa, K., and Takao, S., Screening of microorganisms for raw starch saccharifying enzyme production. Agric. Biol. Chem., 50, 1661-1664 (1986).
  • 2) Takao, S., Sasaki, H., Kurosawa, K., Tanida, M., and Kamagata, Y., Production of a raw starch saccharifying enzyme by Corticium rolfsii. Agric. Biol. Chem., 50, 1979-1987 (1986).
  • 3) Shewale, J. G., and Sadana, J. C., Purification, characterization, and properties of β-glucosidase enzymes from Sclerotium rolfsii. Arch. Biochem. Biophys., 207, 185-196 (1981).
  • 4) Sadana, J. C., Shewale, J. G., and Patil, R. V., β-D-glucosidases of Sclerotium rolfsii: Substrate specificity and mode of action. Carbohydr. Res., 118, 205-214 (1983).
  • 5) Sadana, J. C., Lachke, A. H., and Patil, R. V., Endo-(1→4)-β-D-glucanases from Sclerotium rolfsii: Purification, substrate specificity, and mode of action. Carbohydr. Res., 133, 297-312 (1984).
  • 6) Patil, R. V., and Sadana, J. C., The purification and properties of (1→4)-β-D-glucan cellobiohydrolase from Sclerotium rolfsii: Substrate specificity and mode of action. Can. J. Biochem. Cell. Biol., 62, 920-926 (1984).
  • 7) Sadana, J. C., and Patil, R. V., Endo-type mode of action of (1→4)-β-D-glucan cellobiohydrolase from Sclerotium rolfsii. Can. J. Biochem. Cell. Biol., 63, 1250-1252 (1985).
  • 8) Sadana, J. C., and Patil, R. V., Synergism between enzymes of Sclerotium rolfsii involved in the solubilization of crystalline cellulose. Carbohydr. Res., 140, 111-120 (1985).
  • 9) Kurosawa, K., Hosoguchi, M., Hariantono, J., Sasaki, H., and Takao, S., Degradation of tough materials by cellulase from Corticium rolfsii. Agric. Biol. Chem., 53, 931-937 (1989).
  • 10) Mandels, M., Microbial sources of cellulase. Biotechnol. Bioeng. Symp., 5, 81-105 (1975).
  • 11) Mandels, M., and Sternberg, D., Recent advances in cellulase technology. J. Ferment. Technol., 54, 267-286 (1976).
  • 12) Klyosov, A. A., Trends in biochemistry and enzymology of cellulose degradation. Biochemistry, 29, 10577-10585 (1990).
  • 13) Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York (1989).
  • 14) Gomi, K., Iimura, Y., and Hara, S., Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene. Agric. Biol. Chem., 51, 2549-2555 (1987).
  • 15) Ogawa, M., Kitamoto, K., Gomi, K., Kumagai, C., and Tamura, G., DDBJ Accession No. D28484 (1994).
  • 16) Yamanobe, T., Mitsuishi, Y., and Takasaki, Y., Isolation of a cellulolytic enzyme producing microorganism, culture conditions and some properties of the enzymes. Agric. Biol. Chem., 51, 65-74 (1987).
  • 17) Somogyi, M. J., Notes on sugar determination. J. Biol. Chem., 195, 19-23 (1952).
  • 18) Laemmli, U. K., Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
  • 19) Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., Current “Protocols in Molecular Biology”, Greene Publishing Associates and Wiley-Interscience (1987).
  • 20) Koch, A., Weigel, C. T. O., and Schulz, G., Cloning, sequencing, and heterologous expression of a cellulase-encoding cDNA (cbh1) from Penicillium janthinellum. Gene, 124, 57-65 (1993).
  • 21) Hecker, K. H., and Roux, K. H., High and low temperatures increase both specificity and yield in touchdown and stepdown PCR. BioTechniques, 20, 478-480 (1996).
  • 22) De Oliviera, A. M., and Radford, A., Sequence of cbh-1 of Humicola grisea var. thermoidea. Nucleic acids Res., 18, 668 (1990).
  • 23) Taleb, F., and Radford, A., The cellulase complex of Neurospora crassa: cbh-1 cloning, sequencing and homologies. Gene, 161, 137-138 (1995).
  • 24) Shoemaker, S., Schweickart, V., Landner, M., Gelfand, D., Kwok, S., Myambo, K., and Innis, M. A., Molecular cloning of exo-hydrolases I derived from Trichoderma reesei strain L27. Bio/Thechnol., 1, 691-696 (1983).
  • 25) Sims, P. F. G., James, C., and Broda, P., The identification, molecular cloning and characterization of a gene from Phanerochaete chrysosporium that shows strong homology to the ex-cellobiohydrolase I gene from Trichoderma reesei. Gene, 74, 411-422 (1988).
  • 26) Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
  • 27) Divne, C., Ståhlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J. K. C., Teeri, T. T., and Jones, A., The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science, 265, 524-528 (1994).
  • 28) Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C. Jr., and Warren, R. A. J., Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Rev., 55, 303-315 (1991).
  • 29) Kanda, T., Nakakubo, S., Wakabayashi, K., and Nisizawa, K., Purification and properties of an exo-cellulase of avicelase type from a wood-rotting fungus, Irpex lacteus (Polyporus tulipiferae). J. Biochem., 84, 1217-1226 (1978).
  • 30) 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).
  • 31) Hoshino, E., and Kanda, T., Scope and mechanism of cellulase action on different cellulosic substrates. Oyo Toshitsu Kagaku (in Japanese), 44, 87-104 (1997).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.