306
Views
27
CrossRef citations to date
0
Altmetric
Original Articles

Production and Characterization of Recombinant Phanerochaete chrysosporium β-Glucosidase in the Methylotrophic Yeast Pichia pastoris

, , , , , & show all
Pages 1-7 | Received 14 Mar 2002, Accepted 16 Aug 2002, Published online: 22 May 2014

  • 1) Eriksson, K.-E., Enzyme mechanisms involved in cellulose hydrolysis by the rot fungus Sporotrichum pulverulentum. Biotechnol. Bioeng. Symp., 10, 317-332 (1978).
  • 2) Sternberg, D., Vijayakumar, P., and Reese, E. T., β-Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose. Can. J. Microbiol., 23, 139-147 (1977).
  • 3) Shewale, J. G., β-Glucosidase: its role in cellulase synthesis and hydrolysis of cellulase. Int. J. Biochem., 14, 435-443 (1982).
  • 4) Deshpande, V., Eriksson, K.-E., and Pettersson, B., Production, purification and partial characterization of 1,4-β-glucosidase enzymes from Sporotrichum pulverulentum. Eur. J. Biochem., 90, 191-198 (1978).
  • 5) Bao, W., Lymar, E., and Renganathan, V., Optimization of cellobiose dehydrogenase and β-glucosidase production by cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Microbiol. Biotechnol., 42, 642-646 (1994).
  • 6) Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
  • 7) 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).
  • 8) Henrissat, B., and Bairoch, A., Updating the sequence-based classification of glycosyl hydrolases. Biochem. J., 316, 695-696 (1996).
  • 9) Gaboriaud, C., Bissery, V., Benchetrit, T., and Mornon, J. P., Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett., 224, 149-155 (1987).
  • 10) Callebaut, I., Labesse, G., Durand, P., Poupon, A., Canard, L., Chomilier, J., Henrissat, B., and Mornon, J. P., Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell. Mol. Life Sci., 53, 621-645 (1997).
  • 11) Li, B., and Renganathan, V., Gene cloning and characterization of a novel cellulose-binding β-glucosidase from Phanerochaete chrysosporium. Appl. Environ. Microbiol., 64, 2748-2754 (1998).
  • 12) Harvey, A. J., Hrmova, M., De Gori, R., Varghese, J. N., and Fincher, G. B., Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins, 41, 257-269 (2000).
  • 13) Varghese, J. N., Hrmova, M., and Fincher, G. B., Three-dimensional structure of a barley β-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure, 7, 179-190 (1999).
  • 14) Lymar, E. S., Li, B., and Renganathan, V., Purification and characterization of a cellulose-binding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Environ. Microbiol., 61, 2976-2980 (1995).
  • 15) Igarashi, K., Samejima, M., Saburi, Y., Habu, N., and Eriksson, K.-E. L., Localization of cellobiose dehydrogenase in cellulose-grown cultures of Phanerochaete chrysosporium. Fungal Genet. Biol., 21, 214-222 (1997).
  • 16) Machida, M., Ohtsuki, I., Fukui, S., and Yamashita, I., Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae. Appl. Environ. Microbiol., 54, 3147-3155 (1988).
  • 17) Rajoka, M. I., Bashir, A., Hussain, S. R. A., Ghauri, M. T., Parvez, S., and Malik, K. A., Cloning and expression of β-glucosidase genes in Escherichia coli and Saccharomyces cerevisiae using shuttle vector pYES 2.0. Folia Microbiol., 43, 129-135 (1998).
  • 18) Raynal, A., and Guerineau, M., Cloning and expression of the structural gene for β-glucosidase of Kluyveromyces fragilis in Escherichia coli and Saccharomyces cerevisiae. Mol. Gen. Genet., 195, 108-115 (1984).
  • 19) Takada, G., Kawaguchi, T., Sumitani, J., and Arai, M., Expression of Aspergillus aculeatus No. F-50 cellobiohydrolase I (cbhI) and β-glucosidase 1 (bgl1) genes by Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem., 62, 1615-1618 (1998).
  • 20) Penttila, M. E., Andre, L., Lehtovaara, P., Bailey, M., Teeri, T. T., and Knowles, J. K., Efficient secretion of two cellobiohydrolases by Saccharomyces cerevisiae. Gene, 63, 103-112 (1988).
  • 21) Penttila, M. E., Andre, L., Saloheimo, M., Lehtovaara, P., and Knowles, J. K., Expression of two Trichoderma reesei endoglucanases in the yeast Saccharomyces cerevisiae. Yeast, 3, 175-185 (1987).
  • 22) Dan, S., Maton, I., Dekel, M., Bravdo, B.-A., He, S., Withers, S. G., and Shoseyov, O., Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger β-glucosidase. J. Biol. Chem., 275, 4973-4980 (2000).
  • 23) Boer, H., Teeri, T. T., and Koivula, A., Characterization of Trichoderma reesei cellobiohydrolase Cel7A secreted from Pichia pastoris using two different promoters. Biotechnol. Bioeng., 69, 486-494 (2000).
  • 24) Skory, C. D., Freer, S. N., and Bothast, R. J., Expression and secretion of the Candida wickerhami extracellular β-glucosidase gene, bglB, in Saccharomyces cerevisiae. Curr. Genet., 30, 417-422 (1996).
  • 25) Cregg, J. M., Vedvick, T. S., and Raschke, W. C., Recent advances in the expression of foreign genes in Pichia pastoris. Bio/technology, 11, 905-910 (1993).
  • 26) Heimo, H., Palmu, K., and Suominen, I., Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain. Protein Expr. Purif., 10, 70-79 (1997).
  • 28) Johnsrud, S. C., and Eriksson, K.-E., Cross-breeding of selected and mutated homokaryotic strains of Phanerochaete chrysosporium. K-3: new cellulase deficient strains with increased ability to degrade lignin. Appl. Microbiol. Biotechnol., 21, 320-327 (1985).
  • 29) Kremer, S. M., and Wood, P. M., Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase. Eur. J. Biochem., 205, 133-138 (1992).
  • 30) Scorer, C. A., Clare, J. J., McCombie, W. R., Romanos, M. A., and Sreekrishna, K., Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression. Bio/technology, 12, 181-184 (1994).
  • 31) Iwashita, K., Nagahara, T., Kimura, H., Takano, M., Shimoi, H., and Ito, K., The bglA gene of Aspergilllus kawachii encodes both extracellular and cell wall-bound β-glucosidases. Appl. Environ. Microbiol., 65, 5546-5553 (1999).
  • 32) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
  • 33) Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
  • 27) Yoshida, M., Ohira, T., Igarashi, K., Nagasawa, H., Aida, K., Hallberg, B. M., Divne, C., Nishino, T., and Samejima, M., Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris. Biosci. Biotechnol. Biochem., 65, 2050-2057 (2001).

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.