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- Pioneering strategies for overcoming bacterial drug resistance (2026)
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- HOME > J. Microbiol > Volume 48(6); 2010 > Research Support, Non-U.S. Gov't
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Research Support, Non-U.S. Gov't
- Identification and Functional Analysis of a Gene Encoding β-Glucosidase from the Brown-Rot Basidiomycete Fomitopsis palustris
- Hwang-Woo Ji , Chang-Jun Cha
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Journal of Microbiology 2010;48(6):808-813.
DOI: https://doi.org/10.1007/s12275-010-0482-2
Published online: January 9, 2011
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Corresponding author:
Chang-Jun Cha , Tel: +82-31-670-4840,
Abstract
The brown-rot basidiomycete Fomitopsis palustris is known to degrade crystalline cellulose (Avicel) and produce three major cellulases, exoglucanases, endoglucanases, and β-glucosidases. A novel β-glucosidase designated as Cel3A was identified from F. palustris grown at the expense of Avicel. The deduced amino acid sequence of Cel3A showed high homology with those of other fungal β-glucosidases that belong to glycosyl hydrolase (GH) family 3. The sequence analysis also indicated that Cel3A contains the N- and C-terminal domains of GH family 3 and Asp-209 was conserved as a catalytic nucleophile. The cloned gene was successfully expressed in the yeast Pichia pastoris and the recombinant protein exhibited β-glucosidase activity with cellobiose and some degree of thermostability. Considering the size and sequence of the protein, the β-glucosidase identified in this study is different from the protein purified directly from F. palustris in the previous study. Our results suggest that the fungus possesses at least two β-glucosidase genes.
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