The Journal of Microbiology

, Volume 48, Issue 6, pp 808–813

Identification and functional analysis of a gene encoding β-glucosidase from the brown-rot basidiomycete Fomitopsis palustris


DOI: 10.1007/s12275-010-0482-2

Cite this article as:
Ji, HW. & Cha, CJ. J Microbiol. (2010) 48: 808. doi:10.1007/s12275-010-0482-2


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.


β-glucosidase F. palustris brown-rot fungus glycosyl hydrolase P. pastoris 

Copyright information

© The Microbiological Society of Korea and Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  1. 1.Microbial Biotechnology Lab, Department of Biotechnology (BK21-program)Chung-Ang UniversityAnseongRepublic of Korea

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