Biotechnology Letters

, Volume 30, Issue 8, pp 1373–1378

Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola

Original Research Paper

DOI: 10.1007/s10529-008-9715-4

Cite this article as:
Yoon, JJ., Cha, CJ., Kim, YS. et al. Biotechnol Lett (2008) 30: 1373. doi:10.1007/s10529-008-9715-4


An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was ∼32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC. The partial amino acid sequences of the purified endoglucanase had high homology with endo-β-1,4-glucanase of glycosyl hydrolase family 5 from other fungi. The Km and Kcatvalues for CMC were 12 mg CMC/ml and 670/s, respectively. The purified EG hydrolyzed both cellotetraose (G4) and cellopentaose (G5), but did not degrade either cellobiose (G2) or cellotriose (G3).


Brown-rot fungus Cellulose Endoglucanase Fomitopsis pinicola Microcrystalline cellulose hydrolysis 

Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.Environment & Energy DivisionKorea Institute of Industrial Technology (KITECH)Cheonan, ChungnamKorea
  2. 2.Department of Biotechnology and BET Institute, College of Industrial ScienceChung-Ang UniversityAnseong, Gyeonggi-doKorea
  3. 3.Department of Forest Products, College of Forest ScienceKookmin UniversitySeongbuk, SeoulKorea
  4. 4.Division of Biotechnology, College of Life Sciences and BiotechnologyKorea UniversitySeongbuk, SeoulKorea

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