Abstract
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 K m and K cat values 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).
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Acknowledgements
This study was carried out with the support of Forest Science & Technology Projects (Project No. S210707L010110) provided by the Korea Forest Service. The authors would like to thank Miss N.-M. Kim for her support and technical help.
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Yoon, JJ., Cha, CJ., Kim, YS. et al. Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola . Biotechnol Lett 30, 1373–1378 (2008). https://doi.org/10.1007/s10529-008-9715-4
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DOI: https://doi.org/10.1007/s10529-008-9715-4