Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola
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- Yoon, JJ., Cha, CJ., Kim, YS. et al. Biotechnol Lett (2008) 30: 1373. doi:10.1007/s10529-008-9715-4
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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).