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

Biotechnology Letters
Jeong-Jun YoonWook Kim

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 approximately 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-beta-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).

References

Mar 1, 1996·Analytical Chemistry·A ShevchenkoM Mann

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Citations

Jul 4, 2009·Applied Microbiology and Biotechnology·Marimuthu JeyaJung-Kul Lee
Jul 23, 2014·Journal of Basic Microbiology·Reetika SharmaHarinder Singh Oberoi
Apr 24, 2021·International Journal of Biological Macromolecules·Amisha Patel, Amita Shah
Jan 30, 2015·Chemical Reviews·Christina M PayneGregg T Beckham

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