Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola.
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).
Yoon
Jeong-Jun
JJ
Environment & Energy Division, Korea Institute of Industrial Technology, Cheonan, Chungnam 330-825, Korea. jjyoon@kitech.re.kr
Cha
Chang-Jun
CJ
Kim
Yeong-Suk
YS
Kim
Wook
W
D000595:Amino Acid Sequence; D002480:Cellulase / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism*; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008969:Molecular Sequence Data; D020072:Polyporales / Q000201:enzymology*; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity
D002482:Cellulose; D002480:Cellulase