title: Hydrolysis of cellulose by a mixture of Trichoderma reesei cellobiohydrolase and Aspergillus niger endoglucanase.
abstract: Two endoglucanase-containing fractions were separated from Aspergillus niger cellulase by gel filtration and fast protein liquid chromatofocusing (FPLC). They possessed no ability to bind to or hydrolyze insoluble microcrystalline cellulose (Avicel) but were active toward soluble carboxymethylcellulose. No synergism was observed between Trichoderma reesei cellobiohydrolase I and either endoglucanase from A. niger. These findings may indicate that the role of the endoglucanase component of cellulase in insoluble microcrystalline cellulose hydrolysis is dependent upon its ability to be adsorbed upon the substrate.
authors.affiliation: Chemical Technology Division, Oak Ridge National Laboratory, TN 37831-6194.
authors.forename: N E
authors.initials: NE
authors.lastname: Lee
authors.forename: M
authors.initials: M
authors.lastname: Lima
authors.forename: J
authors.initials: J
authors.lastname: Woodward
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology*; D002480:Cellulase / Q000302:isolation & purification / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism*; D043366:Cellulose 1,4-beta-Cellobiosidase; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006867:Hydrolases; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D014242:Trichoderma / Q000201:enzymology*
chemical_list: D002482:Cellulose; D006867:Hydrolases; D006026:Glycoside Hydrolases; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase