Cellulase complex from Chaetomium cellulolyticum: isolation and properties of major components.
Four major components of the cellulase complex of Chaetomium cellulolyticum have been isolated by gel-filtration, ion-exchange chromatography on DEAE-Toyopearl and Macro Prep Q, and chromatofocusing on Mono P. These components include three endoglucanases (19, 35, and 40 kD) and a cellobiohydrolase (45 kD). The isoelectric points of the enzymes vary from 3.8 to 4.2. The optimal pH values for catalytic activity are in the range 4.5-6.0, and the optimal temperatures are in the range 60-70 degrees C. Of these enzymes the 19 kD endoglucanase is the most stable; it retained high activity within a broad pH range (from 5.0 to 9.6) at 50 degrees C for 3 h. This enzyme also had the highest topolytic activity determined by the efficiency of removal of indigo from the surface of cotton.
Ankudimova
N V
NV
Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia. ankudimova@enzyme.chem.msu.ru
Baraznenok
V A
VA
Becker
E G
EG
Okunev
O N
ON
D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D043366:Cellulose 1,4-beta-Cellobiosidase; D002597:Chaetomium / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013816:Thermodynamics
D009097:Multienzyme Complexes; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase