Cellulase complex from Chaetomium cellulolyticum: Isolation and propertiesof 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 component s 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 op timal pH values for catalytic activity are in the range 4.5-6.0, and the op timal temperatures are in the range 60-70 degrees C. Of these enzymes the 1 9 kD endoglucanase is the mast stable; it retained high activity within a b road pH range (from 5.0 to 9.6) at 50 degrees C for 3 h. This enzyme also h ad the highest topolytic activity determined by the efficiency of removal o f indigo from the surface of cotton.