• 1
    A cellulolytic enzyme (“C1” enzyme) has been isolated from a commercial cellulase preparation derived from culture filtrates of the fungus Trichoderma viride.
  • 2
    The purification method is a four-step procedure including chromatography on Bio-Gel P-10, DEAE-Sephadex chromatography, isoelectric focusing and chromatography on Bio-Gel P-60.
  • 3
    A yield of 144 mg enzyme was obtained per 100 g commercial cellulase.
  • 4
    The isolated enzyme was homogeneous in polyacrylamide gel electrophoresis at pH 5.0 and at pH 8.0 by isoelectric focusing in a polyacrylamide gel and also in the ultracentrifuge.
  • 5
    No enzyme activity towards carboxymethylcellulose could be detected in the purified material under the assay conditions used. Similarly, there was no β-glucosidase activity.
  • 6
    The purified enzyme was associated with 3.3% carbohydrate and is assumed to be a glycoprotein. The enzyme was isoelectric at pH 3.79 (10°C). A molecular weight of 46000 was determined by chromatography of the reduced and alkylated enzyme on a calibrated column of Sepharose 6B in 6 M guanidine-HCl.
  • 7
    Crystalline cellulose (Avicel), phosphoric acid-swollen Avicel and cellotetraose were degraded by the enzyme and in each case the principle reaction product was cellobiose.
  • 8
    Evidence indicates that the purified enzyme is a β-1,4-glucan cellobiohydrolase.