Abstract
A minor component isolated from the extra-cellular cellulase of the anaerobic rumen fungus Neocallimastix frontalis by adsorption on cellulose had a remarkable capacity to degrade crystalline hydrogen-bond-ordered cellulose. When produced in a semi-defined medium the component comprised normally less than 4% of the total protein and only 0.3% of the protein in cultures containing rumen fluid. The minor component showed endoglucanase (carboxymethylcellulase) and β-glucosidase activity and effected the extensive hydrolysis of “crystalline” cellulose in the form of the cotton fibre when acting alone. Glucose was the sole product of hydrolysis. The specific activity of the crystalline cellulose solubilizing factor (CCSF) in degrading cotton fibre was much higher than any other cellulase or cellulase component reported so far. The activity of the CSSF to crystalline hydrogen-bond-ordered cellulose resides in a high molecular mass complex of 670 kDa, that comprised a number of subunits ranging in size from 68 to 135 kDa.
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