Abstract
A cellobiohydrolase component was isolated from an anaerobic thermophilic cellulolytic bacterium, Clostridium stercorarium. When acting alone, the enzyme showed minimal activity towards ordered substrates such as cellulose and filter paper but it has been shown to attack phosphoric-acid swollen cellulose giving cellobiose as principal product. When recombined with endoglucanase it did allow an extensive hydrolysis demonstrating a marked synergism in the action of those two components; the addition of β-glucosidase resulted in a further increase in activity.
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