Purification and Properties of an exo-Cellulase Component of Novel Type from Trichoderma viride

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Abstract
An enzyme extract from Cellulase-Onozuka, a commercial product of Trichoderma viride, was fractionated by Amberlite CG-50 column chromatography into three cellulase [EC 3.2.1.4] groups, peaks I to III. A novel enzyme, which has both β-glucosidase [EC 3. 2. 1. 21] and exo-carboxymethyl-cellulase (exo-CMCase) properties, was obtained from peak III by extensive purification through consecutive column chromatography. The enzyme was homogeneous on ultracentrifugation, SDS-gel and cellulose acetate film electrophoreses and molecular sieve chromatography on Bio-Gel P-150. The molecular weight of this enzyme was estimated to be 53, 000. The enzyme appeared to release cellobiose residues one by one from the nonreducing end of higher cellooligosaccharides and CM-cellulose (CMC), but to release glucosyl residues from reduced cellotriose and β-cellobioside, resembling a β-glucosidase in this respect. Furthermore, this exo-CMCase also attacked xylan exo-wise to produce xylobiose molecules one by one, but it scarcely attacked insoluble cellulose, except for a cellodextrin apparently rich in amorphous structure.

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