A β-glucosidase was intensively purified with high recovery from a commercial preparation of Aspergillus niger by consecutive column chromatography. The enzyme was an acidic protein with a pI of 3.8, and split cellotriose to produce specifically β-D-glucose. Substrate specificity studies demonstrated that the purified enzyme required absolutely the C-4 configuration of the terminal, nonreducing β-D-glucose residues in the substrate molecules.
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Unno et al. (1993) studied this question.