A highly active thermostable beta-glucosidase was purified to homogeneity from a strain of Trichoderma sp. The enzyme was an extracellular glycoprotein and showed hydrolytic activity toward several beta-glucosides. Cellobiose was found to be the substrate of choice for this enzyme. This finding could suggest future technological applications of the purified protein.

A highly active fungal β-glucosidase - Purification and properties

CURRELI, NICOLETTA;RESCIGNO, ANTONIO;SANJUST, ENRICO
1994

Abstract

A highly active thermostable beta-glucosidase was purified to homogeneity from a strain of Trichoderma sp. The enzyme was an extracellular glycoprotein and showed hydrolytic activity toward several beta-glucosides. Cellobiose was found to be the substrate of choice for this enzyme. This finding could suggest future technological applications of the purified protein.
BETA-GLUCOSIDASE; PURIFICATION; BETA-GLUCOSIDES
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/32968
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