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;POMPEI, RAFFAELLO;RESCIGNO, ANTONIO;SANJUST, ENRICO
1994-01-01
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.
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Appl Biochem Biotechnol (1994) Vol 44 pp 263-270.pdf
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