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.
File in questo prodotto:
| File | Dimensione | Formato | |
|---|---|---|---|
|
Appl Biochem Biotechnol (1994) Vol 44 pp 263-270.pdf
Solo gestori archivio
Descrizione: File PDF da scansione
Tipologia:
versione editoriale (VoR)
Dimensione
3.02 MB
Formato
Adobe PDF
|
3.02 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
