A HIGHLY-ACTIVE FUNGAL BETA-GLUCOSIDASE - PURIFICATION AND PROPERTIES

Authors
FADDA MB CURRELI N POMPEI R RESCIGNO A RINALDI A SANJUST E
Citation
Mb. Fadda et al., A HIGHLY-ACTIVE FUNGAL BETA-GLUCOSIDASE - PURIFICATION AND PROPERTIES, Applied biochemistry and biotechnology, 44(3), 1994, pp. 263-270
Citations number
17
Categorie Soggetti
Biothechnology & Applied Migrobiology",Biology
Journal title
Applied biochemistry and biotechnology → ACNP
ISSN journal
02732289
Volume
44
Issue
3
Year of publication
1994
Pages
263 - 270
Database
ISI
SICI code
0273-2289(1994)44:3<263:AHFB-P>2.0.ZU;2-O
Abstract
A highly active thermostable beta-glucosidase was purified to homogene ity from a strain of Trichoderma sp. The enzyme was an extracellular g lycoprotein and showed hydrolytic activity toward several beta-glucosi des. Cellobiose was found to be the substrate of choice for this enzym e. This finding could suggest future technological applications of the purified protein.