Multiple forms of β-glucosidase (EC of were produced when the fungus was grown in a cellulose medium. One β-glucosidase was purified 16fold from 6dold culture filtrates by ionexchange and gelfiltration chromatography. The purified enzyme was free of cellulase activity. It hydrolysed aryl β-Dglucosides and β-Dlinked diglucosides. It was optimally active at pH 5.4, at 65 °C. The apparent values for nitrophenyl β-Dglucoside (PNPG) and cellobiose were 0.29 and 0.83 mM, respectively. Glucose, fucose, nojirimycin and gluconolactone inhibited β-glucosidase competitively. At high (> 1 mM) substrate concentration, β-glucosidase catalysed a parallel transglycosylation reaction. The transglycosylation product formed from cellobiose appeared to be a β-linked tetramer of glucose. Admixtures of β-glucosidase and cellulase components showed that the concept of cellobiose inhibition of cellulases was not valid for all components of the cellulase system of β-Glucosidase supplementation also stimulated cellulose hydrolysis by cellulases when there was no accumulation of cellobiose in reaction mixture.


Article metrics loading...

Loading full text...

Full text loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error