Cellobiase from Termitomyces clypeatus: activity and secretion in presence of glycosylation inhibitors.

In presence of the glycosylation inhibitors, 2-deoxy-D-glucose (1 mg/ml), tunicamycin (30 microg/ml), 1-deoxynojirimycin (30 microg/ml) and D-glucono-delta-lactone (1 mg/ml), total cellobiase activity, in the extracellular, intracellular and cell bound fractions, of the fungus Termitomyces clypeatus grown in 20 ml cellobiose medium (1%, w/v) increased by 50-, 1.8-, 2.4-, 1.3-fold, respectively, with respect to control medium (16.3 U). The inhibitors also stimulated secretion of 95% of the total protein in culture medium, except D-glucono-delta-lactone which released 60% of the total protein. 2-Deoxy-D-glucose (1 mg/ml) led to production of extracellular cellobiase up to 40 U/ml, whereas in absence of the inhibitors only 0.59 U/ml enzyme was detected.