Functional analyses of the digestive β-glucosidase of Formosan subterranean termites (Coptotermes formosanus)

The research was to elucidate the function of the β-glucosidase of Formosan subterranean termites in vitro and in vivo. The gene transcript was detected predominantly in the salivary gland tissue, relative to the midgut and the hindgut of the foraging worker caste, indicating salivary glands were the major expression sites of the β-glucosidase. Using recombinant β-glucosidase produced in Escherichia coli, the enzyme showed higher affinity and activity toward cellobiose and cellotriose than other substrates tested. In assessing impacts of specific inhibitors, we found that the β-glucosidase could be irreversibly inactivated by conduritol B epoxide (CBE) but not gluconolactone. Termite feeding assays showed that the CBE treatment reduced the glucose supply in the midgut and resulted in the body weight loss while no effect was observed for the gluconolactone treatment. These findings highlighted that the β-glucosidase is one of the critical cellulases responsible for cellulose degradation and glucose production; inactivation of these digestive enzymes by specific inhibitors may starve the termite.

Highlights► Relative expression levels of a β-glucosidase gene were examined among different digestive tissues of Coptotermes formosanus. ► The recombinant β-glucosidase had better affinity and activity toward cellobiose and cellotriose than other substrates tested. ► Conduritol B epoxide (CBE) strongly inhibited the activity of β-glucosidase. ► Feeding termites with CBE reduced the glucose concentration in the midgut and resulted in body weight loss.