Stability of the endo-beta-1,4-glucanase and beta-1,4-glucosidase from Bacteroides succinogenes.

The endo-beta-1,4-glucanase (carboxymethylcellulase) activity in cell extracts prepared from Bacteroides succinogenes S85 was almost unaffected by prolonged incubation at 39 degrees C in the presence of merthiolate, a sulfhydryl inhibitor. The beta-1,4-glucosidase (cellobiase) activity, however, was rapidly inactivated by the same treatment. The cellobiase was also inactivated by exposure to air, but was stabilized by dithiothreitol in a nitrogen atmosphere. These results suggest that the cellobiase required reduced sulfhydryl groups for activity.