Abstract
The endo-.beta.-1,4-glucanase (carboxymethylcellulase) activity in cell extracts prepared from B. succinogenes S85 was almost unaffected by prolonged incubation at 39.degree. C in the presence of merthiolate, a SH inhibitor. The .beta.-1,4-glucosidase (cellobiase) activity was rapidly inactivated by the same treatment. The cellobiase also was inactivated by exposure to air but was stabilized by dithiothreitol in a N2 atmosphere. The cellobiase apparently required reduced SH groups for activity.

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