Forsberg C W, Groleau D
Can J Microbiol. 1982 Jan;28(1):144-8. doi: 10.1139/m82-017.
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.
从产琥珀酸拟杆菌S85制备的细胞提取物中的内切-β-1,4-葡聚糖酶（羧甲基纤维素酶）活性，在硫柳汞（一种巯基抑制剂）存在的情况下于39℃长时间孵育时几乎未受影响。然而，β-1,4-葡萄糖苷酶（纤维二糖酶）活性经相同处理后迅速失活。纤维二糖酶暴露于空气中也会失活，但在氮气氛围中可被二硫苏糖醇稳定。这些结果表明，纤维二糖酶的活性需要还原型巯基基团。
