Kanda T, Wakabayashi K, Nisizawa K
J Biochem. 1976 May;79(5):997-1005. doi: 10.1093/oxfordjournals.jbchem.a131167.
The substrate specificities of three endo-cellulase [EC 3.2.1.4] components, F-1, F-2, and S-1, obtained from the culture filtrate of Irpex lacteus (Polyporus tulipiferae), were investigated in detail. It was confirmed that the former is of a more random type, belonging to the carboxymethyl-cellulase (CMCcase) group, and the latter two are of a less random type, beloning to the Avicelase group. It was found that a mixture of CMCase and Avicelase shows a remarkable synergistic action in the degradation of cotton and Avicel and that CMCase lowers the degree of polymerization of both cotton and CM-cellulose faster than Avicelases, relative to the production of reducing sugar. Thus, it was assumed that cotton and similar cellulosic substrates were degraded mainly by the synergistic action of these cellulase components produced by this celluloytic fungus.
对从乳白耙齿菌(多孔菌科)培养滤液中获得的三种内切纤维素酶[EC 3.2.1.4]组分F-1、F-2和S-1的底物特异性进行了详细研究。证实前者是更随机类型的,属于羧甲基纤维素酶(CMC酶)组,而后两者是较不随机类型的,属于微晶纤维素酶组。发现CMC酶和微晶纤维素酶的混合物在棉花和微晶纤维素的降解中表现出显著的协同作用,并且相对于还原糖的产生,CMC酶比微晶纤维素酶更快地降低棉花和羧甲基纤维素的聚合度。因此,推测棉花和类似的纤维素底物主要通过这种纤维素分解真菌产生的这些纤维素酶组分的协同作用而被降解。