Lee N E, Lima M, Woodward J
Chemical Technology Division, Oak Ridge National Laboratory, TN 37831-6194.
Biochim Biophys Acta. 1988 Dec 15;967(3):437-40. doi: 10.1016/0304-4165(88)90107-9.
Two endoglucanase-containing fractions were separated from Aspergillus niger cellulase by gel filtration and fast protein liquid chromatofocusing (FPLC). They possessed no ability to bind to or hydrolyze insoluble microcrystalline cellulose (Avicel) but were active toward soluble carboxymethylcellulose. No synergism was observed between Trichoderma reesei cellobiohydrolase I and either endoglucanase from A. niger. These findings may indicate that the role of the endoglucanase component of cellulase in insoluble microcrystalline cellulose hydrolysis is dependent upon its ability to be adsorbed upon the substrate.
通过凝胶过滤和快速蛋白质液相色谱聚焦法(FPLC)从黑曲霉纤维素酶中分离出两个含内切葡聚糖酶的组分。它们没有结合或水解不溶性微晶纤维素(微晶纤维素)的能力,但对可溶性羧甲基纤维素具有活性。在里氏木霉纤维二糖水解酶I与来自黑曲霉的任何一种内切葡聚糖酶之间均未观察到协同作用。这些发现可能表明纤维素酶的内切葡聚糖酶组分在不溶性微晶纤维素水解中的作用取决于其吸附在底物上的能力。