Nummi M, Niku-Paavola M L, Lappalainen A, Enari T M, Raunio V
Biochem J. 1983 Dec 1;215(3):677-83. doi: 10.1042/bj2150677.
A 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91) was purified from the culture liquid of Trichoderma reesei by using biospecific sorption on amorphous cellulose and immunoaffinity chromatography. A single protein band in polyacrylamide-gel electrophoresis and one arc in immunoelectrophoresis corresponded to the enzyme activity. The Mr was 65 000. The pI was 4.2-3.6. The purified enzyme contained about 10% hexose. The enzyme differs from previously described cellobiohydrolases in being more effective in the hydrolysis of cellulose.
通过对无定形纤维素进行生物特异性吸附和免疫亲和层析,从里氏木霉的培养液中纯化出一种1,4-β-D-葡聚糖纤维二糖水解酶(EC 3.2.1.91)。聚丙烯酰胺凝胶电泳中的单一蛋白条带和免疫电泳中的一条弧与酶活性相对应。其相对分子质量为65000,等电点为4.2 - 3.6。纯化后的酶含有约10%的己糖。该酶与先前描述的纤维二糖水解酶不同,它在纤维素水解方面更有效。