Henriksson G, Pettersson G, Johansson G, Ruiz A, Uzcategui E
Department of Biochemistry, University of Uppsala, Sweden.
Eur J Biochem. 1991 Feb 26;196(1):101-6. doi: 10.1111/j.1432-1033.1991.tb15791.x.
Cellobiose oxidase from the white rot fungus Phanerochaete chrysosporium has been purified to homogeneity by a new method. The enzyme has been cleaved by papain into two fragments: one containing the heme group and one containing the flavin group. The flavin fragment can oxidize cellobiose and is reoxidized by oxygen. Cellobiose oxidase binds to cellulose to approximately the same extent as cellobiohydrolase I. The cellulose-binding site is located on the flavin domain. The enzyme cannot be totally displaced from cellulose by cellobiose, and it is still active when adsorbed to cellulose. The possible role of the enzyme in lignocellulose degradation is discussed.
通过一种新方法，已将来自白腐真菌黄孢原毛平革菌的纤维二糖氧化酶纯化至同质。该酶已被木瓜蛋白酶切割成两个片段：一个含有血红素基团，另一个含有黄素基团。黄素片段可氧化纤维二糖，并被氧气再氧化。纤维二糖氧化酶与纤维素的结合程度与纤维二糖水解酶I大致相同。纤维素结合位点位于黄素结构域上。纤维二糖不能将该酶完全从纤维素上置换下来，并且当吸附到纤维素上时它仍然具有活性。文中讨论了该酶在木质纤维素降解中的可能作用。
