Purification and properties of cellobiose: quinone oxidoreductase from Sporotrichum pulverulentum.
Cellobiose: quinone oxidoreductase was purified by ammonium sulfate precipitation, SP-Sephadex C-50 chromatography, and hydroxylapatite column chromatography. The purified enzyme is homogeneous by ultracentrifugal and SDS-gel electrophoretic analyses. The enzyme is a flavoprotein with FAD as the prosthetic group and produces cellobiono-delta-lactone as the product of cellobiose oxidation. Cellopentaose is also oxidized but no oxidation of cellulose could be detected. The enzyme oxidizes lactose and 4-beta-glucosylmannose but not 4-beta-mannosylglucose which implicates the C-2-hydroxyl of the non-reducing end of the disaccharide as important for substrate specificity.
D000429:Alcohol Oxidoreductases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D002845:Chromatography; D003208:Concanavalin A / Q000378:metabolism; D004187:Disaccharides; D011809:Quinones; D013175:Sporothrix / Q000201:enzymology*
D004187:Disaccharides; D011809:Quinones; D003208:Concanavalin A; D000429:Alcohol Oxidoreductases