Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum.
An extracellular enzyme which utilizes molecular oxygen to oxidize cellodextrins to the corresponding aldonic acids has been isolated from culture filtrates of the white-rot fungus Sporotrichum pulverulentum. This enzyme, tentatively named cellobiose oxidase, has been highly purified by classical techniques and has been demonstrated to be a glycoprotein with a molecular weight of approximately 93000. Ultraviolet spectra of the enzyme in the presence and absence of substrate are characteristic of a hemoprotein. Acidic hydrolyses of the enzyme followed by a spectrofluorimetric investigation of the hydrolysate has demonstrated the presence of approximately one flavin component per enzyme molecule. The possible role of this complex enzyme in cellulose degradation is discussed.
D002237:Carbohydrate Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D002475:Cellobiose; D006420:Hemeproteins / Q000302:isolation & purification* / Q000378:metabolism; D006861:Hydrogen Peroxide; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D010101:Oxygen Consumption; D013053:Spectrophotometry; D013175:Sporothrix / Q000201:enzymology*; D013379:Substrate Specificity
D006420:Hemeproteins; D002475:Cellobiose; D006861:Hydrogen Peroxide; D002237:Carbohydrate Dehydrogenases; C019858:cellobiose oxidase