-
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.
PMID: 710416 [PubMed - indexed for MEDLINE]
-
Cited by 18 PubMed Central articles
-
Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium.
Vanden Wymelenberg A, Sabat G, Mozuch M, Kersten PJ, Cullen D, Blanchette RA.
Appl Environ Microbiol. 2006 Jul; 72(7):4871-7.
[Appl Environ Microbiol. 2006]
-
Purification and Characterization of Cellobiose Dehydrogenases from the White Rot Fungus Trametes versicolor.
Roy BP, Dumonceaux T, Koukoulas AA, Archibald FS.
Appl Environ Microbiol. 1996 Dec; 62(12):4417-4427.
[Appl Environ Microbiol. 1996]
-
Purification and Characterization of a Cellulose-Binding (beta)-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium.
Lymar ES, Li B, Renganathan V.
Appl Environ Microbiol. 1995 Aug; 61(8):2976-2980.
[Appl Environ Microbiol. 1995]
- » See all...