Purification and properties of cellobiose: quinone oxidoreductase from Sporotrichum pulverulentum

Acta Chem Scand B. 1975;29(4):419-24.

Abstract

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.

MeSH terms

  • Alcohol Oxidoreductases / analysis
  • Alcohol Oxidoreductases / isolation & purification*
  • Alcohol Oxidoreductases / metabolism
  • Chromatography
  • Concanavalin A / metabolism
  • Disaccharides
  • Quinones
  • Sporothrix / enzymology*

Substances

  • Disaccharides
  • Quinones
  • Concanavalin A
  • Alcohol Oxidoreductases