Immobilization of pyranose oxidase (Phanerochaete chrysosporium): characterization of the enzymic properties

Enzyme Microb Technol. 1991 Sep;13(9):755-9. doi: 10.1016/0141-0229(91)90055-f.

Abstract

Immobilization of pyranose oxidase (E.C.1.1.3.10) from Phanerochaete chrysosporium is described. The enzyme was bound to a glass-beaded support according to the glutardialdehyde, diazo, and carbodiimide methods with activity yields of 10%-23.3%. Characterization of the enzyme immobilized with the glutardialdehyde showed enhanced operational, storage, and temperature stability. The temperature optimum remained unchanged, but the pH optimum was slightly altered. Kinetic properties and the relative substrate specificities for glucose and xylose showed certain differences.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / enzymology*
  • Carbohydrate Dehydrogenases / isolation & purification
  • Carbohydrate Dehydrogenases / metabolism*
  • Chromatography, Gel / methods
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism*
  • Kinetics

Substances

  • Enzymes, Immobilized
  • Carbohydrate Dehydrogenases
  • pyranose oxidase