Immobilization of pyranose oxidase (Phanerochaete chrysosporium): characterization of the enzymic properties.
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.
Department of Pure and Applied Biochemistry, University of Lund, Sweden.
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Olsson
C F
CF
Mandenius
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Kubatova
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J
Volc
D000363:Agaricales / Q000201:enzymology*; D002237:Carbohydrate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel / Q000379:methods; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics
D004800:Enzymes, Immobilized; D002237:Carbohydrate Dehydrogenases; C022489:pyranose oxidase