Similar to glucose oxidase (GO), pyranose oxidase (P2O) may well have desired functionalities in some food applications in general, particularly breadmaking. As its name implies, P2O oxidises a variety of monosaccharides. P2O purified from a culture of Trametes multicolor (P2O-Tm) had high affinity towards is-glucose (K-M = 3.1 mM) and lower affinity to other monosaccharides. GO from Aspergillus niger (GO-An) had a K-M value of 225 mM towards glucose, which points to a significant difference in glucose affinity between the two enzymes. Furthermore, P2O-Tm had higher affinity towards O-2 (K-M = 0.46 mM) than GO-An (K-M = 2.9 mM). Dehydroascorbic acid did not accept electrons in the reactions catalysed by P2O-Tm and GO-An. For the same activity towards glucose in saturating conditions, the rate of ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract were higher with P2O-Tm, than with GO-An. The demonstrated differences in properties and functional features between P2O-Tm and GO-An allow prediction of differences in functional behaviour of the enzymes, in food applications. (C) 2011 Elsevier Ltd. All rights reserved.