Abstract
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 d-glucose (KM=3.1mM) and lower affinity to other monosaccharides. GO from Aspergillusniger (GO-An) had a KM value of 225mM towards glucose, which points to a significant difference in glucose affinity between the two enzymes. Furthermore, P2O-Tm had higher affinity towards O2 (KM=0.46mM) than GO-An (KM=2.9mM). 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.
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