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Gewählte Publikation:

Decamps, K; Joye, IJ; Haltrich, D; Nicolas, J; Courtin, CM; Delcour, JA.
(2012): Biochemical characteristics of Trametes multicolor pyranose oxidase and Aspergillus niger glucose oxidase and implications for their functionality in wheat flour dough
FOOD CHEM. 2012; 131(4): 1485-1492. FullText FullText_BOKU

Similar to glucose oxidase (GO), pyranose oxidase (P(2)O) may well have desired functionalities in some food applications in general, particularly breadmaking. As its name implies, P(2)O oxidises a variety of monosaccharides. P(2)O purified from a culture of Trametes multicolor (P(2)O-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, P(2)O-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 P(2)O-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 P(2)O-Tm, than with GO-An. The demonstrated differences in properties and functional features between P(2)O-Tm and GO-An allow prediction of differences in functional behaviour of the enzymes, in food applications. (C) 2011 Elsevier Ltd. All rights reserved.
Autor*innen der BOKU Wien:
Haltrich Dietmar

Find related publications in this database (Keywords)
Pyranose oxidase
Glucose oxidase
Ferulic acid

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