Biochemical characteristics of Trametes multicolor pyranose oxidase and Aspergillus niger glucose oxidase and implications for their functionality in wheat flour dough

Pyranose Oxidase from Trametes multicolor Impacts Dough and Bread Microstructure

“…P 2 O of T. multicolor was produced recombinantly in Escherichia coli and purified as described in Decamps et al (2012b). P 2 O of T. multicolor was produced recombinantly in Escherichia coli and purified as described in Decamps et al (2012b).…”

“…Improving agents are typically added during breadmaking to overcome deficiencies and variability in wheat flour quality (Delcour and Hoseney 2010). 1.1.3.10) catalyzes oxidation of C 2 or C 3 of several mono-and disaccharides by O 2 to the corresponding dicarbonyl derivatives and H 2 O 2 (Leitner et al 2001;Decamps et al 2012b). 1.1.3.4), an oxidizing enzyme catalyzing the oxidation of C 1 of β-D-glucose in the presence of O 2 to yield H 2 O 2 and D-glucono-1,5-lactone (Bankar et al 2009).…”

“…Pyranose oxidase (P 2 O, E.C. 1.1.3.10) catalyzes oxidation of C 2 or C 3 of several mono-and disaccharides by O 2 to the corresponding dicarbonyl derivatives and H 2 O 2 (Leitner et al 2001;Decamps et al 2012b). Use of P 2 O in breadmaking is rare.…”

Electrochemical characterization of the pyranose 2-oxidase variant N593C shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity

“…1,2 A major drawback of using POx for glucose sensing, however, is its high affinity towards oxygen, as determined by Decamps. 3 POx has a K m value towards oxygen of 0.46 mM, whereas the affinity of GOx from Aspergillus niger ( An GOx) for oxygen is 6-fold lower as expressed by the higher Michaelis constant K m of 2.9 mM. Oxygen reduction at POx thus interferes with the overall sensitivity towards glucose for a POx-based biosensor operating at low potentials, excluding the approach of detecting the enzymatically produced H 2 O 2 by oxidation at potentials above +600 mV vs. Ag|AgCl.…”

“…In contrast to GOx, which is anomerically restricted to catalyze only the oxidation of β- d -glucose, 7 POx converts both α- and β- d -glucose. 3 The FAD cofactor is covalently bound to the polypeptide chain of POx, 6,8 whereas the FAD cofactor of GOx is only tightly entrapped within the apoenzyme, and GDH relies on a freely diffusing PQQ cofactor. 9 …”