4.7 Article

The Bread Dough Stability Improving Effect of Pyranose Oxidase from Trametes multicolor and Glucose Oxidase from Aspergillus niger: Unraveling the Molecular Mechanism

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 61, Issue 32, Pages 7848-7854

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf4021416

Keywords

oxidizing enzymes; gluten proteins; arabinoxylan; glutathione; ferulic acid; tyrosine

Funding

  1. Fonds voor Wetenschappelijk Onderzoek - Vlaanderen (FWO, Brussels, Belgium)
  2. European Commission [FP7-People-2011-10E-300408]

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Glucose oxidase (GO) and pyranose oxidase (P2O) improve dough stability and bread quality. We here studied whether their mode of action resides in cross-linking of proteins and/or arabinoxylan (AX) molecules through the production of H2O2. Evidence for both was deduced from a decrease in extractability of protein and AX from dough made with P2O, GO, or H2O2, using sodium dodecyl sulfate containing buffer and water, respectively. The addition of H2O2, P2O, or GO to a glutathione solution sharply decreased its sulfhydryl (SH) content. P2O or GO can trigger protein cross-linking through the formation of disulfide (SS) bonds. As a result thereof, SH/SS interchange reactions between low molecular mass SH containing compounds and gluten proteins can be hampered. Furthermore, a decrease in the level of monomeric ferulic add (FA) esterified to AX in dough points to a role of FA bridges in cross-linking of AX molecules. Our results indicate that the molecular mechanism of dough and bread improvement by P2O and GO resides in cross-linking of gluten proteins and AX by formation of H2O2. They furthermore show that the extent of cross-linking upon addition of P2O or GO strongly depends on the concentration (and production rate) of H2O2.

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