Abstract
AbstractThe disrupted gluten structure of infested wheat flours leads to low‐quality doughs unusable in bread‐making processes. Enzymes are replacing chemical treatments in the food industry as a tool to treat weak flours. Glucose oxidase is one of the most promising oxidative enzymes, although its efficiency compared with the alcohol‐soluble fraction of gluten proteins has not yet been demonstrated. If this enzyme could restore the broken covalent bonds between glutenin subunits, the gluten network of damaged wheat flour would recover its native structure and functionality. This treatment would allow bakers to use damaged flour, reducing the economic losses caused by this plague around Europe and North Africa. Electrophoretic studies demonstrated the formation of high‐molecular‐weight aggregates in the glutenin fraction, which had a characteristic thermal stability depending on enzyme dosage. Those molecular studies agreed with the bread‐making assays made with maximum enzyme dosage and microstructure determination. Overall results showed that glucose oxidase is a real alternative to traditionally used chemical oxidants. It acted specifically on the high‐molecular‐weight glutenin subunits of damaged wheat, forming dityrosine crosslinks between the wheat proteins, which reinforced the gluten network and gave away the dough functionality. Copyright © 2007 Society of Chemical Industry
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