The unique properties of wheat reside primarily in its gluten-forming storage proteins. Their intrinsic viscoelastic behavior is responsible for the characteristics of different wheat-based foods and for the use of wheat gluten proteins in different food products. Wheat-based food processing generally develops and sets the gluten protein network. Heat-induced gluten aggregation proceeds through cross-linking within and between its protein fractions. Prominent reactions include sulfhydryl (SH) oxidation and SH-disulfide (SS) interchange, which lead to SS cross-links. Other covalent bonds are also formed. Gluten functionality can be (bio-) chemically impacted. We focus on bread making, in which gluten proteins contribute to dough properties, bread loaf volume, and structure, and on pasta production, in which gluten proteins generate the desired cooking quality. Furthermore, it is speculated that the structure and texture of soft wheat products are also, at least to some degree, shaped by the heat-induced changes in the gluten protein fraction.


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  • Article Type: Review Article
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