Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4516589 | Journal of Cereal Science | 2009 | 10 Pages |
During breadmaking, wheat gluten proteins form a continuous network which is stabilized by disulfide bonds and modified by thiol/disulfide interchange reactions. This gluten network results in visco-elastic dough that holds together the other dough components and assists in retaining carbon dioxide. Wheat flour contains several components, enzyme co-factors and enzymes which can affect the formation and properties of the gluten network and, hence, the dough and bread characteristics. We present a brief overview of our current knowledge of the fate of gluten proteins during breadmaking, and how they are affected by endogenous wheat components (e.g. glutathione, cysteine and NAD(P)(H)) and enzyme systems (e.g. tyrosinase, peroxidase, the NADP-dependent thioredoxin and glutathione enzyme systems, protein disulfide isomerase, lipoxygenase, catalase and dehydrogenases).