Investigations on the extractability of gluten proteins from wheat bread in comparison with flour
- Cite this article as:
- Wieser, H. Z Lebensm Unters Forsch (1998) 207: 128. doi:10.1007/s002170050306
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Immunochemical methods are recommended for the quantitation of small amounts of gluten in food produced for those with coeliac disease. A major problem, however, is the reduced extractability of gliadin, the toxic factor of gluten, with aqueous alcohol, when foods have been heat-processed. A combined extraction/HPLC procedure was used to study the extractability of all gluten protein types from wheat flour and bread under both non-reducing and reducing conditions. Gliadin isolated from wheat flour was used as a reference protein for quantitation. The results indicate that the extractability of gliadin from bread with 60% ethanol under non-reducing conditions is strongly reduced. α- and γ-gliadins are much more affected than ω-gliadins, and less gliadin was extracted from the crust than from the crumb. For a complete extraction of gliadins from bread, reducing conditions and increased temperature are required. However, glutenin subunits are coextracted with the gliadins. This extract can be used for the quantitation of total gluten proteins by RP-HPLC. The recovery of gliadin added to flour before dough-mixing and bread-making is 98%.