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Cereal Chem 64:311-314   |  VIEW ARTICLE

Changes in the Gliadin Fraction(s) During Breadmaking: Isolation and Characterization by High-Performance Liquid Chromatography and Polyacrylamide Gel Electrophoresis.

M. Menkovska, G. L. Lookhart, and Y. Pomeranz. Copyright 1987 by the American Association of Cereal Chemists, Inc. 

Polyacrylamide gel electrophoresis (PAGE) and high-performance liquid chromatography (HPLC) were used to study the stability and interaction of gliadin proteins during mixing, fermentation, and baking. The proteins were stable during dough mixing or fermentation, as evidenced by absence of changes in gliadin patterns. However, gliadin degradations or interactions were found during baking. The PAGE gliadin bands with low relative mobility (RM less than 40) were more intensely stained and those with RM greater than 40 were less intensely stained from the extract of the crumb of bread baked from a composite hard red winter wheat flour when compared to the flour extract. The intensity (concentration) of all gliadin PAGE bands in the bread crust was significantly reduced. HPLC analysis of gliadin crumb extracts indicated that the highly hydrophobic gliadins (longest elution times greater than 23 min) were more heat labile (and probably interacted more with other flour components) than the less hydrophobic gliadins (shorter elution times less than 23 min). That interaction was confirmed by in vitro heat treatments of HPLC-isolated fractions (20-23 min and 23-26 min) and subsequent analysis by PAGE and HPLC.

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