ABSTRACTVital wheat gluten was modified by deamidation and succinylation. Deamidation caused a progressive degradation of gliadin with concomitant increase in low molecular weight components, but glutenin was not affected. Deamidation also markedly increased the net negative charge and surface hydrophobicity of gluten, while the bread loaf volume and dough extensibility were decreased. The most significant change in physiochemical properties of gluten caused by succinylation was an increase in net negative charge. Succinylation led to a pronounced decrease in dough extensibility but no significant changes in specific loaf volume. The data indicated the importance of hydrogen bonding offered by the amide groups of gluten in the breadmaking process. Changes in molecular weight distribution and hydrophobic interaction may also affect the baking performance of gluten. Ionic interaction may be involved in dough development but is less critical in controlling the overall baking performance of gluten.
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