Abstract
Roles of SH and amide groups for heat-induced aggregation of wheat gluten were investigated.
The crude glutenin fraction was far more sensitive to heat than the crude gliadin portion of gluten.
The beat-induced aggregation of wheat gluten was not observed in the range of pH 2 to 4, but the gel formation was accelerated by the addition of reducing agents having SS bond cleaving ability. The hardness of gel increased with rising pH.
The thiol blocking reagents prevented the heat-induced gel formation of gluten. SH-modified gluten also could not form the gel.
The deamidation and succinylation prevented the heat-induced aggregation of wheat gluten.
These results may suggest that the heat-induced aggregation of wheat gluten is due to the formation of additional disulfide cross-links between chain molecules of the protein by SH-SS exchange reaction.
