Abstract
Wheat gluten protein (WGP) was modified by deamidation and succinylation to improve its functional properties. The properties of deamidated and succinylated WGP were compared with those of unmodified WGP, deamidated WGP and succinylated WGP. Structural analysis was carried out with FTIR. Surface visualization was carried out with SEM and the thermal stability was determined by DSC. The results showed that an acylation level of 73.64% produced the optimal properties for modified WGP. After modification, its functional properties were significantly improved. Modification did not significantly change the α-helical content, but there was a significant decrease in its β-turn content and significant increases in β-sheet and random coil content. According to SEM images, the modified WGP exhibited a smooth and evenly distributed sheet-like structure. The thermal stability of WGP was slightly decreased by modification. These results provide important information for the use of modified WGP in novel products. For example, adding deamidated and succinylated WGP to pound cake may reduce the amount of butter needed by up to 20%.
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