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Wheat protein disulfide isomerase improves bread properties via different mechanisms

•wPDI shows positive effect on dough alveographic and bread texture properties.•Less oxidation of sulfhydryl occurs in wPDI added dough and bread.•wPDI catalyzes oxidation of rheologically important disulfide bond formation.•wPDI catalyzes gluten network formation in a substrate specific manner. Glu...

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Bibliographic Details
Published in:Food chemistry 2020-06, Vol.315, p.126242-126242, Article 126242
Main Authors: Zhao, Chunfei, Luo, Ziyue, Li, Mingze, Gao, Jihui, Liang, Zhongxin, Sun, Siyuan, Wang, Xi, Yang, Dong
Format: Article
Language:English
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Summary:•wPDI shows positive effect on dough alveographic and bread texture properties.•Less oxidation of sulfhydryl occurs in wPDI added dough and bread.•wPDI catalyzes oxidation of rheologically important disulfide bond formation.•wPDI catalyzes gluten network formation in a substrate specific manner. Gluten network formation by the oxidation of glutenin sulfhydryl group majorly impacts the subsequent dough and bread properties, and an evolutionary list of chemical oxidants has been used as improvers in bread making. A systematic comparison between azodicarbonamide (ADA), Vc, wheat protein disulfide isomerase (wPDI) and disulfide bond formation protein C (DsbC) of their effects on the alveographic characters of dough and texture properties of subsequent bread was performed. Results show that wPDI improves dough alveographic characters and bread texture properties better in most aspects than other reagents. Free sulfhydryl analysis finds that addition of wPDI increased the free sulfhydryl content in both dough and bread. Compare with inorganic reagents and its bacterial homologue, improving the dough and bread properties with less oxidation of sulfhydryl lead to the proposal that wPDI acts by catalyzing the formation of rheologically active disulfide and reduction of inactive ones in a substrate specific manner.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2020.126242