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Protein-transitions in and out of the dough matrix in wheat flour mixing

Wang, X., Appels, R., Zhang, X., Bekes, F., Torok, K., Tömösközi, S., Diepeveen, D., Ma, W. and Islam, S. (2017) Protein-transitions in and out of the dough matrix in wheat flour mixing. Food Chemistry, 217 . pp. 542-551.

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Sequential protein behavior in the wheat dough matrix under continuous mixing and heating treatment has been studied using Mixolab-dough samples from two Australian wheat cultivars, Westonia and Wyalkatchem. Size exclusion high performance liquid chromatography (SE-HPLC) and two-dimensional gel electrophoresis (2-DGE) analysis indicated that 32 min (80 °C) was a critical time point in forming large protein complexes and loosing extractability of several protein groups like y-type high molecular weight glutenin subunits (HMW-GSs), gamma-gliadins, beta-amylases, serpins, and metabolic proteins with higher mass. Up to 32 min (80 °C) Westonia showed higher protein extractability compared to Wyalkatchem although it was in the opposite direction thereafter. Twenty differentially expressed proteins could be assigned to chromosomes 1D, 3A, 4A, 4B, 4D, 6A, 6B, 7A and 7B. The results expanded the range of proteins associated with changes in the gluten-complex during processing and provided targets for selecting new genetic variants associated with altered quality attributes of the flour.

Publication Type: Journal Article
Murdoch Affiliation: School of Veterinary and Life Sciences
Publisher: Elsevier Limited
Copyright: © 2016 Elsevier Ltd.
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