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

    Access Status
    Fulltext not available
    Authors
    Wang, X.
    Appels, R.
    Zhang, X.
    Bekes, F.
    Torok, K.
    Tomoskozi, S.
    Diepeveen, Dean
    Ma, W.
    Islam, S.
    Date
    2017
    Type
    Journal Article
    
    Metadata
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    Citation
    Wang, X. and Appels, R. and Zhang, X. and Bekes, F. and Torok, K. and Tomoskozi, S. and Diepeveen, D. et al. 2017. Protein-transitions in and out of the dough matrix in wheat flour mixing. Food Chemistry. 217: pp. 542-551.
    Source Title
    Food Chemistry
    DOI
    10.1016/j.foodchem.2016.08.060
    ISSN
    0308-8146
    School
    Department of Mathematics and Statistics
    URI
    http://hdl.handle.net/20.500.11937/57895
    Collection
    • Curtin Research Publications
    Abstract

    © 2016 Elsevier Ltd 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.

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