Details

Autor(en) / Beteiligte

• Wang, Xiaolong
• Appels, Rudi
• Zhang, Xiaoke
• Bekes, Ferenc
• Torok, Kitti
• Tomoskozi, Sandor
• Diepeveen, Dean
• Ma, Wujun
• Islam, Shahidul

Titel

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

Ist Teil von

• Food chemistry, 2017-02, Vol.217, p.542-551

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2017

Quelle

MEDLINE

Beschreibungen/Notizen

• •Mixolab proteomics expand our knowledge of the range of proteins in gluten matrix.•Dynamic exchanges of gliadins and globulins in the gluten matrix are identified.•Starch gelatinization stabilizes specific protein behavior in the gluten complex.•Varietal variation of protein behavior confers varied flour quality attributes.•The varied protein encoding genes are located to different chromosomes groups. 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 32min (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 32min (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.