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Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing

Wang, X., Appels, R., Zhang, X., Békés, F., Diepeveen, D.ORCID: 0000-0002-1535-8019, Ma, W.ORCID: 0000-0002-1264-866X, Hu, X. and Islam, S. (2020) Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing. Food Chemistry, 312 . Article 126038.

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To understand wheat dough protein behavior under dual mixing and thermal treatment, solubility of Mixolab-dough proteins were investigated using nine extraction buffers of different dissociation capacities. Size exclusion high performance liquid chromatography (SE-HPLC) and two-dimensional gel electrophoresis (2-DGE) demonstrated that overall changes of protein fractions and dynamic responses of specific proteins during dough processing were well reflected by their solubility variations. After starch pasting, the abundance of 0.5 M NaCl extractable proteins were decreased except for six protein groups including α-amylase inhibitors and superoxide dismutase (SOD). The solubility loss of glutenin proteins at C3 (32 min; 80 ℃) was mainly ascribed to the un-extractable HMW-GSs, LMW-GSs, globulin and triticin, while the extract yield of α-, β-, γ-gliadins and avenin-like proteins (ALPs) increased after starch pasting. Differential responses of dough proteins to extraction systems provides the basis for further exploring wheat protein dynamics in processing.

Item Type: Journal Article
Murdoch Affiliation: College of Science, Health, Engineering and Education
Publisher: Elsevier Limited
Copyright: © 2019 Elsevier Ltd.
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