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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Abstract
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 |
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Murdoch Affiliation: | College of Science, Health, Engineering and Education |
Publisher: | Elsevier Limited |
Copyright: | © 2019 Elsevier Ltd. |
URI: | http://researchrepository.murdoch.edu.au/id/eprint/53971 |
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