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

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

X. Wang, R. Appels, X. Zhang, F. Békés, D. Diepeveen, W. Ma, X. Hu and S. Islam
Food Chemistry, Vol.312, Article 126038
2020
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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.

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Source: InCites

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
3 Agriculture, Environment & Ecology
3.85 Food Science & Technology
3.85.99 Cereal Starch Properties
Web Of Science research areas
Chemistry, Applied
Food Science & Technology
Nutrition & Dietetics
ESI research areas
Agricultural Sciences
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