Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing.
Solubility variation of wheat dough proteins: A practical way to track protein behaviors in dough processing.
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DOI:
10.1016/j.foodchem.2019.126038
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发表时间:
2019-12
期刊:
影响因子:
8.8
通讯作者:
Xiaolong Wang;R. Appels;Xiaoke Zhang;F. Békés;D. Diepeveen;Wujun Ma;Xinzhong Hu;S. Islam
中科院分区:
文献类型:
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作者:
Xiaolong Wang;R. Appels;Xiaoke Zhang;F. Békés;D. Diepeveen;Wujun Ma;Xinzhong Hu;S. Islam
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.