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
Xiaolong Wang;R. Appels;Xiaoke Zhang;F. Békés;D. Diepeveen;Wujun Ma;Xinzhong Hu;S. Islam
中科院分区:
农林科学1区
文献类型:
--
作者:
Xiaolong Wang;R. Appels;Xiaoke Zhang;F. Békés;D. Diepeveen;Wujun Ma;Xinzhong Hu;S. Islam

文献摘要

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为了了解小麦面团蛋白在双重混合和热处理条件下的行为,采用9种不同解离能力的萃取缓冲液研究了mixolab -面团蛋白的溶解度。粒径排除高效液相色谱(SE-HPLC)和二维凝胶电泳(2-DGE)结果表明,面皮加工过程中蛋白质组分的整体变化和特定蛋白质的动态响应可以通过其溶解度变化得到很好的反映。淀粉糊后,除α-淀粉酶抑制剂和超氧化物歧化酶(SOD) 6组蛋白外,0.5 M NaCl可提取蛋白的丰度均降低。淀粉糊化后,谷蛋白在C3 (32 min; 80℃)的溶解度损失主要是由于hw - gss、lw - gss、球蛋白和小麦蛋白无法提取,而α-、β-、γ-麦胶蛋白和avenin-like protein (ALPs)的提取率增加。面团蛋白对提取系统的差异响应为进一步研究小麦加工过程中的蛋白质动力学提供了基础。
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.