Dynamic Changes in Glutenin Macropolymer during Different Dough Mixing and Resting Processes.
Dynamic Changes in Glutenin Macropolymer during Different Dough Mixing and Resting Processes.
复制标题
不同面团搅拌和静置过程中谷蛋白大分子聚合物的动态变化
DOI：
10.3390/molecules26030541
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发表时间：
2021-01-21
期刊：
影响因子：
--
通讯作者：
Chen H
中科院分区：
文献类型：
--
作者：
Feng Y;Zhang H;Wang J;Chen H
麦谷蛋白大聚合体（GMP）是小麦粉中麦谷蛋白的重要组成部分，对面团特性和面包制作品质起着重要作用。本研究探讨了GMP特性的变化过程中的面团加工的混合和休息阶段。结果表明，当搅拌时间从3 min增加到5 min时，GMP含量下降约20.20%，而增加静置时间可使部分GMP含量恢复。静止促进更大尺寸GMP颗粒的形成，这可能与在此过程中GMP中二硫键含量增加有关。相反，混合的机械力导致GMP解聚和形成较小的颗粒。此外，混合后，蛋白质二级结构趋于无序，蛋白质形态变得不规则，蛋白质亚基比例发生变化。因此，混合具有许多与静止相反的效果，尽管静止可以（在某种程度上）恢复混合后GMP的性质。然而，过长的静置时间会导致阴性结果，反映在较低的二硫键（SS）和GMP含量以及更不规则的颗粒尺寸。所呈现的结果表明，面团混合诱导面团的蛋白质结构的重排，和休息有点恢复化学键和内部蛋白质结构。
The glutenin macropolymer (GMP), which is an important component of the glutenin protein in wheat flour, plays a prominent role in governing dough properties and breadmaking quality. This study investigated the changes in GMP properties during the mixing and resting stages of dough processing. The results show that the GMP content decreases by about 20.20% when the mixing time increases from 3 to 5 min, while increasing the resting time can lead to restoration of some GMP contents. Resting promotes greater formation of large-sized GMP particles, which is likely related to the increased disulfide bond content in the GMP during this process. In contrast, the mechanical force of mixing causes GMP depolymerization and formation of smaller particles. Furthermore, after mixing, the protein secondary structure tends to be disordered, the protein morphology becomes irregular, and the protein subunit ratio changes. Thus, mixing has many of the opposite effects to resting, although resting can (to some extent) restore the properties of the GMP after mixing. However, excessive resting time can lead to negative results, reflected in lower disulfide bond (SS) and GMP contents, and more irregular particle sizes. The presented results suggest that dough mixing induces rearrangement of the dough’s protein structure, and resting somewhat restores the chemical bonds and internal protein structure.
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影响因子：
8.8
作者：
Bruneel, Charlotte;Lagrain, Bert;Delcour, Jan A.
通讯作者：
Delcour, Jan A.
影响因子：
2.4
作者：
Ong, Y. L.;Ross, A. S.;Engle, D. A.
通讯作者：
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影响因子：
3.8
作者：
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通讯作者：
Boom, RM
影响因子：
2.4
作者：
Sapirstein, HD;Suchy, J
通讯作者：
Suchy, J
DOI：
10.1098/rstb.2001.1024
发表时间：
2002-02-28
影响因子：
6.3
作者：
Shewry, PR;Halford, NG;Tatham, AS
通讯作者：
Tatham, AS