Macromolecular networks interactions in wheat flour dough matrices during sequential thermal-mechanical treatment
Macromolecular networks interactions in wheat flour dough matrices during sequential thermal-mechanical treatment
复制标题
连续热机械处理过程中小麦面粉面团基质中大分子网络的相互作用
作者：
Wang Xiaolong;Peng Pai;Appels Rudi;Tian Linpei;Zou Xiaoyang
在面团加工的Mixolab测量的差异进行了研究，作为基础，面粉从纯育种，同基因，小麦品系携带高分子量麦谷蛋白亚基5 + 10或2 + 12。在面团糊化前，5 + 10亚基主要依靠二硫键和氢键形成稳定的面筋网络，而2 + 12亚基容易形成以二硫键和疏水性为主的脆性蛋白质聚集体。在面团糊化过程中，5 + 10亚基的面团中形成了一个更广泛的富含不可提取的聚合蛋白、二硫键和β-折叠的蛋白质网络，从而形成了一个广泛而紧密的蛋白质-淀粉复合体，该复合体具有高热稳定性和低淀粉糊化的特点，而在2 + 12亚基的面团中通过二硫键、疏水性和氢键的组合控制具有片段化蛋白质聚集体的多孔蛋白质-淀粉凝胶，所述氢键促进反平行β-折叠的形成。
Differences in Mixolab measurements of dough processing were examined using, as a base, flour from pure breeding, isogenic, wheat lines carrying either the high molecular weight glutenin subunits 5 + 10 or 2 + 12. Before dough pasting, subunits 5 + 10 tend to form a stable gluten network relying mainly on disulfide bonds and hydrogen bonds, but 2 + 12 flour was prone to generating fragile protein aggregates dominated by disulfide bonds and hydrophobicity. During dough pasting, a broader protein network rich in un-extractable polymeric proteins, disulfide bonds and β-sheets was formed in the dough with subunits 5 + 10, thus resulting in an extensive and compact protein-starch complex which was characterized by high thermal stability and low starch.gelatinization, while in the dough of the 2 + 12 line, a porous protein-starch gel with fragmented protein aggregates was controlled by the combination of disulfide bonds, hydrophobicity and hydrogen bonds that facilitated the formation of antiparallel β-sheets.