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小麦球蛋白与面筋在碱或盐条件下的相互作用及其对面团流变学和最终品质的影响。

Interactions between wheat globulin and gluten under alkali or salt condition and its effects on noodle dough rheology and end quality.

作者信息

Zhang Li-Li, Li Meng-Meng, Guan Er-Qi, Yang Yu-Ling, Zhang Ting-Jing, Liu Yuan-Xiao, Bian Ke

机构信息

College of Food Science and Engineering, Henan University of Technology, Zhengzhou, Henan 450001, China.

College of Food Science and Engineering, Henan University of Technology, Zhengzhou, Henan 450001, China.

出版信息

Food Chem. 2022 Jul 15;382:132310. doi: 10.1016/j.foodchem.2022.132310. Epub 2022 Feb 2.

Abstract

The influences of wheat globulin on dough and noodle quality under alkali or salt conditionwere investigated, and the protein interactions were revealed. Results indicated that dough viscoelasticity, noodle hardness, springiness and extensibility of samples with globulin added were remarkably increased under alkali condition. However, the corresponding enhancement was less significant under salt condition. In dough system, added globulin decreased the protein surface hydrophobicity by 38.71%, implying the enhancement of hydrophobic interactions. Under salt and alkali conditions, added globulin further increased the β-sheets structure by 1.68% and 3.17%, respectively, indicating the enhancement of hydrogen bonds interaction. In addition, disulfide bonds interactions between globulin and gluten have also been demonstrated induced by alkali. The results were accountable for protein network polymerization observed in micro-structures. This paper provides new insights into the structural properties of wheat globulin, and demonstrates the excellent potential to improve noodle processing quality under alkali condition significantly.

摘要

研究了碱或盐条件下小麦球蛋白对面团和面条品质的影响,并揭示了蛋白质间的相互作用。结果表明,在碱性条件下添加球蛋白的样品面团粘弹性、面条硬度、弹性和延展性显著提高。然而,在盐条件下相应的增强作用不太显著。在面团体系中,添加球蛋白使蛋白质表面疏水性降低了38.71%,这意味着疏水相互作用增强。在盐和碱条件下,添加的球蛋白分别使β-折叠结构进一步增加了1.68%和3.17%,表明氢键相互作用增强。此外,还证明了碱诱导球蛋白与面筋之间的二硫键相互作用。这些结果解释了微观结构中观察到的蛋白质网络聚合现象。本文为小麦球蛋白的结构特性提供了新的见解,并证明了其在显著改善碱性条件下面条加工品质方面的巨大潜力。

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