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转谷氨酰胺酶诱导的小麦面筋蛋白流变学特性及结构变化

Changes in rheological properties and structure of wheat gluten proteins induced by transglutaminase.

作者信息

Yu Yingtao, Wang Fengjiao, Yang Yufan, Zhang Jiapeng, Liu Hao, Liang Ying, Wang Jinshui

机构信息

College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China.

School of International Education, Henan University of Technology, Zhengzhou 450001, China.

出版信息

Int J Biol Macromol. 2025 Mar;295:139599. doi: 10.1016/j.ijbiomac.2025.139599. Epub 2025 Jan 7.

DOI:10.1016/j.ijbiomac.2025.139599
PMID:39788262
Abstract

To elucidate the effect of transglutaminase (TG) on the rheological properties of wheat gluten, this study investigates the underlying mechanisms by analyzing changes in gluten structure. The results demonstrated that the TG-treated gluten samples had higher storage modulus (G') and loss modulus (G″) compared to the control, conversely, creep and recovery strains followed an opposite trend. Notably, the most pronounced effects were observed with adding 2 U/g TG for 20-30 min. Size exclusion/reversed phase-high performance liquid chromatography profiles revealed that the treatment with TG elevated the levels of glutenin subunits, alongside reduced α- and γ-gliadins, promoting gluten aggregation. Moreover, the extractability of gluten gradually decreased due to TG-induced oxidation of sulfhydryl groups, which formed new disulfide bonds and cross-linked products. This structural modification reduced surface hydrophobic regions and promoted the aggregation of low molecular weight proteins into larger molecular weight aggregates. Microstructural analysis further confirmed that TG enhanced gluten network stability through covalent cross-linking. Overall, this study demonstrates that TG enhances the rheological characteristics of wheat gluten by facilitating the formation of a more robust network structure, driven by cross-linking reactions and disulfide bond formation.

摘要

为阐明转谷氨酰胺酶(TG)对小麦面筋流变学特性的影响,本研究通过分析面筋结构变化来探究其潜在机制。结果表明,与对照组相比,经TG处理的面筋样品具有更高的储能模量(G')和损耗模量(G''),相反,蠕变和回复应变则呈现相反趋势。值得注意的是,添加2 U/g TG处理20 - 30分钟时观察到最显著的效果。尺寸排阻/反相高效液相色谱图显示,TG处理提高了谷蛋白亚基的水平,同时降低了α-和γ-醇溶蛋白的水平,促进了面筋聚集。此外,由于TG诱导的巯基氧化,面筋的可提取性逐渐降低,形成了新的二硫键和交联产物。这种结构修饰减少了表面疏水区域,并促进了低分子量蛋白质聚集成更大分子量的聚集体。微观结构分析进一步证实,TG通过共价交联增强了面筋网络稳定性。总体而言,本研究表明,TG通过促进形成更坚固的网络结构来增强小麦面筋的流变学特性,这一过程由交联反应和二硫键形成驱动。

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