麦谷蛋白通过两端的半胱氨酸之间形成二硫键而交联，并包埋麦胶蛋白形成面筋网络，是面团具有延展特性的分子基础。麦谷蛋白高分子量亚基1Dx5氮端（NTD）半胱氨酸的交联对面团流变特性影响最大。尽管如此，对1Dx5-NTD半胱氨酸间形成二硫键的交联模式、交联程度和交联速率研究尚不明确。蛋白质二硫键异构酶在内质网中介导麦谷蛋白的交联，并在面团处理中仍然发挥作用，然而尚缺乏对它和1Dx5-NTD互作机制的研究。系统性综合研究不同反应条件对1Dx5-NTD交联过程以及蛋白质二硫键异构酶介导下该过程的影响未见报道。本项目拟进一步明晰1Dx5-NTD的三个半胱氨酸在形成面筋网络中的内部结构因素，及催化机理、结构信息都已明确的蛋白质二硫键异构酶DsbC与1Dx5-NTD相互作用的分子机理和结构学基础，并系统性探索各种反应条件对交联过程的影响。将上述影响因素在面团加工中加以验证，全面理解面团流变特性的分子基础。

Glutenin crosslinks with each other via the cysteines on both of its terminals, and encapsulates gliadins within to form the gluten network. Thus it is the molecular basis that endows dough the extension characters. High molecular weight glutenin subunits 1Dx5 forms disulfide bonds via cysteines on its N-terminal domain and impact the rheological properties of the dough most. Even so, research on the crosslink pattern, extent and velocity of 1Dx5-NTD remains unclear. Protein disulfide isomerase mediates the crosslink of gluten in the endoplasmic reticulum, and keeps playing a role during dough treatment. However, the mechanism of interaction between protein disulfide isomerase and 1Dx5-NTD remains unknown. There is currently no report of a systematic study on the comprehensive impact of reaction conditions to the crosslink of 1Dx5-NTD and its protein disulfide isomerase mediated process. This research aims to further elucidate the internal roles of the three cysteines in the formation of gluten network, and the interaction mechanism and structural basis of 1Dx5-NTD with a protein disulfide isomerase DsbC with known catalytic mechanism and structural information. And systematically investigate the impact of different reaction conditions to this crosslink process. Eventually to apply these factors to the dough treatment process and comprehensively understand the molecular basis of dough rheological properties.