College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China.
National Technique Innovation Center for Regional Wheat Production/Key Laboratory of Crop Physiology, Ecology and Management, Ministry of Agriculture/National Engineering and Technology Center for Information Agriculture, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China.
J Agric Food Chem. 2020 Apr 1;68(13):4005-4016. doi: 10.1021/acs.jafc.9b08122. Epub 2020 Feb 27.
Interactions between gluten proteins and water-extractable arabinoxylan (WEAX) during the heating stage are crucial for the organoleptic quality of high-fiber cereal products. To reveal the molecular mechanism of WEAX on gluten characteristic upon heating, the current study comparatively investigated the effects of WEAX with different molecular weights () on the heat-evoked conformational variation and polymerization behavior of gluten. Results showed that WEAX, especially low WEAX (L-WEAX), facilitated the polymerization ability of α-/γ-gliadins into glutenins, whereas high WEAX (H-WEAX) reduced the polymerizing temperature of glutenin and gliadin. L-WEAX could develop more hydrogen bonds with tyrosine of gluten and stabilize the secondary structure more evidently than H-WEAX upon heating. Compared with disulfide bridge formation, hydrophobic interactions were not the driving force involved in the heat-induced polymerization behavior affected by WEAX. WEAX evoked the reinforced glutenin network and heterogeneous distribution of gliadin, with a more uniform molecular surface developed for gluten.
在加热阶段，面筋蛋白与可提取阿拉伯木聚糖（WEAX）之间的相互作用对面筋类高纤维谷物产品的感官品质至关重要。为了揭示 WEAX 对面筋特性的加热影响的分子机制，本研究比较研究了不同分子量（）的 WEAX 对面筋热诱导构象变化和聚合行为的影响。结果表明，WEAX，特别是低分子量 WEAX（L-WEAX），促进了α-/γ-麦谷蛋白向醇溶蛋白的聚合能力，而高分子量 WEAX（H-WEAX）则降低了醇溶蛋白和麦谷蛋白的聚合温度。L-WEAX 比 H-WEAX 能在加热过程中与面筋中的酪氨酸形成更多的氢键，更明显地稳定二级结构。与二硫键形成相比，疏水相互作用不是 WEAX 影响的热诱导聚合行为的驱动力。WEAX 引发了强化的醇溶蛋白网络和麦谷蛋白的不均匀分布，形成了更均匀的面筋分子表面。
