不同筋力小麦面筋聚集特性及结构特性分析

通过分析面团质构特性、面筋蛋白聚集特性、面筋蛋白含量、分子量分布、二级结构以及微观结构，研究“郑麦103”、“郑麦136”、“新麦26”3 种不同筋力小麦面筋蛋白聚集特性及结构特性并探讨其差异。结果表明：随着小麦筋力的增强，面团的硬度、弹性、内聚性、胶着性、咀嚼性和回复性升高，黏性降低。相比于“郑麦103”和“郑麦136”，“新麦26”的峰值形成时间较长、峰值扭矩较大且面筋蛋白聚集能较高，面筋蛋白含量更高。随着小麦筋力的增强，面筋蛋白各亚基含量及种类增多。与“郑麦103”和“郑麦136”相比，“新麦26”面筋蛋白的二级结构中β-折叠和β-转角含量增多，α-螺旋含量降低，无规则卷曲含量先减少再增加。小麦筋力越强，面筋蛋白网络结构连续性越好，包裹淀粉能力越强。综上所述，相比于“郑麦103”和“郑麦136”，“新麦26”面筋蛋白含量较高，面筋蛋白亚基种类较多，可促进面筋蛋白的聚集，面筋蛋白中增多的β-折叠结构促进面筋蛋白结构的稳定性，面筋网络结构的连续性增强，进而提高面团的强度和弹性。

Analysis of Gluten Aggregation Characteristics and Structural Characteristics of Wheat with Different Gluten Strengths

By analyzing the dough texture characteristics，gluten protein aggregation characteristics，gluten protein content，molecular weight distribution，secondary structure，and microstructure，the gluten protein aggregation characteristics and structural characteristics of three wheat with different gluten strengths：′Zhengmai 103′，′Zhengmai 136′and′Xinmai 26′were explored and their differences were discussed.The results showed that with the increase of the wheat gluten strength，the hardness，springiness，cohesiveness，gumminess，chewiness and resilience of dough increased，while the adhesiveness decreased.Compared with ′Zhengmai 103′and′Zhengmai 136′，′Xinmai 26′ had a longer peak formation time，higher peak torque，and higher gluten protein aggregation energy.′Xinmai 26′ had a higher gluten protein content.With the increase of wheat gluten strength，the content and types of gluten protein subunits increased.Compared with ′Zhengmai 103′ and′Zhengmai 136′，the contents of β-sheet and β-turn in the secondary structure of ′Xinmai 26′ increased，the content of α-helix decreased，and the content of random coil increased first and then decreased.The stronger the gluten strength of wheat，the better the continuity of the gluten protein network structure，and the stronger the ability to wrap starch.In conclusion，compared with′Zhengmai 103′and′Zhengmai 136′，′Xinmai 26′had a higher gluten protein content，more types of gluten protein subunits，which can promote the aggregation of gluten proteins，and the increased β-sheet structure in gluten protein promoted the stability of gluten protein structure，enhanced the continuity of gluten network，thereby improving the strength and springiness of dough.