谷蛋白
面筋
醇溶蛋白
作文(语言)
蛋白质亚单位
蛋白质二级结构
食品科学
化学
普通小麦
小麦面筋
流变学
面包制作
植物蛋白
植物
生物
生物化学
材料科学
基因
语言学
哲学
复合材料
染色体
作者
Xuejun Li,Tianhong Liu,Lijun Song,Heng Zhang,Liqun Li,Xin Gao
标识
DOI:10.1016/j.foodchem.2016.07.043
摘要
As one of critical gluten proteins, high-molecular-weight glutenin subunits (HMW-GS) mainly affect the rheological behaviour of wheat dough. The influence of HMW-GS variations at the Glu-A1 and Glu-D1 loci on both secondary and micro structures of gluten and rheological properties of wheat dough was investigated in this study. Results showed that the Amide I bands of the three near-isogenic lines (NILs) shifted slightly, but the secondary structures differed significantly. The micro structure of gluten in NIL 4 (Ax null) showed bigger apertures and less connection, compared to that in Xinong 1330 (Ax1). The micro structure of gluten in NIL 5 (Dx5+Dy10) showed more compact than that in Xinong 1330 (Dx2+Dy12). Correlation analysis demonstrated that the content of β-sheets and disulfide bonds in gluten has a significant relationship with dough properties. The secondary structures of native gluten are suggested to be used as predictors of wheat quality.
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