期刊
FOOD CHEMISTRY
卷 197, 期 -, 页码 1184-1190出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2015.11.085
关键词
Wheat glutenin subunits; Secondary structure of gluten; Microstructure; Dough rheological behavior
资金
- National Natural Science Foundation of China [31501300]
- National Special Program for Transgenetic Wheat Breeding from The Ministry of Agriculture of the People's Republic of China [2013ZX08002-003]
- Coordinator innovative engineering project of Shaanxi Province [2014KTZB02-01-01]
- Research Fund for the Doctoral Program of Northwest AF University [2013BSJJ055]
- Chinese Universities Scientific Fund [2452015009]
Glutenin is one of the critical gluten proteins that affect the processing quality of wheat dough. High-molecular-weight glutenin subunits (HMW-GS) affect rheological behavior of wheat dough. This research demonstrated the effects of four variations of HMW-GS composition at the Glu-B1 locus on secondary and micro structures of gluten and rheological properties of wheat dough, using the bread wheat Xinong 1330 and its three near-isogenic lines (NILs). Results indicated that the Amide I bands of the four wheat lines shifted slightly, but the secondary structure, such as content of alpha-helices, beta-sheets, disulfide bands, tryptophan bands and tyrosine bands, differed significantly among the four NILs. The micro structure of gluten in NIL 2 (Bx14 + By15) and NIL 3 (Bx17 + By18) showed more cross linkage, with two contrasting patterns. Correlation analysis demonstrated that the content of beta-sheets and disulfide bonds has a significant relationship with dough stability, which suggests that the secondary structures could be used as predictors of wheat quality. (C) 2015 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据