蛋白质二级结构
化学
傅里叶变换红外光谱
面筋
含水量
玻璃化转变
红外光谱学
光谱学
酰胺
大气温度范围
结晶学
分析化学(期刊)
化学工程
食品科学
色谱法
热力学
有机化学
生物化学
量子力学
物理
工程类
岩土工程
聚合物
作者
Dominique M.R. Georget,Peter Belton
出处
期刊:Biomacromolecules
[American Chemical Society]
日期:2006-01-05
卷期号:7 (2): 469-475
被引量:238
摘要
The effect of temperature on gluten conditioned at the following water contents, 0%, 13%, and 47% (wet weight basis), was studied by FTIR spectroscopy over the temperature range of 25−85 °C. A detailed discussion of the assignment of the amide I band is given. At 0% hydration no changes in the secondary structure with temperature could be detected; spectra were consistent with a tight disordered structure with many protein−protein interactions. At 13% hydration, distinctive changes occurred in the low-frequency region of the amide I band (1630−1613 cm-1). This was attributed to changes in the β-sheet structure. On cooling to 25 °C, these changes were mainly reversed. It was noted that most of the changes observed occurred above the glass transition temperature. At 47% hydration, more complex changes took place: as the temperature was raised distinct bands at 1630 and 1613 cm-1 merged. However, this process was partially reversed, with recovery of both bands, on cooling. The significance of these results in relation to other changes in gluten proteins in flour and dough with temperature and water content is discussed.
科研通智能强力驱动
Strongly Powered by AbleSci AI