The glass-transition behaviour of wheat gluten proteins.
The glass-transition behaviour of wheat gluten proteins.
复制标题
DOI：
10.1016/0141-8130(95)93521-x
复制
发表时间：
1995
影响因子：
8.2
通讯作者：
T. Noel;R. Parker;S. Ring;A. Tatham
中科院分区：
文献类型：
--
作者：
T. Noel;R. Parker;S. Ring;A. Tatham
采用差示扫描量热法（DSC）研究了4种水合小麦面筋蛋白（α-醇溶蛋白、γ-醇溶蛋白、ω-醇溶蛋白和高分子量麦谷蛋白亚基）的玻璃化转变行为。通过拟合的戈登-泰勒方程，这是以前被用来描述聚合物的塑化稀释剂的数据，玻璃化转变温度（Tg）的干蛋白质，发现外推。Tg值在397-418 K之间。还测定了增塑蛋白质在Tg时的热容量增量Δ Cp值，其范围为0.29 - 0.47 J g-1 K-1，与水含量无关。蛋白质的玻璃化转变行为的差异进行了讨论，在其二级结构。
The glass-transition behaviour of four hydrated wheat gluten proteins (α-gliadin, γ-gliadin, ω-gliadin and high-molecular-weight (HMW) subunits of glutenin) was studied using differential scanning calorimetry (DSC). By fitting the data to the Gordon-Taylor equation, which has previously been used to describe the plasticization of polymers by diluents, the glass-transition temperatures (Tg) for the dry proteins were found by extrapolation. The values for Tgwere within the range 397–418 K. Values for the heat capacity increment ACp at Tgfor the plasticized proteins were also determined and ranged from 0.29−0.47 J g−1K−1with no dependence on water content. The differences in glass-transition behaviour of the proteins are discussed in relation to their secondary structure.