小麦面筋蛋白的玻璃化转变行为。

The glass-transition behaviour of wheat gluten proteins.

作者信息

Noel T R, Parker R, Ring S G, Tatham A S

机构信息

Institute of Food Research, Norwich Laboratory, Norwich Research Park, UK.

出版信息

Int J Biol Macromol. 1995 Apr;17(2):81-5. doi: 10.1016/0141-8130(95)93521-x.

DOI:10.1016/0141-8130(95)93521-x

PMID:7547719

Abstract

The glass-transition behaviour of four hydrated wheat gluten proteins (alpha-gliadin, gamma-gliadin, omega-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 Tg were within the range 397-418 K. Values for the heat capacity increment delta Cp at Tg for the plasticized proteins were also determined and ranged from 0.29-0.47 J g-1 K-1 with no dependence on water content. The differences in glass-transition behaviour of the proteins are discussed in relation to their secondary structure.

摘要

使用差示扫描量热法（DSC）研究了四种水合小麦面筋蛋白（α-醇溶蛋白、γ-醇溶蛋白、ω-醇溶蛋白和谷蛋白的高分子量（HMW）亚基）的玻璃化转变行为。通过将数据拟合到先前用于描述稀释剂对聚合物增塑作用的戈登-泰勒方程，通过外推法得出了干燥蛋白质的玻璃化转变温度（Tg）。Tg值在397 - 418 K范围内。还测定了增塑蛋白质在Tg时的热容增量ΔCp值，其范围为0.29 - 0.47 J g⁻¹ K⁻¹，且与含水量无关。讨论了蛋白质玻璃化转变行为的差异与其二级结构的关系。