A small-angle X-ray scattering study of gliadins in distilled water over a wide concentration range

A small-angle X-ray scattering study of gliadins in distilled water over a wide concentration range
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蒸馏水中宽浓度范围内麦醇溶蛋白的小角 X 射线散射研究

DOI:
10.1021/acs.jafc.5b02902
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发表时间:
2015
影响因子:
6.1
通讯作者:
Molecular assembly of wheat gliadins into nanostructures
Molecular assembly of wheat gliadins into nanostructures
中科院分区:
农林科学1区
文献类型:
--
作者:
N. Sato;A. Matsumiya;Y. Higashino;S. Funaki;Y. Kitao;Y. Oba;R. Inoue;F. Arisaka;M. Sugiyama;and R. Urade;Molecular assembly of wheat gliadins into nanostructures

文献摘要

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醇溶蛋白是与谷蛋白共同组成面筋蛋白的主要蛋白质之一,它对面团的物理特性有重要影响。在这项研究中,水化醇溶蛋白提取到蒸馏水的纳米结构主要是通过小角X射线散射(SAXS)在很宽的浓度范围内进行了研究。醇溶蛋白可溶于低于10重量%的蒸馏水中。Guinier分析表明,麦醇溶蛋白作为单体与少量的二聚体和低聚物一起存在于非常稀的溶液中。SAXS曲线还表明,颗粒间干扰出现在0.5重量%以上,因为麦醇溶蛋白组件之间的静电排斥。高于15重量%,麦醇溶蛋白形成凝胶状水合固体。在较高浓度下,由于大团聚体的形成,在低q区出现陡峭的上升,在中q区出现宽肩,显示内部的密度波动。本研究表明,SAXS可以有效地揭示水合醇溶蛋白组装体的纳米结构。
Gliadin, one of the major proteins together with glutenin composing gluten, affects the physical properties of wheat flour dough. In this study, nanoscale structures of hydrated gliadins extracted into distilled water were investigated primarily by small-angle X-ray scattering (SAXS) over a wide range of concentrations. Gliadins are soluble in distilled water below 10 wt %. Guinier analyses of SAXS profiles indicate that gliadins are present as monomers together with small amounts of dimers and oligomers in a very dilute solution. The SAXS profiles also indicate that interparticle interference appears above 0.5 wt % because of electrostatic repulsion among gliadin assemblies. Above 15 wt %, gliadins form gel-like hydrated solids. At greater concentrations, a steep upturn appears in the low-qregion owing to the formation of large aggregates, and a broad shoulder appears in the middle-qregion showing density fluctuation inside. This study demonstrates that SAXS can effectively disclose the nanostructure of hydrated gliadin assemblies.