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
复制标题
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
中科院分区:
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
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.