面筋蛋白在乙醇水溶液中的聚合组装
Polymeric Assembly of Gluten Proteins in an Aqueous Ethanol Solvent
摘要：
小麦面筋蛋白的超分子结构在很大程度上是未知的，由于这个家族的蛋白质的内在复杂性和它们在水中的不溶性。我们在水/乙醇（50/50 v/v）中破碎谷蛋白，并获得蛋白质提取物，其耗尽麦醇溶蛋白（小麦谷蛋白的单体部分），并富含谷蛋白（小麦谷蛋白的聚合部分）。我们调查的结构的蛋白质在溶剂中用于提取在很宽的浓度范围内，通过结合X射线散射和多角度静态和动态光散射。我们的数据表明，在乙醇/水混合物中，蛋白质显示出良好溶剂中柔性聚合物链的特征。在稀的制度，蛋白质形成非常松散的结构的特征尺寸为150 nm，与内部动力学，这是定量类似的分支聚合物线圈。在更集中的制度，数据突出了一个层次结构与一个特征的长度尺度的顺序为几纳米，这显示了缩放与浓度预期的半稀释聚合物在良好的溶剂，和分形排列在更大的长度尺度。这种结构与聚合物凝胶的结构惊人地相似，从而提供了一些事实知识来合理化小麦面筋蛋白及其组装体的粘弹性。
英文摘要：
The supramolecular organization of wheat gluten proteins is largely unknown due to the intrinsic complexity of this family of proteins and their insolubility in water. We fractionate gluten in a water/ethanol (50/50 v/v) and obtain a protein extract which is depleted in gliadin, the monomeric part of wheat gluten proteins, and enriched in glutenin, the polymeric part of wheat gluten proteins. We investigate the structure of the proteins in the solvent used for extraction over a wide range of concentration, by combining X-ray scattering and multi-angle static and dynamic light scattering. Our data show that, in the ethanol/water mixture, the proteins display features characteristic of flexible polymer chains in a good solvent. In the dilute regime, the protein form very loose structures of characteristic size 150 nm, with an internal dynamics which is quantitatively similar to that of branched polymer coils. In more concentrated regimes, data highlight a hierarchical structure with one characteristic length scale of the order of a few nm, which displays the scaling with concentration expected for a semi-dilute polymer in good solvent, and a fractal arrangement at much larger length scale. This structure is strikingly similar to that of polymeric gels, thus providing some factual knowledge to rationalize the viscoelastic properties of wheat gluten proteins and their assemblies.
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