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首页> 外文会议>ICEF11;International congress on engineering and food >Investigation on the relationship between rheological properties and structure of proteins to improve the viscoelasticity of zein dough through high molecular weight (HMW) glutenin addition
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Investigation on the relationship between rheological properties and structure of proteins to improve the viscoelasticity of zein dough through high molecular weight (HMW) glutenin addition

机译：通过添加高分子量谷蛋白来改善玉米蛋白面团的粘弹性的蛋白质流变特性与蛋白质结构的关系的研究

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Among cereal proteins, only wheat gluten is considered to have the unique ability to form a viscoelasticdough upon hydration and mixing. Gluten is generally divided into two protein groups based on theirsolubility: the gliadins and glutenins. Gliadins are aqueous alcohol-soluble monomeric proteins. On the otherhand, glutenins are insoluble in alcohols and exist as polymeric proteins stabilized by inter-chain disulphidebonds. In addition, the high molecular weight (HMW) subunits of glutenin are considered to be the maindeterminant of the viscoelastic properties of gluten and dough. The contribution of HMW glutenin to glutenelasticity has been associated with its ability to form secondary structure β-type conformations, which havebeen found to play an important role on the elasticity of gluten. Unlike wheat gluten, zein, the major storageprotein of maize, is not able to form viscoelastic dough at room temperature. Until now very little work hasbeen performed on the viscoelasticity of the zein dough systems. Zein is an alcohol-soluble protein analogousin a number of respects to gliadin in wheat gluten and lacks HMW glutenin which as discussed is thought tobe responsible for the elasticity of dough. In a previous study in our laboratory, zein was found to present asecondary structure which was mainly composed of α-helices. However, upon hydration at 35°C, asignificant increase in β-sheet structure and decrease in α-helical structure was observed. Based on thosepreliminary data it is now hypothesized that addition of co-protein, such as HMW subunits of glutenin inwheat gluten, may improve the viscoelasticity of zein dough systems. Therefore, zein and gliadin doughsystems were prepared with and without HMW glutenin addition at different amounts of HMW glutenin.Large deformation rheological measurements were performed by using lubricated squeezing flow viscometryto determine the extensional viscosities of the dough samples. Secondary structures of proteins in dough statewere determined by using Fourier Transform InfraRed (FTIR) spectrometry. An increase in extensionalviscosity (η_(ext)) values, determined by squeezing flow viscometry was obtained with the addition of HMWglutenin to both zein and gliadin samples. The effect of HMW glutenin on zein was more distinctive than ongliadin. Infrared spectra also indicated changes in zein structure with HMW glutenin addition.
机译：在谷物蛋白中，仅小麦面筋被认为具有形成粘弹性的独特能力 水合和混合后的面团。麸质通常根据其蛋白质分为两个蛋白质组 溶解度：麦醇溶蛋白和谷蛋白。麦醇溶蛋白是可溶于水的单体蛋白。在另一 另一方面，谷蛋白不溶于醇，并以通过链间二硫化物稳定的聚合蛋白形式存在 债券。此外，谷蛋白的高分子量（HMW）亚基被认为是主要的 面筋和面团的粘弹性的决定因素。 HMW谷蛋白对面筋的贡献 弹性与其形成二级结构β型构象的能力有关， 被发现对面筋的弹性起重要作用。与小麦面筋，玉米蛋白不同，主要储存 玉米蛋白，在室温下不能形成粘弹性面团。到现在为止，几乎没有什么工作 对玉米蛋白面团系统的粘弹性进行测试。玉米醇溶蛋白是一种醇溶性蛋白类似物 小麦面筋中的麦醇溶蛋白在许多方面都缺乏，但缺乏HMW谷蛋白，如前所述 负责面团的弹性。在我们实验室的先前研究中，玉米蛋白被发现具有 二级结构，主要由α-螺旋组成。但是，在35°C水化后， 观察到β-折叠结构的显着增加和α-螺旋结构的减少。基于那些 初步数据是，现在假设添加了辅助蛋白，例如谷胱甘肽的HMW亚基 小麦面筋，可能会改善玉米蛋白面团系统的粘弹性。因此，玉米蛋白和麦醇溶蛋白面团 在不同的HMW谷蛋白量下添加和不添加HMW谷蛋白制备系统。 使用润滑挤压流动粘度法进行大变形流变测量 确定面团样品的拉伸粘度。面团状态下蛋白质的二级结构 使用傅立叶变换红外（FTIR）光谱法测定。伸展运动的增加 通过添加HMW获得通过挤压流动粘度法测定的粘度（η_（ext））值 玉米蛋白和麦醇溶蛋白样品中的谷蛋白。 HMW谷蛋白对玉米醇溶蛋白的作用比对玉米醇溶蛋白的影响更明显 麦醇溶蛋白。红外光谱还表明，添加HMW谷蛋白的玉米醇溶蛋白结构发生了变化。

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