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Distribution and function of LMW glutenins, HMW glutenins, and gliadins in wheat doughs analyzed with ‘in situ’ detection and quantitative imaging techniques
Journal of Cereal Science ( IF 3.8 ) Pub Date : 2020-05-01 , DOI: 10.1016/j.jcs.2020.102931
Jose C. Bonilla , Merve Y. Erturk , James A. Schaber , Jozef L. Kokini

Abstract The different gluten subunits, gliadins, LMW glutenins, and HMW glutenins have been reported to play different key roles in different type of wheat products. This paper studied the interaction between gliadin, LMW and HMW glutenins in soft, hard and durum semolina flour doughs during different stages of mixing. In order to see how do the gluten subunits (gliadin, LMW glutenin and HMW glutenin) redistribute during mixing, dough samples were taken at maximum strength and 10 min after maximum strength. The doughs have been mixed with the same level of added water (55%), therefore they all have different strengths values due to their changes in proteins content. Oscillatory rheological measurements were performed on the doughs. It has been found that HMW glutenins are relatively immobile because of their less molecular mobility and do no redistribute themselves especially at high strength for doughs such as hard wheat flour. LMW glutenins and gliadins on the other hand redistribute themselves at even at high dough strengths forming a more stable network. In weaker doughs such as soft wheat, the breakdown of the three proteins subunits is responsible for the decay in dough strength. We have also visualized how the greater amount of LMW glutenins in semolina is in constant interaction with HMW glutenins and gliadins allowing the dough to maintain a stable strength for an extended mixing time. Finally, we have found the ‘in situ’ detection and quantitative analysis techniques to be more sensitive to the changes occurring in the gluten network of the dough than the oscillatory rheological analysis.

中文翻译:

用“原位”检测和定量成像技术分析小麦面团中 LMW 谷蛋白、HMW 谷蛋白和麦醇溶蛋白的分布和功能

摘要 据报道,不同的谷蛋白亚基、麦醇溶蛋白、LMW 谷蛋白和 HMW 谷蛋白在不同类型的小麦产品中发挥着不同的关键作用。本文研究了软、硬和硬质粗面粉面团在不同混合阶段中麦胶蛋白、LMW 和 HMW 谷蛋白之间的相互作用。为了观察面筋亚基(麦醇溶蛋白、LMW 谷蛋白和 HMW 谷蛋白)在混合过程中如何重新分布,在最大强度和最大强度后 10 分钟采集面团样品。面团已与相同水平的添加水 (55%) 混合,因此由于蛋白质含量的变化,它们都具有不同的强度值。对面团进行振荡流变测量。已经发现,HMW 谷蛋白由于其分子移动性较低而相对固定,并且不会重新分配自身,尤其是在高强度下,对于硬质小麦粉等面团。另一方面,即使在高面团强度下,LMW 谷蛋白和麦胶蛋白也会重新分布,形成更稳定的网络。在较弱的面团(如软小麦)中,三个蛋白质亚基的分解是造成面团强度衰减的原因。我们还可视化了粗面粉中大量的 LMW 谷蛋白如何与 HMW 谷蛋白和麦醇溶蛋白持续相互作用,从而使面团在较长的混合时间内保持稳定的强度。最后,
更新日期:2020-05-01
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