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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Heat-Induced Changes Occurring in Oil/Water Emulsions Stabilized by Soy Glycinin and β-Conglycinin
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Heat-Induced Changes Occurring in Oil/Water Emulsions Stabilized by Soy Glycinin and β-Conglycinin

机译：大豆大豆球蛋白和β-伴大豆球蛋白稳定化的油/水乳液中的热诱导变化

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Glycinin and β-conglycinin are the two major proteins in soy protein isolate, and their emulsifying behavior was the subject of this study. These proteins form a thin layer of 30-40 nm when adsorbed at the interface. Microcalorimetric experiments showed that the thermal transitions of these proteins in the emulsion were very similar to those of the proteins in solution. The results also suggested that molecular rearrangements occurred during adsorption of β-conglycinin, as an endothermic transition peak appeared at high temperature when this protein was present at the interface. In general, β-conglycinin exhibited greater emulsifying activity than glycinin, confirming previous reports. Heating at 95 °C for 15 min caused a decrease in solubility of glycinin, and interactions between the oil droplets, with an increase in the apparent viscosity, shear thinning behavior, and droplet particle size distribution of the emulsions. While, similar behavior was noted in b-conglycinin after heating at both 75 and 95 °C. Furthermore, the order of processing affected the subunits' composition at the interface. Heating the solution before emulsification caused a higher protein load at the interface and with all of the subunits present. On the other hand, when heating was carried out after homogenization, the basic glycinin polypeptide and the β subunit of β-conglycinin were absent from the interface, suggesting that heat-induced complexes between these subunits formed and remained soluble in the unadsorbed phase.
机译：大豆球蛋白分离物中的两个主要蛋白是大豆球蛋白和大豆球蛋白，它们的乳化行为是本研究的主题。这些蛋白质吸附在界面上时会形成30-40 nm的薄层。微量热实验表明，乳液中这些蛋白质的热转变与溶液中蛋白质的热转变非常相似。结果还表明，在吸附β-伴大豆球蛋白过程中发生了分子重排，因为当该蛋白质存在于界面时，在高温下会出现吸热跃迁峰。通常，β-伴大豆球蛋白的乳化活性高于大豆球蛋白，证实了以前的报道。在95°C下加热15分钟会导致大豆球蛋白的溶解度降低，油滴之间的相互作用降低，表观粘度，剪切稀化行为和乳液的液滴粒度分布也会增加。同时，在75和95°C加热后，β-伴大豆球蛋白也表现出相似的行为。此外，处理顺序影响了界面上亚基的组成。在乳化之前加热溶液会导致界面和所有亚基存在较高的蛋白质负载。另一方面，当均质化后进行加热时，界面上不存在碱性大豆球蛋白多肽和β-伴大豆球蛋白的β亚基，这表明在这些亚基之间形成了热诱导的复合物，并仍可溶于未吸附相中。

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