The effect of pH on heat denaturation and gel forming properties of soy proteins
The effect of pH on heat denaturation and gel forming properties of soy proteins
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DOI：
10.1016/s0168-1656(00)00239-x
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发表时间：
2000-05-26
影响因子：
4.1
通讯作者：
van Vliet, T
中科院分区：
文献类型：
--
作者：
Renkema, JMS;Lakemond, CMM;van Vliet, T
本文研究了pH值对大豆分离蛋白和大豆球蛋白凝胶形成特性的影响。在pH 7.6时，形成更多的细链凝胶，其特征在于低G'值和光滑、略微浑浊的外观，而在pH 3.8时，获得粗凝胶，其具有高硬度和颗粒状的白色外观。如在pH 7.6下发现的低G'值与大豆球蛋白和大豆蛋白分离物的高溶解度相关（约100%）。50%）。在pH 3.8时，所有蛋白质在加热时沉淀，这与相对高的G'值相关。β-伴大豆球蛋白在SPI凝胶化过程中的作用在pH 7.6下似乎较小，这由以下事实表明：与pH 3.8相反，在β-伴大豆球蛋白热变性后没有开始显著的凝胶形成。此外，凝胶形成的机制似乎受pH的影响，因为与pH 3.8相比，在pH 7.6下，大豆球蛋白的酸性多肽和碱性多肽之间的二硫桥在加热时断裂。(C)2000 Elsevier Science B. V.保留所有权利。
This study is focussed on the influence of pH on the gel forming properties of soy protein isolate and purified glycinin in relation to denaturation and aggregation. At pH 7.6 more fine-stranded gels were formed characterised by low G' values, and a smooth, slightly turbid appearance, whereas at pH 3.8 coarse gels were obtained with a high stiffness and a granulated, white appearance. Low G' values, as found at pH 7.6, correlate with a high solubility of glycinin and soy protein isolate (ca. 50%) after heating at low protein concentration. At pH 3.8 all protein precipitated upon heating, which correlates with relatively high G' values. The role of beta-conglycinin during gelation of SPI seems to be minor at pH 7.6, which is indicated by the fact that, in contrast to pH 3.8, notable gel formation did not start upon heat denaturation of beta-conglycinin. Furthermore, the mechanism of gel formation seems to be affected by pH, because at pH 7.6, in contrast to pH 3.8, the disulphide bridge between the acidic and the basic polypeptide of glycinin is broken upon heating. (C) 2000 Elsevier Science B.V. All rights reserved.