Gelling Properties of Soybean β-Conglycinin Having Different Subunit Compositions
Gelling Properties of Soybean β-Conglycinin Having Different Subunit Compositions
复制标题
DOI：
10.1271/bbb.68.1091
复制
发表时间：
2004-01
期刊：
影响因子：
--
通讯作者：
Bin Mohamed Salleh Mohamad Ramlan;N. Maruyama;Koji Takahashi;K. Yagasaki;T. Higasa;Y. Matsumura;S. Utsumi
中科院分区：
文献类型：
--
作者：
Bin Mohamed Salleh Mohamad Ramlan;N. Maruyama;Koji Takahashi;K. Yagasaki;T. Higasa;Y. Matsumura;S. Utsumi
将蛋白质浓度、加热温度和时间对缺乏α或α'亚基的大豆β-伴大豆球蛋白（7S球蛋白）的胶凝特性的影响与含有所有三个亚基（α、α'和β）的7S进行比较，以确定每个亚基的贡献是否相等。在大多数情况下，凝胶硬度的相对顺序为α′-缺乏>7S>α-缺乏。从傅里叶变换红外研究来看，三个样品加热后二级结构的变化非常相似；因此，二次结构变化并不是凝胶硬度差异的原因。通过使用扫描电子显微镜，我们观察到三个样品之间链厚度和凝胶网络密度的差异。这些差异与凝胶硬度的差异密切相关。
The effects of protein concentration, and heating temperature and time on the gelling properties of soybean β-conglycinin (7S globulins) lacking the α or α′ subunit were compared with those of 7S containing all three subunits (α, α′, and β) to determine whether each subunit contributes equally. In most of the conditions, the relative order of gel hardness was α′-lacking > 7S > α-lacking. From Fourier transform infrared studies, the secondary structure change after heating was very similar among the three samples; thus, the secondary structural change is not the reason for the differences in gel hardness. By using scanning electron microscopy, we observed differences in strand thickness and the density of the gel network among the three samples. These differences correlated well with the differences in gel hardness.