Comparison of molecular and emulsifying properties of gum arabic and mesquite gum using asymmetrical flow field-flow fractionation
Comparison of molecular and emulsifying properties of gum arabic and mesquite gum using asymmetrical flow field-flow fractionation
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DOI：
10.1016/j.foodhyd.2011.04.008
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发表时间：
2012-01-01
影响因子：
10.7
通讯作者：
Nilsson, Lars
中科院分区：
文献类型：
--
作者：
Alftren, Johan;Penarrieta, J. Mauricio;Nilsson, Lars
采用多角度光散射与折射率检测相结合的非对称流场流动分级技术，对阿拉伯胶(GA)和麦斯奎胶(MG)的分子和乳化性质进行了表征。测定了摩尔质量、均方根半径(r(RMS))、流体动力学半径(r(H))、构象、表观密度和蛋白质物质在整个摩尔质量范围内的分布等性质。GA具有低摩尔质量(3.4×10(5)g/mol)、低蛋白质组分(种群1)和高摩尔质量(1.9×10(6)g/mol)、富含蛋白质组分(种群2)。镁的摩尔质量为1，平均摩尔质量为1.1×10(6)g/mol。GA和MG的构象(r(RMS)/r(H))都随着摩尔质量的增加而变得越来越球形。然而，对于特定的摩尔质量，MG具有较高的r(RMS)/r(H)值，这表明GA和MG在结构上存在差异。两种牙胶的蛋白质含量都随着摩尔质量的增加而增加，但GA的增加幅度更大。在乳化实验中，可以观察到GA第二种群的选择性吸附，这可能是由于GA的蛋白质含量更高，结构更灵活，使其具有比第一种群更强的表面活性。从乳液稳定性的角度比较GA和MG，可以得出结论：GA稳定的乳液具有相当高的抗聚结稳定性。(C)2011爱思唯尔有限公司。保留所有权利。
The molecular and emulsifying properties of gum arabic (GA) and mesquite gum (MG) were characterized using asymmetrical flow field-flow fractionation connected to multi-angle light scattering and refractive index detection. Properties such as molar mass, root-mean-square radius (r(rms)), hydrodynamic radius (r(h)), conformation, apparent densities and distribution of proteinaceous matter over the whole molar mass range were determined. GA displayed a low molar mass (3.4 x 10(5) g/mol), protein-poor component (population 1) and a high molar mass (1.9 x 10(6) g/mol), protein-rich component (population 2). MG displayed one molar mass population with an average molar mass of 1.1 x 10(6) g/mol. For both GA and MG, the conformation (r(rms)/r(h)) was increasingly spherical with increasing molar mass. However, MG had higher values of r(rms)/r(h) for a specific molar mass suggesting differences in structure between GA and MG. The protein content increased with increasing molar mass for both gums, although to a higher extent for GA. Selective adsorption, during emulsification experiments, could be observed of population 2 of GA which may be due to a combination of the higher protein content and a more flexible structure rendering it more surface active than population 1. Comparing GA and MG in terms of emulsion stability, it could be concluded that GA-stabilized emulsions have considerably higher stability against coalescence. (C) 2011 Elsevier Ltd. All rights reserved.