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卵清蛋白-阿拉伯胶复合凝聚体的结构特征和流变性能。

Structural characteristics and rheological properties of ovalbumin-gum arabic complex coacervates.

机构信息

Food Safety Key Lab of Zhejiang Province, The School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China.

Food Safety Key Lab of Zhejiang Province, The School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China.

出版信息

Food Chem. 2018 Sep 15;260:1-6. doi: 10.1016/j.foodchem.2018.03.141. Epub 2018 Mar 30.

DOI:10.1016/j.foodchem.2018.03.141
PMID:29699649
Abstract

After formation of the ovalbumin (OVA)-gum arabic (GA) complex coacervates, a more ordered crystal structure was obtained, and the protein denaturation temperature increased from 72 to 96 °C. GA can reduce the pH-induced conformational perturbations of ovalbumin. The presence of GA improved the stability of the α-helix and β-turn regions against pH, but showed less influence on the random coil and β-sheet domains. The complex coacervates showed the highest viscosity value at pH 3.7 compared with the other pH values tested (4.0, 3.4, 3.0, 2.7) due to the stronger interactions of OVA and GA. A large thixotropic loop was observed for the coacervate obtained at pH 3.7 compared with that obtained at pH 4.0. Moreover, the salt concentration and OVA:GA ratio influenced the rheological properties by affecting the structure and composition of the complexes. A stronger interaction between OVA and GA led to greater viscoelastic properties.

摘要

卵清蛋白(OVA)-阿拉伯胶(GA)复合凝聚物形成后,得到了更有序的晶体结构,蛋白质变性温度从 72°C 升高到 96°C。GA 可以减少 pH 诱导的卵清蛋白构象扰动。GA 的存在提高了 α-螺旋和 β-转角区域对 pH 的稳定性,但对无规卷曲和 β-折叠结构域的影响较小。与其他测试 pH 值(4.0、3.4、3.0、2.7)相比,复合凝聚物在 pH 3.7 时表现出最高的黏度值,这是由于 OVA 和 GA 之间更强的相互作用。与在 pH 4.0 时相比,在 pH 3.7 时获得的凝聚物具有较大的触变环。此外,盐浓度和 OVA:GA 比通过影响复合物的结构和组成来影响流变性质。OVA 和 GA 之间更强的相互作用导致更大的黏弹性。

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