Structural interplay and macroscopic aggregation of rice albumins after binding with heavy metal ions

Structural interplay and macroscopic aggregation of rice albumins after binding with heavy metal ions
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大米清蛋白与重金属离子结合后的结构相互作用和宏观聚集

DOI:
10.1016/j.foodhyd.2019.105248
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发表时间:
2020
期刊:
影响因子:
10.7
通讯作者:
Tao Wang
Tao Wang
中科院分区:
农林科学1区
文献类型:
--
作者:
Ren Wang;Tingting Wang;Tiantian Dong;Qixin Zhong;Zhengxing Chen;Wei Feng;Tao Wang

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谷物重金属污染正在严重威胁人类健康,特别是在中国中部地区。在此,我们报告了大米清蛋白(RA)与 Cu(II)、Cd(II)和 Pb(II)结合后超分子纳米结构发生了巨大变化。原子力显微镜和扫描电子显微镜显示,Cu(II)引发RA的立即沉淀,而Cd(II)和Pb(II)促进核心-卫星结构的形成,核心由多个蛋白质颗粒组成,周围被卫星颗粒包围。荧光和等温滴定量热法研究揭示了熵驱动的自发结合行为。因此,引发了 RA 显着的螺旋片层转变,并由于疏水性吸引力而发生宏观沉淀。我们的结果可能有助于从亲水胶体的角度了解重金属和谷物成分之间的结合,最终开发出检测和去除策略来对抗重金属污染。
Contamination of cereal grains by heavy metals is becoming a serious threat to human health, especially in the central regions of China. Herein, we report drastic changes in the supramolecular nanostructures of rice albumins (RAs) after binding with Cu(II), Cd(II), and Pb(II). Atomic force microscopy and scanning electron microscopy revealed that Cu(II) initiated an immediate precipitation of RAs, whereas Cd(II) and Pb(II) promoted the formation of core-satellite structures with a core of multiple protein particles surrounded by satellite particulates. Fluorescence and isothermal titration calorimetry studies revealed an entropy-driven, spontaneous behavior of the binding. Consequently, remarkable helix-sheet transitions of RAs were triggered and macroscopic precipitation occurred due to hydrophobic attraction. Our results may help to understand the binding between heavy metals and cereal ingredients from a hydrocolloid perspective to eventually develop detection and removal strategies to combat heavy metal contamination.
大米蛋白和大豆分离蛋白之间的结构相互作用机制设计新型蛋白质亲水胶体
DOI: 10.1016/j.foodhyd.2018.06.024
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