不同米蛋白组分与铅的结合规律
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Study on Binding Behaviors of Lead to Different Insoluble Rice Proteins
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    摘要:

    为了探究不同米蛋白组分与重金属铅(Pb2+)的结合规律,从动力学、热力学角度对3种水不溶性米蛋白(球蛋白、谷蛋白、醇溶蛋白)与Pb2+的结合特征进行了分析。结果表明:3种蛋白质与Pb2+的结合均很迅速,30 min即可达到反应平衡;醇溶蛋白对Pb2+的结合能力最强,平衡结合量达20.54 mg/g;米蛋白与Pb2+的结合过程符合准二级动力学模型,Langmuir等温吸附模型的拟合效果(R2=0.980~0.995)要优于Freundlich模型(R2=0.847~0.987),说明两者结合以化学吸附为主;热力学参数ΔS°> 0、ΔH°> 0、ΔG°< 0,说明3种米蛋白与Pb2+的结合均为自发、熵驱动的吸热反应。X射线光电子能谱(XPS)表明醇溶蛋白与Pb2+结合后,N1s和S2p的特征峰强度显著降低(P<0.05),说明Pb2+主要与醇溶蛋白中的含氮、含硫基团相结合。扫描电镜(SEM)显示醇溶蛋白与Pb2+结合后,颗粒发生聚集,呈致密团块状结构,进一步验证了Pb2+和醇溶蛋白的结合。

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    The binding characteristics of three water-insoluble rice proteins(globulin, glutenin, prolamin) and Pb2+ were studied from the perspective of kinetics and thermodynamics to explore the binding behaviors of different rice protein components and heavy metal lead ion(Pb2+). The result showed that Pb2+ was rapidly bound to each insoluble rice protein, and the binding equilibrium was reached within 30 min. The prolamin showed the highest binding capacity with a binding adsorption quantity(q) of 20.54 mg/g. The binding of Pb2+ to rice proteins was consistent with the quasi-second-order kinetic model, and the Langmuir equation(R2=0.980~0.995) had greater fitting effect than that of the Freundlich equation(R2=0.847~0.987). The result indicated the interaction between protein subunits and Pb2+ was mainly by chemical absorptions. The thermodynamic parameters, i.e., ΔS°>0, ΔH°>0 and ΔG°<0, indicated the spontaneous, entropy-driven and endothermic binding reaction. X-ray photoelectron spectroscopy(XPS) showed that the characteristic peak intensity of N1s and S2p was significantly decreased after binding (P< 0.05), suggesting that the major binding sites of prolamin for Pb2+ were nitrogen- and sulfur-containing groups. Scanning electron microscopy (SEM) displayed that the prolamin structures aggregated and formed a compact cloddy structure after binding to Pb2+, which further verified the binding of Pb2+ to rice prolamin.

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冯伟,范大明,董田田,李克强,倪双双,王涛,张昊,王韧.不同米蛋白组分与铅的结合规律[J].食品与生物技术学报,2021,40(12):52-58.

FENG Wei, FAN Daming, DONG Tiantian, LI Keqiang, NI Shuangshuang, WANG Tao, ZHANG Hao, WANG Ren. Study on Binding Behaviors of Lead to Different Insoluble Rice Proteins[J]. Journal of Food Science and Biotechnology,2021,40(12):52-58.

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  • 在线发布日期: 2021-12-27
  • 出版日期: 2021-12-25
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