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Enhanced stability of enzymes adsorbed onto nanoparticles

机译:增强吸附在纳米颗粒上的酶的稳定性

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We have discovered that the highly curved surface of C-60 fullerenes enhances enzyme stability in strongly denaturing environments to a greater extent than flat supports. The half-life of a model enzyme, soybean peroxidase, adsorbed onto fullerenes at 95 degrees C was 117 min, ca. 2.5-fold higher than that of the enzyme adsorbed onto graphite flakes and ca. 13-fold higher than that of the native enzyme. Furthermore, this phenomenon is not unique to fullerenes, but can also be extended to other nanoscale supports including silica and gold nanoparticles. The enhanced stability was exploited in the preparation of highly active and stable polymer-nanocomposite films. The ability to enhance protein stability by interfacing them with nanomaterials may impact numerous fields ranging from the design of diagnostics, sensors, and nanocomposites to drug delivery.
机译:我们已经发现,C-60富勒烯的高度弯曲表面在强变性环境中比平面载体更大程度地增强了酶的稳定性。模型酶大豆过氧化物酶在95摄氏度下吸附在富勒烯上的半衰期约为117分钟。比吸附在石墨薄片上的酶高约2.5倍比天然酶高13倍。此外,这种现象不是富勒烯独有的,而且还可以扩展到包括二氧化硅和金纳米颗粒在内的其他纳米级载体。在制备高活性和稳定的聚合物-纳米复合材料薄膜中利用了增强的稳定性。通过将蛋白质与纳米材料连接来增强蛋白质稳定性的能力可能会影响从诊断,传感器和纳米复合材料的设计到药物递送的众多领域。

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