Enhanced stability of enzymes adsorbed onto nanoparticles

被引:56
作者
Asuri, Prashanth
Karajanagi, Sandeep S.
Vertegel, Alexey A.
Dordick, Jonathan S. [1 ]
Kane, Ravi S.
机构
[1] Rensselaer Polytech Inst, Dept Chem & Biol Engn, Troy, NY 12180 USA
[2] Rensselaer Polytech Inst, Dept Mat Sci & Engn, Troy, NY 12180 USA
关键词
fullerenes; nanoparticles; enzyme stability; biocatalytic films;
D O I
10.1166/jnn.2007.453
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:1675 / 1678
页数:4
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