4.2 Article

Enhanced stability of enzymes adsorbed onto nanoparticles

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JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
卷 7, 期 4-5, 页码 1675-1678

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AMER SCIENTIFIC PUBLISHERS
DOI: 10.1166/jnn.2007.453

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fullerenes; nanoparticles; enzyme stability; biocatalytic films

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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.

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