title: Enhanced stability of enzymes adsorbed onto nanoparticles.
abstract: We have discovered that the highly curved surface of C60 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.
authors: Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
authors: Prashanth
authors: P
authors: Asuri
authors: Sandeep S
authors: SS
authors: Karajanagi
authors: Alexey A
authors: AA
authors: Vertegel
authors: Jonathan S
authors: JS
authors: Dordick
authors: Ravi S
authors: RS
authors: Kane
mesh_terms: D000327:Adsorption; D002384:Catalysis; D016503:Drug Delivery Systems; D004563:Electrochemistry / Q000379:methods; D004798:Enzymes / Q000737:chemistry*; D037741:Fullerenes / Q000737:chemistry*; D006108:Graphite; D018625:Microscopy, Atomic Force; D008956:Models, Chemical; D053758:Nanoparticles / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D009195:Peroxidase / Q000737:chemistry; D011485:Protein Binding; D013025:Glycine max / Q000201:enzymology
chemical_list: D004798:Enzymes; D037741:Fullerenes; D006108:Graphite; D009195:Peroxidase; C069837:fullerene C60