(370c) Enhanced Stability of Enzymes Adsorbed Onto Nanoparticles

Authors: 
Asuri, P. - Presenter, Rensselaer Polytechnic Institute
Karajanagi, S. S. - Presenter, Rensselaer Polytechnic Institute
Vertegel, A. A. - Presenter, Rensselaer Polytechnic Institute
Kane, R. S. - Presenter, Rensselaer Polytechnic Institute
Dordick, J. S. - Presenter, Rensselaer Polytechnic Institute


The emergence of nanomaterials with precise dimensions, geometries, and surface properties has resulted in an increasingly large number of applications ranging from electronics and sensing elements to high-strength, lightweight materials. To date, proteins and other biomolecules have been used to functionalize nanomaterials and influence their properties. However, very little is known about the ability of these nanoscale materials to enhance protein structure and function. 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. Furthermore, this phenomenon is not unique to fullerenes, but can also be extended to other nanoscale supports including silica and gold nanoparticles. This study supports the hypothesis that protein stabilization strongly correlates with the unique surface curvature present on nanoscale materials. The enhanced stability provided by fullerenes and other nanoparticles was exploited in the preparation of highly active enzyme-containing films that are stable under highly denaturing conditions. Further extension of this phenomenon to other enzyme systems and nanomaterials would directly impact the design of novel hybrid materials that integrate biotic and abiotic components.