Enzyme-Carbon Nanotube Conjugates in Room Temperature Ionic Liquids

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Authors
Eker, Bilge
Asuri, Prashanth
Murugesan, Saravanababu
Linhardt, Robert J.
Dordick, Jonathan S.
Issue Date
2007-11-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Room-temperature ionic liquids (RTILs) are intriguing solvents, which are recognized as "green" alternatives to volatile organics. Although RTILs are nonvolatile and can dissolve a wide range of charged, polar, and nonpolar organic and inorganic molecules, there remain substantial challenges in their use, not the least of which is the solvents' high viscosity that leads to potential mass transfer limitations. In the course of this work, we discovered that the simple adsorption of the bacterial protease, proteinase K, onto single-walled carbon nanotubes (SWNTs) results in intrinsically high catalytic turnover. The high surface area and the nanoscopic dimensions of SWNTs offered high enzyme loading and low mass transfer resistance. Furthermore, the enzyme-SWNT conjugates displayed enhanced thermal stability in RTILs over the native suspended enzyme counterpart and allowed facile reuse. These enzyme-SWNT conjugates may therefore provide a way to overcome key operational limitations of RTIL systems.
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Applied Biochemistry and Biotechnology, 143, 153-163
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Full Citation
Enzyme-Carbon Nanotube Conjugates in Room Temperature Ionic Liquids, B. Eker, P. Asuri, S. Murugesan, R. J. Linhardt, J. S. Dordick, Applied Biochemistry and Biotechnology, 143, 153-163, 2007.
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2732289
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