We report a simple method that uses proteins to solubilize single-walled carbon nanotubes (SWNTs) in water. Characterization by a variety of complementary techniques including UV-Vis spectroscopy, Raman spectroscopy, and atomic force microscopy confirmed the dispersion at the individual nanotube level. A variety of proteins differing in size and structure were used to generate individual nanotube solutions by this noncovalent functionalization procedure. Protein-mediated solubilization of nanotubes in water may be important for biomedical applications. This method of solubilization may also find use in approaches for controlling the assembly of nanostructures, and the wide variety of functional groups present on the adsorbed proteins may be used as orthogonal reactive handles for the functionalization of carbon nanotubes.

We report the activity, stability, and reusability of enzyme-carbon nanotube conjugates in aqueous solutions. A variety of enzymes were covalently attached to oxidized multi-walled carbon nanotubes (MWNTs). These conjugates were soluble in aqueous buffer, retained a high fraction of their native activity, and were stable at higher temperatures relative to their solution phase counterparts. Furthermore, the high surface area of MWNTs afforded high enzyme loadings, yet the intrinsic high length of the MWNT led to facile filtration. These water-soluble carbon nanotube-enzyme conjugates represent novel preparations that possess the virtues of both soluble and immobilized enzymes, thus providing a unique combination of useful attributes such as low mass transfer resistance, high activity and stability, and reusability.

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