Enzyme-Nanomaterial-Polymer Composites as Antifouling Surfaces

The molecular level interactions that govern the structure, function, and stability of proteins on the surface of nanoscale materials is being elucidated through experimental and computational strategies. This information has been used to assemble functional nanobiocomposites.

In one example, enzyme-nanomaterial-polymer composites have been prepared and are endowed with surface active properties that completely resist protein fouling (Dordick, Kane). This is important as the initial attachment of proteins to surfaces represents the key event in the binding of microorganisms, which ultimately lead to the formation of intractable biofilms. The enzyme-nanomaterial-polymer composites were prepared with the proteolytic enzyme subtilisin (commonly found in laundry detergents) and trypsin, both conjugated to single-wall carbon nanotubes and embedded within a poly(methyl methacrylate) polymer.

Challenging the composite with a blood serum protein resulted in the complete resistance of the polymer surface to the protein. For polymer without the enzyme-nanotube conjugate, high protein binding was observed. Microbial and biological molecule adhesion to surfaces is a problem that impacts industrial, medical, and security applications. Retarding the binding of these agents onto surfaces will extend the lifetime of a material, eliminate toxic compounds (e.g., chemical and biological threats), prevent spread of disease, and enable medical and implantable materials to be more benign.