This stabilization of proteins through gold nanoparticles occurs through two mechanisms: 1) binding of the protein in its active structure stabilizes that structure; 2) the gold particles lower the interfacial energy between air and water, thus diminishing the driving force for denaturation. The result is a functional biocatalyst that can be readily applied to biotechnological applications.
Enzymes are highly specific and efficient biocatalysts with a wide range of biotechnological and industrial applications. The amphiphilic nature of proteins, however, leads to their instability at air–water and oil–water interfaces. Conditions that expose proteins to these interfacial environments, for instance through transport, printing, or mixing, can cause irreversible protein denaturation leading to a loss of activity.
One way of increasing the stability of proteins is through immobilization of enzymes onto solid supports. Dr. Vincent Rotello and his group used nano-sized particles as scaffolds to support and stabilize the enzyme chymotrypsin. Rotello, the Charles A. Goessmann Professor of Chemistry at the University of Massachusetts, explained his group's recent work to Nanowerk: "The key finding is that we can stabilize proteins under conditions that would normally reduce or eliminate their activity."
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By Michael Berger, Copyright 2006 Nanowerk LLC.