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Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles
4.F. Tatini, I. Landini, F. Scaletti, L. Massai, S. Centi, F. Ratto, S. Nobili, G. Romano, F. Fusi, L. Messori, E. Mini, and R. Pini, J. Mater. Chem. B 2, 6072 (2014).
7.A. Sileikaite, J. Puiso, I. Prosycevas, and S. Tamulevicius, Materials Science 15, 21 (2009).
See supplementary material at http://dx.doi.org/10.1063/1.4939849
for supplementary material to this article at AIP Advances which supports the stability of α-amylase – nano gold colloidal systems and also the vibrational signature confirms that protein does not denature.[Supplementary Material]
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Nano gold / α-amylase colloidal dispersions of profound stability were made using simple procedure with a conventional reducing agent. The surface plasmon resonance of the goldnanocrystals was used to quantify the extent of the dispersion stability and functionalization. It is found that the reduced goldnanoparticles were trapped into the protein network without denaturation the structure of α-amylase protein. This kind of entrapment of particles into the protein network prevents clustering of individual goldnanoparticles (6.42 nm ± 0.92 nm) by acting as a natural spacer. Systematic entrapment was facilitated by the affinity of gold to the sulfur moieties (Au-S) in the protein structure.
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