Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles
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 gold nanocrystals was used to quantify the extent of the dispersion stability and functionalization. It is found that the reduce...
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doaj-56d61302126a49dfbe4a746ded46a3472020-11-25T01:14:44ZengAIP Publishing LLCAIP Advances2158-32262016-01-0161015005015005-810.1063/1.4939849019601ADVInfluence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticlesA. Nitthin Ananth0A. Nimrodh Ananth1Sujin P. Jose2S. Umapathy3T. Mathavan4Nano Laboratory, School of Physics, Madurai Kamaraj University, Madurai – 625 021, Tamil Nadu, IndiaNano Laboratory, School of Physics, Madurai Kamaraj University, Madurai – 625 021, Tamil Nadu, IndiaNano Laboratory, School of Physics, Madurai Kamaraj University, Madurai – 625 021, Tamil Nadu, IndiaNano Laboratory, School of Physics, Madurai Kamaraj University, Madurai – 625 021, Tamil Nadu, IndiaDepartment of Physics, N.M.S.S.V.N College, Madurai – 625 019, Tamil Nadu, IndiaNano gold / α-amylase colloidal dispersions of profound stability were made using simple procedure with a conventional reducing agent. The surface plasmon resonance of the gold nanocrystals was used to quantify the extent of the dispersion stability and functionalization. It is found that the reduced gold nanoparticles 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 gold nanoparticles (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.http://dx.doi.org/10.1063/1.4939849 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
A. Nitthin Ananth A. Nimrodh Ananth Sujin P. Jose S. Umapathy T. Mathavan |
spellingShingle |
A. Nitthin Ananth A. Nimrodh Ananth Sujin P. Jose S. Umapathy T. Mathavan Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles AIP Advances |
author_facet |
A. Nitthin Ananth A. Nimrodh Ananth Sujin P. Jose S. Umapathy T. Mathavan |
author_sort |
A. Nitthin Ananth |
title |
Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
title_short |
Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
title_full |
Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
title_fullStr |
Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
title_full_unstemmed |
Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
title_sort |
influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles |
publisher |
AIP Publishing LLC |
series |
AIP Advances |
issn |
2158-3226 |
publishDate |
2016-01-01 |
description |
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 gold nanocrystals was used to quantify the extent of the dispersion stability and functionalization. It is found that the reduced gold nanoparticles 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 gold nanoparticles (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. |
url |
http://dx.doi.org/10.1063/1.4939849 |
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