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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Main Authors: A. Nitthin Ananth, A. Nimrodh Ananth, Sujin P. Jose, S. Umapathy, T. Mathavan
Format: Article
Language:English
Published: AIP Publishing LLC 2016-01-01
Series:AIP Advances
Online Access:http://dx.doi.org/10.1063/1.4939849
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spelling 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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