Enhanced immobilization of hexa-arginine-tagged esterase on gold nanoparticles using mixed self-assembled monolayers

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Title
Enhanced immobilization of hexa-arginine-tagged esterase on gold nanoparticles using mixed self-assembled monolayers
Author(s)
Jin Young JeongChang-Soo Lee; Sang Jeon Chung; Bong Hyun Chung
Bibliographic Citation
Bioprocess and Biosystems Engineering, vol. 33, no. 1, pp. 165-169
Publication Year
2010
Abstract
Mixed self-assembled monolayers (MSAMs) composed of diverse ligands offer a mechanism for the specific binding of biomolecules onto solid surfaces. In this study, we examined the formation of MSAMs on gold nanoparticles (AuNPs) and the immobilization of hexa-arginine-tagged esterase (Arg6-esterase) on the surfaces of the resulting particles. The functionalization of AuNPs with MSAMs was achieved by introducing a mixture of tethering and shielding ligands into an AuNP solution. The formation of self-assembled monolayers (SAMs) on the AuNP surface was characterized by UV/visible spectroscopy, transmission electron microscopy, and Fourier-transform infrared spectroscopy. Arg 6-esterase was immobilized in a highly specific manner onto AuNPs treated with mixed SAMs (MSAM-AuNPs) by providing a shielding ligand which reduce the non-specific adsorption of enzymes caused by hydrophobic interaction compared to AuNPs treated with single-component SAMs (SSAM-AuNPs). Moreover, Arg6-esterase immobilized on MSAM-AuNPs showed substantially enhanced catalytic activity up to an original activity compared to that on SSAM-AuNPs (58%).
Keyword
Enzyme activityEnzyme immobilizationGold nanoparticlesMixed self-assembled monolayer
ISSN
1615-7591
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s00449-009-0353-6
Type
Article
Appears in Collections:
Division of Research on National Challenges > Environmental diseases research center > 1. Journal Articles
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
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