Oxidase-functionalized Fe(3)O(4) nanoparticles for fluorescence sensing of specific substrate.
Cheng-Hao Liu, Wei-Lung Tseng
Index: Anal. Chim. Acta 703(1) , 87-93, (2011)
Full Text: HTML
Abstract
This study reports the development of a reusable, single-step system for the detection of specific substrates using oxidase-functionalized Fe(3)O(4) nanoparticles (NPs) as a bienzyme system and using amplex ultrared (AU) as a fluorogenic substrate. In the presence of H(2)O(2), the reaction pH between Fe(3)O(4) NPs and AU was similar to the reaction of oxidase and the substrate. The catalytic activity of Fe(3)O(4) NPs with AU was nearly unchanged following modification with poly(diallyldimethylammonium chloride) (PDDA). Based on these features, we prepared a composite of PDDA-modified Fe(3)O(4) NPs and oxidase for the quantification of specific substrates through the H(2)O(2)-mediated oxidation of AU. By monitoring fluorescence intensity at 587 nm of oxidized AU, the minimum detectable concentrations of glucose, galactose, and choline were found to be 3, 2, and 20 μM using glucose oxidase-Fe(3)O(4), galactose oxidase-Fe(3)O(4), and choline oxidase-Fe(3)O(4) composites, respectively. The identification of glucose in blood was selected as the model to validate the applicability of this proposed method.Copyright © 2011 Elsevier B.V. All rights reserved.
Related Compounds
Related Articles:
2012-08-13
[Biomacromolecules 13(8) , 2418-28, (2012)]
Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans.
2013-02-01
[Glycobiology 23(2) , 211-21, (2013)]
In vivo enzyme immobilization by inclusion body display.
2010-08-01
[Appl. Environ. Microbiol. 76(16) , 5563-9, (2010)]
2013-01-01
[PLoS ONE 8(1) , e54112, (2013)]
Live diatom silica immobilization of multimeric and redox-active enzymes.
2012-01-01
[Appl. Environ. Microbiol. 78(1) , 211-8, (2012)]