A Polyaniline-Based Optical Biosensing Platform Using an Entrapped Oxidoreductase Enzyme

Louis R. Nemzer; Arthur J. Epstein

doi:10.1016/j.snb.2010.06.054

A Polyaniline-Based Optical Biosensing Platform Using an Entrapped Oxidoreductase Enzyme

Louis R. Nemzer
, Arthur J. Epstein

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

A novel optical biosensing platform utilizing the unique solubility and chemochromic properties of polyaniline is presented. A facile, ion-induced reprecipitation method leads to the entrapment of a chosen oxidoreductase enzyme, which, in the presence of its associated substrate, catalyzes a reversible redox change in the host polymer. This change is monitored via the UV-vis absorption and subsequently analyzed to fit a Michaelis-Menten model. Here, in vitro prototype devices demonstrate selective sensing of glucose, choline, and uric acid, and the potential to be adapted for use as part of real-time in vivo monitoring systems is discussed. © 2010 Published by Elsevier B.V.

Original language	American English
Pages (from-to)	376-383
Number of pages	8
Journal	Sensors and Actuators B: Chemical
Volume	150
Issue number	1
DOIs	https://doi.org/10.1016/j.snb.2010.06.054
State	Published - Sep 21 2010
Externally published	Yes

Funding

The authors would like to express their appreciation to Dr. Nan-Rong Chiou and Dr. Yong Min for their insights and invaluable suggestions. This material is based upon work supported by the National Science Foundation under IGERT Grant No. 0221678 and NSEC Grant No. EEC-0425626 as well as an Ohio State University Institute for Materials Research facilities grant.

Funders	Funder number
NSEC
National Science Foundation	0221678

ASJC Scopus Subject Areas

Electronic, Optical and Magnetic Materials
Instrumentation
Condensed Matter Physics
Surfaces, Coatings and Films
Metals and Alloys
Electrical and Electronic Engineering
Materials Chemistry

Keywords

Gelation
Glucose monitoring
Glucose oxidase
Optical biosensor
Oxidoreductase
Polyaniline

Disciplines

Medicine and Health Sciences
Physical Sciences and Mathematics
Electrical and Computer Engineering
Instrumentation
Materials Science and Engineering
Materials Chemistry
Condensed Matter Physics

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10.1016/j.snb.2010.06.054

Cite this

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AU - Epstein, Arthur J.

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N2 - A novel optical biosensing platform utilizing the unique solubility and chemochromic properties of polyaniline is presented. A facile, ion-induced reprecipitation method leads to the entrapment of a chosen oxidoreductase enzyme, which, in the presence of its associated substrate, catalyzes a reversible redox change in the host polymer. This change is monitored via the UV-vis absorption and subsequently analyzed to fit a Michaelis-Menten model. Here, in vitro prototype devices demonstrate selective sensing of glucose, choline, and uric acid, and the potential to be adapted for use as part of real-time in vivo monitoring systems is discussed. © 2010 Published by Elsevier B.V.

AB - A novel optical biosensing platform utilizing the unique solubility and chemochromic properties of polyaniline is presented. A facile, ion-induced reprecipitation method leads to the entrapment of a chosen oxidoreductase enzyme, which, in the presence of its associated substrate, catalyzes a reversible redox change in the host polymer. This change is monitored via the UV-vis absorption and subsequently analyzed to fit a Michaelis-Menten model. Here, in vitro prototype devices demonstrate selective sensing of glucose, choline, and uric acid, and the potential to be adapted for use as part of real-time in vivo monitoring systems is discussed. © 2010 Published by Elsevier B.V.

KW - Gelation

KW - Glucose monitoring

KW - Glucose oxidase

KW - Optical biosensor

KW - Oxidoreductase

KW - Polyaniline

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DO - 10.1016/j.snb.2010.06.054

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SN - 0925-4005

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JO - Sensors and Actuators B: Chemical

JF - Sensors and Actuators B: Chemical

IS - 1

ER -

A Polyaniline-Based Optical Biosensing Platform Using an Entrapped Oxidoreductase Enzyme

Abstract

Funding

ASJC Scopus Subject Areas

Keywords

Disciplines

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