Chemistry and Physics Faculty Articles
Title
Enzyme Entrapment in Polyaniline FIlms Observed via Fluorescence Anisotropy and Antiquenching
Document Type
Article
Publication Date
5-10-2014
Publication Title
Modern Physics Letters B
Keywords
Antiquenching, Biosensor, Fluorescence anisotropy, Enzyme immobilization, Oxidoreductase, Polyaniline
ISSN
0217-9849
Volume
28
Issue/No.
11
First Page
1
Last Page
12
Abstract
The facile entrapment of oxidoreductase enzymes within polyaniline polymer films by inducing hydrophobic collapse using phosphate buffered saline (PBS) has been shown to be a cost-effective method for fabricating organic biosensors. Here, we use fluorescence anisotropy measurements to verify enzyme immobilization and subsequent electron donation to the polymer matrix, both prerequisites for an effective biosensor. Specifically, we measure a three order of magnitude decrease in the ratio of the fluorescence to rotational lifetimes. In addition, the observed fluorescence antiquenching supports the previously proposed model that the polymer chain assumes a severely coiled conformation when exposed to PBS. These results help to empirically reinforce the theoretical basis previously laid out for this biosensing platform.
NSUWorks Citation
Nemzer, L. R., McCaffrey, M., & Epstein, A. J. (2014). Enzyme Entrapment in Polyaniline FIlms Observed via Fluorescence Anisotropy and Antiquenching. Modern Physics Letters B, 28, (11), 1 - 12. https://doi.org/10.1142/S021798491430004X. Retrieved from https://nsuworks.nova.edu/cnso_chemphys_facarticles/90
DOI
10.1142/S021798491430004X
