Electrostatic immobilization of glucose oxidase in a weak acid, polyelectrolyte hyperbranched ultrathin film on gold: Fabrication, characterization, and enzymatic activity

Citation
Jg. Franchina et al., Electrostatic immobilization of glucose oxidase in a weak acid, polyelectrolyte hyperbranched ultrathin film on gold: Fabrication, characterization, and enzymatic activity, ANALYT CHEM, 71(15), 1999, pp. 3133-3139
Citations number
63
Categorie Soggetti
Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences
Journal title
ANALYTICAL CHEMISTRY
ISSN journal
00032700 → ACNP
Volume
71
Issue
15
Year of publication
1999
Pages
3133 - 3139
Database
ISI
SICI code
0003-2700(19990801)71:15<3133:EIOGOI>2.0.ZU;2-5
Abstract
In this paper we show that hyperbranched polymers can be used as a host mat rix for electrostatic entrapment of enzymes, Specifically, amine-functional ized glucose oxidase (GOx(+)) and horseradish peroxidase, as well as poly(a midoamine) dendrimer-modified horseradish peroxidase, reversibly sorb into polyanionic, hyperbranched poly(sodium acrylate) (PAA(-)) films that are on the order of a few hundred angstroms thick. The quantity of GOx(+) entrapp ed within the PAA(-) films depends on the nature of film preparation but is typically on the order of 0.06 unit/cm(2). The extent to which entrapped G Ox(+) retains its activity depends on the film history, but for PAA(-)/GOx( +) composites not exposed to glucose and stored at 4 degrees C, the origina l activity is retained for up to 68 days and perhaps longer.