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