High-activity enzyme-polyurethane coatings.
The synthesis of water-borne polyurethane coatings in the presence of diisopropylfluorophosphatase (DFPase, E.C. 3.8.2.1) enabled the irreversible attachment of the enzyme to the polymeric matrix. The distribution of immobilized DFPase as well as activity retention are homogeneous within the coating. The resulting enzyme-containing coating (ECC) film hydrolyzes diisopropylfluorophosphate (DFP) in buffered media at high rates, retaining approximately 39% intrinsic activity. Decreasing ECC hydrophilicity, via the use of a less hydrophilic polyisocyanate during polymerization, significantly enhanced the intrinsic activity of the ECC. DFPase-ECC has biphasic deactivation kinetics, where the initial rapid deactivation of DFPase-ECC leads to the formation of a hyperstable and active form of enzyme.
Drevon
Géraldine F
GF
Department of Chemical and Petroleum Engineering, University of Pittsburgh, 1249 Benedum Hall, Pennsylvania 15261, USA.
Danielmeier
Karsten
K
Federspiel
William
W
Stolz
Donna B
DB
Wicks
Douglas A
DA
Yu
Poli C
PC
Russell
Alan J
AJ
D020099:Coated Materials, Biocompatible / Q000138:chemical synthesis*; D004058:Diffusion; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004950:Esterases / Q000737:chemistry*; D044345:Phosphoric Triester Hydrolases; D011140:Polyurethanes / Q000737:chemistry*; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D012995:Solubility; D013379:Substrate Specificity; D013696:Temperature; D014867:Water / Q000737:chemistry
D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D011140:Polyurethanes; D014867:Water; D004950:Esterases; D044345:Phosphoric Triester Hydrolases; C020061:diisopropyl-fluorophosphatase