Géraldine F. Drevon

Irreversible immobilization of diisopropylfluorophophatase into polyurethane coatings

The synthesis of polyurethane polymers in the presence of diisopropylfluorophosphatase (DFPase) has enabled the irreversible attachment of the enzyme to the polymeric matrix. The resulting bioplastic hydrolyzes diisopropylfluorophosphate (DFP) in buffered media up to 67% of the rate for the same amount of soluble enzyme. Above a DFPase concentration of approximately 0.1 mg/gfoam, the rate of the reaction catalyzed by the enzyme-containing polymer was controlled by internal mass transfer. Increasing foam hydrophilicity, via the use of nonionic surfactants during polymerization, significantly affected the structural properties of matrix, thereby enhancing the intrinsic and apparent efficiency of modified DFPase. The resulting reduction in internal mass transfer limitations was explained morphologically with electron microscopy.

Preparation of methylcyclopentane-1-d1

The title compound has been prepared in 70% yield by the reaction between 1-chloro-1-methylcyclopentane and deuterotributylstannane, without solvent. Small amounts (0.7–3.5%) of unreacted starting material remained after the reaction and were removed by solvolytic HCl elimination with water or aqueous sodium hydroxide, followed by oxidation with potassium permanganate or bromine addition at low temperature, which form products of low volatility. Small amounts of a by-product, deuterobutane, resulting from the cleavage of the carbon-tin bond in the reactant were also observed in the product. Copyright