High-activity enzyme-polyurethane coatings

• Published in: Biotechnology and bioengineering 2002-09, Vol.79 (7), p.785-794
• Main Authors: Drevon, Géraldine F., Danielmeier, Karsten, Federspiel, William, Stolz, Donna B., Wicks, Douglas A., Yu, Poli C., Russell, Alan J.
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; bioplastic; Biotechnology; Coated Materials, Biocompatible - chemical synthesis; coating; DFPase; Diffusion; Enzyme Activation; Enzyme Stability; Enzymes, Immobilized - chemistry; Esterases - chemistry; Fundamental and applied biological sciences. Psychology; immobilization; Immobilization of enzymes and other molecules; Immobilization techniques; Methods. Procedures. Technologies; Phosphoric Triester Hydrolases; polyurethane; Polyurethanes - chemistry; Reproducibility of Results; Sensitivity and Specificity; Solubility; Substrate Specificity; Temperature; Water - chemistry
• ISSN: 0006-3592; 1097-0290
• DOI: 10.1002/bit.10334

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. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 79: 785–794, 2002.