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High‐activity enzyme‐polyurethane coatings
Author(s) -
Drevon Géraldine F.,
Danielmeier Karsten,
Federspiel William,
Stolz Donna B.,
Wicks Douglas A.,
Yu Poli C.,
Russell Alan J.
Publication year - 2002
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10334
Subject(s) - polyurethane , chemistry , coating , polymerization , hydrolysis , enzyme , chemical engineering , kinetics , enzyme assay , immobilized enzyme , homogeneous , polymer chemistry , matrix (chemical analysis) , chromatography , organic chemistry , polymer , physics , quantum mechanics , engineering , thermodynamics
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.