Enzyme-containing Michael-adduct-based coatings.
A two-step method was developed to homogeneously insert carbonic anhydrase (CA, E.C. 4.2.1.1) into Michael-adduct-based coatings. CA was first covalently coupled to an N-vinylformamide-based water-soluble polymer. Unlike native CA, the resulting polymer/CA system could be dispersed within a film matrix. The enzyme-containing coating (ECC) hydrolyzes p-nitrophenyl propionate in buffered media at high rates retaining approximately 7% apparent activity. In comparison, other two-step techniques for the chemical coupling of CA to the coating surface were less efficient and led to coatings with significantly less activity. A three-step immobilization process coupling the enzyme to the surface of a partially hydrolyzed coating also raised retention of activity after coating synthesis. CA-ECC is stable under ambient conditions retaining 45% activity after 90 days of storage at room temperature.
Department of Chemical and Petroleum Engineering, University of Pittsburgh, 1249 Benedum Hall, Pittsburgh, Pennsylvania 15261, USA.
Géraldine F
GF
Drevon
Claus
C
Urbanke
Alan J
AJ
Russell
D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D020099:Coated Materials, Biocompatible / Q000737:chemistry* / Q000378:metabolism; D018736:DNA Adducts / Q000138:chemical synthesis; D004355:Drug Stability; D006358:Hot Temperature; D009496:Neurotensin / Q000737:chemistry; D013499:Surface Properties
D020099:Coated Materials, Biocompatible; D018736:DNA Adducts; D009496:Neurotensin; D002256:Carbonic Anhydrases