PubMed · 12741784
Enzyme-containing Michael-adduct-based coatings.
Abstract
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.
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Géraldine F Drevon, Claus Urbanke, Alan J Russell. Enzyme-containing Michael-adduct-based coatings.. https://doi.org/10.1021/bm034034l
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