Enhanced stability of urease immobilized onto phospholipid covalently bound to silica, tungsten, and fluoropolymer surfaces
Exceptionally high stability of urease covalently immobilized on silica, tungsten and poly-(tetrafluoroethylene) (Teflon) supports has been observed by using a novel immobilization protocol that links the enzyme via its surface-exposed carboxylic groups to phospholipid-coated surfaces. It was found...
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Veröffentlicht in: | Analytical chemistry (Washington) 1993-09, Vol.65 (18), p.2459-2467 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Exceptionally high stability of urease covalently immobilized on silica, tungsten and poly-(tetrafluoroethylene) (Teflon) supports has been observed by using a novel immobilization protocol that links the enzyme via its surface-exposed carboxylic groups to phospholipid-coated surfaces. It was found that urease bound to lipid-coated silica or Teflon could be boiled in aqueous solution for one hour with minimal loss of activity. |
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ISSN: | 0003-2700 1520-6882 |
DOI: | 10.1021/ac00066a010 |