beta-NADH oxidase purified from Thermus aquaticus was covalently immobilised on various solid supports. The preparations obtained were compared with the soluble enzyme for activity and kinetic properties. Activated glutaryl-PVA was found to be the best support. The immobilised enzyme was less stable at high temperatures than the soluble enzyme. No differences could be detected in the presence of organic solvents.
|Titolo:||Properties of Thermus aquaticus b-NADH oxidase immobilised on various supports|
|Data di pubblicazione:||1997|
|Tipologia:||1.1 Articolo in rivista|
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|Sanjust et al 1997 Properties of Thermus aquaticus ?-NADH oxidase immobilised on various supports.pdf||Editoriale||Non specificato||Administrator Richiedi una copia|