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Properties of Thermus aquaticus β‐NADH oxidase immobilised on various supports
Author(s) -
Sanjust Enrico,
Curreli Nicoletta,
Rescigno Antonio,
Bannister Joe V.,
Cocco Dina
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201581
Subject(s) - thermus aquaticus , enzyme , thermus , chemistry , covalent bond , biochemistry , oxidase test , chromatography , organic chemistry , thermophile
β‐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.