Properties of Thermus aquaticus beta-NADH oxidase immobilised on various supports.
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.
Sanjust
E
E
Istituto di Chimica Biologica, Università di Cagliari, Italy.
Curreli
N
N
Rescigno
A
A
Bannister
J V
JV
Cocco
D
D
D001426:Bacterial Proteins / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D013824:Thermus / Q000201:enzymology*
D001426:Bacterial Proteins; D009097:Multienzyme Complexes; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases