Properties of Thermus aquaticus b-NADH oxidase immobilised on various supports

SANJUST, ENRICO;CURRELI, NICOLETTA;RESCIGNO, ANTONIO;
1997-01-01

Abstract

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.
1997
Inglese
41
3
555
562
8
WOS:A1997WQ34800014
2-s2.0-0030957510
9090463
Esperti anonimi
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.
internazionale
scientifica
no
Sanjust, Enrico; Curreli, Nicoletta; Rescigno, Antonio; Bannister, Jv; Cocco, D.
1.1 Articolo in rivista
info:eu-repo/semantics/article
1 Contributo su Rivista::1.1 Articolo in rivista
262
5
reserved
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