ISSN:
1432-072X
Keywords:
Key words NADH oxidase
;
Membrane
;
Alkaliphile
;
Halophile
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A membrane-bound NADH oxidase of an anaerobic alkaliphile, M-12 (a strain of Amphibacillus sp.), was solubilized with decanoyl N-methylglucamide and purified by chromatography on DEAE-Sepharose and hydroxyapatite. The purified enzyme appears to consist of a single polypeptide component with an apparent molecular mass of 56 kDa. The enzyme catalyzed the oxidation of NADH with the formation of H2O2 and exhibited a specific activity of 46 μmol NADH min–1 (mg protein)–1. NADPH did not serve as a substrate for the enzyme. The K m for NADH was estimated to be 0.05 mM. The enzyme exhibited a pH dependence for activity, with a pH optimum at approximately 9.5. The enzyme required a high concentration of salt and exhibited maximum activity in the presence of 600 mM NaCl.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050705
