Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis.
A new NADH oxidase, useful for the regeneration of NAD+, was isolated and characterized from Lactobacillus brevis. In crude extracts the activity was from 10-15 U mg(-1). After purification by four chromatographic steps, an activity of 116 U mg(-1) was obtained with 14% yield. Highest activity was from pH 5.5-7 and at 40 degrees C. The enzyme requires dithiothreitol to prevent oxidative deactivation. The Km value for NADH was 24 microM.
Hummel
Werner
W
Institut für Enzymtechnologie der Heinrich-Heine-Universität, Forschungszentrum Jülich, Wilhelm-Johnen-Str., D-52426 Jülich, Germany. w.hummel@fz-juelich.de
Riebel
Bettina
B
D004149:Dioxoles; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007778:Lactobacillus / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D009097:Multienzyme Complexes / Q000096:biosynthesis / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D009247:NADH, NADPH Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D011786:Quality Control; D013045:Species Specificity; D013696:Temperature
D004149:Dioxoles; D009097:Multienzyme Complexes; C403865:stresgenin B; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases