[Purification and characterization of 2-carbonyl reductase from marine bacteria Bacillus sp].
ANADPH-dependent 2-Oxoaldehyde reductase was isolated and purified from a marine bacteria Bacillus sp. The purification procedure involved ammonium sulfate fractionation and Q Sepharose FF, Hydroxyapatite, Sephadex G-100 column chromatographies. The specific activity of the purified enzyme was increased by 141.1 folds over crude extract and the recovery yield was 11.4%. 2-Oxoaldehyde compounds were found to be speciall good substrates. The optimum pH of the enzyme activity was 6.2-6.6. The Km coefficient for 3-deoxyglucosone was 2.5 mmol/L. The molecular weight of the enzyme was estimated to be 33 kD The enzyme activity is stable below 30 degrees C and pH 5.0-8.0. EDTA, beta-mercaptoethanol and dithiothreitol enhanced the enzyme activity. On the other hand, the enzyme activity was partially lost by idoacetic acid or N-ethylmaleimide.
Li
X
X
Industrial Experimental Centre of GuangXi University, Nanning 530004, China.
Luo
H
H
Pang
Z
Z
Huang
S
S
Liang
Z
Z
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D001407:Bacillus / Q000737:chemistry / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D007700:Kinetics; D012623:Seawater / Q000382:microbiology*
D001426:Bacterial Proteins; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+)