Characterization and potential application of purified aldehyde oxidase from Pseudomonas stutzeri IFO12695.
The molecular weight of purified aldehyde oxidase from Pseudomonas stutzeri IFO12695 was estimated to be 160 kDa by a gel filtration method. SDS-PAGE showed that the enzyme consisted of three non-identical subunits with molecular weights of 18, 38, and 83 kDa. The enzyme exhibited an absorption spectrum with maxima at 277, 325, 365, 415, 450, 480, and 550 nm and possessed molybdenum, CMP, iron, sulfur, and FAD as its cofactors, indicating that it belonged to the xanthine oxidase family. A variety of aliphatic and aromatic aldehydes were oxidized; and among them n-hexylaldehyde gave the most rapidly action. When 10 mM formaldehyde was treated with the aldehyde oxidase in the presence of catalase for 240 min, the formaldehyde concentration was reduced to 0.8 mM, suggesting this enzyme might be effective for the removal of formaldehyde contained in wastewater.
Uchida
H
H
Department of Applied Chemistry and Biotechnology, Faculty of Engineering, University of Fukui, 9-1, Bunkyo 3-Chome, Fukui-shi, 910-8507, Japan.
Fukuda
T
T
Satoh
Y
Y
Okamura
Y
Y
Toriyama
A
A
Yamashita
A
A
Aisaka
K
K
Sakurai
T
T
Nagaosa
Y
Y
Uwajima
T
T
D042931:Aldehyde Oxidase / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D044223:Pseudomonas stutzeri / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D042931:Aldehyde Oxidase