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Purification and characterization of a new aldehyde oxidase from pseudomonas sp. AIU 362
Yasutaka Sasaki1, Kimiyasu Isobe, Michihiko Kataoka
1The United Graduate School of Agricultural Sciences, Iwate University, 18-8 Ueda 3- chome, Morioka 020-8550, Japan.
Abstract:
An aldehyde oxidase exhibiting high activity on glyoxal was purified to an electrophoretically homogenous state from Pseudomonas sp. AIU 362, which was isolated from a soil sample using a methoxyethanol medium. The enzyme oxidized not only glyoxal but also short-chain aliphatic aldehydes and aromatic aldehydes. Thus, this enzyme was classified into the aldehyde oxidase (ALOD) group. However, it was composed of four identical subunits with a molecular mass of 27 kDa, whereas other microbial ALODs were composed of three hetero subunits, and ALODs from plant and animals were composed of two identical subunits. The NH(2)-terminal sequence also showed no similarity to that of other ALODs. These results indicate that ALOD from Pseudomonas sp. AIU 362 is a new aldehyde oxidase. This ALOD was induced by 2-methoxyethanol, methanol or isopropanol.
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