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Purification and characterization of a new aldehyde oxidase from pseudomonas sp. AIU 362

Paper ID Volume ID Publish Year Pages File Format Full-Text
22303 43267 2008 6 PDF Available
Title
Purification and characterization of a new aldehyde oxidase from pseudomonas sp. AIU 362
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 NH2-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.

Keywords
aldehyde oxidase; glyoxal; methoxyethanol
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Purification and characterization of a new aldehyde oxidase from pseudomonas sp. AIU 362
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 3, September 2008, Pages 297–302
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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