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Purification and characterization of a novel alcohol oxidase from Paenibacillus sp. AIU 311

Paper ID Volume ID Publish Year Pages File Format Full-Text
22197 43260 2007 5 PDF Available
Title
Purification and characterization of a novel alcohol oxidase from Paenibacillus sp. AIU 311
Abstract

An oxidase catalyzing the conversion of glycolaldehyde to glyoxal was purified to the homogeneous state from Paenibacillus sp. AIU 311, and its properties were revealed. This enzyme was specific to glycolaldehyde and glyceraldehyde, and the reaction rates to other alcohols and aldehydes were less than 6% of that of glycolaldehyde. The Km values for glycolaldehyde and glyceraldehyde were estimated to be 13.2 and 7.5 mM, respectively. The glycolaldehyde oxidation was optimum at pH 6.5 and 50°C. The molecular mass of this enzyme was 49 kDa, and it consisted of two identical subunits of 24 kDa. The NH2-terminal sequence was not homologous to those of alcohol oxidases. This is the first report of an oxidase exhibiting high specificity to a hydroxy group of aldehyde alcohols.

Keywords
glycolaldehyde; glyceraldehyde; alcohol oxidase; Paenibacillus sp.
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Purification and characterization of a novel alcohol oxidase from Paenibacillus sp. AIU 311
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 104, Issue 2, August 2007, Pages 124–128
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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