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Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813

Paper ID Volume ID Publish Year Pages File Format Full-Text
20991 43201 2012 5 PDF Available
Title
Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813
Abstract

An l-amino acid oxidase was found from a newly isolated strain, Pseudomonas sp. AIU 813. This enzyme was remarkably induced by incubation with l-lysine as a nitrogen source, and efficiently purified using an affinity chromatography with l-lysine as ligand. The enzyme oxidized l-lysine, l-ornithine and l-arginine, but not other l-amino acids and d-amino acids. The oxidase activity for l-lysine was detected in a wide pH range, and its optimal was pH 7.0. In contrast, the oxidase activity for l-ornithine and l-arginine was not shown in acidic region from pH 6.5, and optimal pH for both substrates was 9.0. The enzyme was a flavoprotein and composed of two identical subunits with molecular mass of 54.5 kDa. The N-terminal amino acid sequence was similar to that of putative flavin-containing amine oxidase and putative tryptophan 2-monooxygenase, but not to that of l-amino acid oxidases.

Keywords
l-Amino acid oxidase; l-Lysine; l-Arginine; l-Ornithine; Pseudomonas
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Purification and characterization of an l-amino acid oxidase from Pseudomonas sp. AIU 813
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 114, Issue 3, September 2012, Pages 257–261
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us