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J Biosci Bioeng. 2014 Mar;117(3):263-8. doi: 10.1016/j.jbiosc.2013.08.019. Epub 2013 Oct 7.

Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205.

Author information

1
Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan.
2
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
3
Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan. Electronic address: kiso@iwate-u.ac.jp.

Abstract

We isolated Aspergillus carbonarius AIU 205 as a new producer of an enzyme catalyzing oxidative deamination of 4-aminobutanamide (4-ABAD) to 4-oxobutanamide with the subsequent release of ammonia and hydrogen peroxide. Since the strain produced three enzymes with different Km values for 4-ABAD, the enzyme with lowest Km value (0.31 mM) was purified and revealed certain remarkable properties. The enzyme also oxidized aliphatic monoamines, aromatic amines and aliphatic aminoalcohols, but did not oxidize l-amino acids and aliphatic diamines. The Vmax/Km values for aliphatic monoamines were higher than that for 4-ABAD, and the enzyme activity was strongly inhibited by inhibitors of copper-containing amine oxidases. Thus, it was concluded that the enzyme might belong to a group of copper-containing amine oxidase. The 4-ABAD oxidase activity of this enzyme was optimum at pH 7.0, and the enzyme activity at pH 6.0 was 65% of that at pH 7.0. The enzyme was useful for increasing the sensitivity of l-lysine assay using l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813.

KEYWORDS:

4-Aminobutanamide; Amine oxidase; Aminoamide; Aspergillus carbonarius; l-Amino acid oxidase/oxygenase; l-Lysine; l-Ornithine

PMID:
24113361
DOI:
10.1016/j.jbiosc.2013.08.019
[Indexed for MEDLINE]
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