| RRC ID |
34049
|
| Author |
Sugawara A, Matsui D, Komeda H, Asano Y, Isobe K.
|
| Title |
Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205.
|
| Journal |
J Biosci Bioeng
|
| 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.
|
| Volume |
117(3)
|
| Pages |
263-8
|
| Published |
2014-3-1
|
| DOI |
10.1016/j.jbiosc.2013.08.019
|
| PII |
S1389-1723(13)00320-4
|
| PMID |
24113361
|
| MeSH |
Amides / metabolism*
Amine Oxidase (Copper-Containing) / isolation & purification
Amine Oxidase (Copper-Containing) / metabolism*
Aspergillus / enzymology*
Hydrogen-Ion Concentration
L-Amino Acid Oxidase / isolation & purification
L-Amino Acid Oxidase / metabolism
Lysine / metabolism
Oxidation-Reduction
Pseudomonas / enzymology
Substrate Specificity
Temperature
|
| IF |
2.366
|
| Times Cited |
4
|
|
WOS Category
|
FOOD SCIENCE & TECHNOLOGY
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
|
| Resource |
| General Microbes |
JCM 5546
JCM 5548
JCM 5697 |
