Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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We isolated Aspergillus carbonarius MU 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 K_m values for 4-ABAD, the enzyme with lowest K_m 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 V_<max>/K_m 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 wddase/monooxygenase from Pseudomonas sp. MU 813.
著者
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Isobe Kimiyasu
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Asano Yasuhisa
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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Komeda Hidenobu
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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Sugawara Asami
Department Of Biological Chemistry And Food Science Faculty Of Agriculture Iwate University
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Matsui Daisuke
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
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