Characterization of a novel L-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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An enzyme exhibiting oxidase activity for β-lactoglobulin, myoglobin, and L-lysine-containing peptides was found from a newly isolated fungal strain, Penicillium steckii AIU 027. The enzyme also oxidized L-amino acids, N^α-benzyloxycarbonyl-L-lysine (N^α-Z-L-lysine) and N^ε-Z-L-lysine, but not D-amino acids and amines. Thus, the enzyme was classified into a group of L-amino acid oxidases (L-AAOs). However, characteristics of this L-AAO were significantly different from those of other L-AAOs as follows. The L-AAO from P. steckii AIU 027 oxidized both the α-amino group and the ε-amino group in L-amino acids and L-lysine-containing peptides, and the K_m values for L-lysine-containing polypeptides were lower than those for N^α-Z-L-lysine and L-lysine-containing dipeptides. The enzyme contained flavin and iron, and composed of four identical subunits with molecular mass of 75.3 kDa. The N-terminal amino acid sequence, ENIADVADAMGPWFDGVAYMKSKKN, was different from that of other L-AAOs. Thus, the L-AAO with protein oxidase activity was first reported here from P. steckii AIU 027.
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