Purification and Some Properties of An Aldehyde Oxidase from
Streptomyces Rimosus ATCC10970 |
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Authors: | Hiroyuki Uchida Yoshimasa Okamura Hiroki Yamanaka Tetsuya Fukuda Sachie Haneda Kazuo Aisaka Yutaka Fujii |
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Institution: | (1) Department of Applied Chemistry and Biotechnology, Faculty of Engineering, University of Fukui, 9-1, Bunkyo 3-Chome, 910-8507 Fukui-shi, Japan;(2) Tokyo Research Laboratories, Kyowa Hakko Co., Ltd., 3-6-6, Asahi-cho, Machida-shi, 194-0021 Tokyo, Japan;(3) Department of Molecular Life Chemistry, Fukui Medical College, University of Fukui, 9-1, Matsuoka-cho, 910-1193 Fukui, Japan |
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Abstract: | Summary An aldehyde oxidase was purified from a cell-free extract of Streptomyces rimosus ATCC10970 to an electrophoretically homogeneous state. The molecular mass of the native enzyme was estimated to be 150 kDa
by a gel filtration. SDS-polyacryamide gel electrophoresis showed that the enzyme consisted of three non-identical subunits
with molecular masses of 79, 39 and 23 kDa. The absorption spectrum revealed a distinctive feature as an enzyme belonging
to the xanthine oxidase family with maxima at 277, 325, 365, 415, 450, 480, and 550 nm. A variety of aliphatic and aromatic
aldehydes were oxidized, but nitrogen-containing heterocyclic compounds were not. Among the substrates tested, n-heptanal was most rapidly acted on. Its optimum pH and temperature were pH 7.0 and 30 °C, respectively. |
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Keywords: | Aldehyde oxidase N-terminal amino acid sequence purification Streptomyces rimosus ATCC10970 subunit structure xanthine oxidase family |
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