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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Uchida, H., Okamura, Y., Yamanaka, H. et al. Purification and Some Properties of An Aldehyde Oxidase from Streptomyces Rimosus ATCC10970. World J Microbiol Biotechnol 22, 469–474 (2006). https://doi.org/10.1007/s11274-005-9058-4
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DOI: https://doi.org/10.1007/s11274-005-9058-4