alexa Purification and Some Properties of An Aldehyde Oxidase from Streptomyces Rimosus ATCC10970


Fermentation Technology

Author(s): Hiroyuki Uchida, Yoshimasa Okamura, Hiroki Yamanaka, Tetsuya Fukuda

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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.

This article was published in World Journal of Microbiology and Biotechnology and referenced in Fermentation Technology

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