Abstract
A putative carotenoid oxygenase from Novosphingobium aromaticivorans was purified with a specific activity of 0.8 U/mg by His-Trap affinity chromatography. The native enzyme was estimated to be a 52 kDa monomer. Enzyme activity for β-apo-8′-carotenal was maximal at pH 8.0 and 45 °C, with a half life of 15.3 h, K m of 21 μM, and k cat of 25 l/min. The enzyme exhibited cleavage activity only for carotenoids containing one β-ionone ring and its catalytic efficiency (k cat/K m) followed the order β-apo-8′-carotenal > β-apo-4′-carotenal > γ-carotene. The enzyme converted these carotenoids to β-apo-13-carotenones by cleaving their C13–C14 double bonds. The oxygen atom of β-apo-13-carotenone originated not from water but from molecular oxygen. Thus, the enzyme was an apo-carotenoid 13,14-dioxygenase.
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This study was supported by a grant (2009-0084490) from the Basic Research Program, Ministry of Education, Science and Technology.
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Kim, YS., Seo, ES. & Oh, DK. Characterization of an apo-carotenoid 13,14-dioxygenase from Novosphingobium aromaticivorans that converts β-apo-8′-carotenal to β-apo-13-carotenone. Biotechnol Lett 34, 1851–1856 (2012). https://doi.org/10.1007/s10529-012-0969-5
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DOI: https://doi.org/10.1007/s10529-012-0969-5