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Original Articles

Purification and Characterization of Cyclohexanone 1,2-Monooxygenase from Exophiala jeanselmei strain KUFI-6N

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Pages 2696-2698 | Received 29 May 2000, Accepted 09 Aug 2000, Published online: 22 May 2014
 

Abstract

Baeyer-Villiger cyclohexanone 1,2-monooxygenase (CHMO) was purified 17.1-fold from cell extracts of the fungus Exophiala jeanselmei grown on cyclohexanol to electrophoretically homogeneity by serial chromatographies. The molecular mass of the native enzyme was approximately 74 kDa by gel filtration and SDS-PAGE. Some enzymic characterizations were studied. The NH2-terminal amino acid residues were Ala-Lys-Ser-Leu-Asp-Val-Leu-Ile-Val-Gly-Ala-Gly-Phe-Gly-Gly-Ile-Tyr-Gln-Leu-, with similarity to the bacterial CHMOs of FAD-binding and NADPH-dependent type Baeyer- Villiger monooxygenases.

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