Journal
JOURNAL OF BIOTECHNOLOGY
Volume 142, Issue 2, Pages 164-169Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2009.04.008
Keywords
Biocatalysis; Baeyer-Villiger oxidation; Corynebacterium glutamicum; Cyclohexanone monooxygenase; epsilon-Caprolactone
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Funding
- Korea Research Foundation, Korean Government [KRF-2008-331-F00064]
- Seoul RBD Program [11000]
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The biocatalytic efficiency of recombinant Corynebacterium glutamicum expressing the chnB gene encoding cyclohexanone monooxygenase (CHMO) of Acinetobacter calcoaceticus NCIMB 9871 was investigated. Optimization of an expression system and induction conditions enabled the recombinant biocatalyst to produce CHMO to a specific activity of ca. 0.5 U mg(-1) protein. Tight control of feeding of an energy source (i.e., glucose) and dissolved oxygen tension during fed-batch culture-based biotransformation allowed the cells to produce epsilon-caprolactone to a concentration of 16.0 gl(-1). The specific and volumetric productivity for cyclohexanone oxidation were 0.12 g g dry cell s(-1)h(-1) (17.5 Ug(-1) of dry cells) and 2.3 gl(-1) h(-1) (330 Ul(-1)), respectively. These values correspond to over 5.4- and 2.7-fold of recombinant Escherichia call expressing the same gene under similar reaction conditions. It could be concluded that the recombinant C. glutamicum is a promising biocatalyst for Baeyer-Villiger oxidations. (C) 2009 Elsevier B.V. All rights reserved.
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