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Productivity of cyclohexanone oxidation of the recombinant Corynebacterium glutamicum expressing chnB of Acinetobacter calcoaceticus

Title
Productivity of cyclohexanone oxidation of the recombinant Corynebacterium glutamicum expressing chnB of Acinetobacter calcoaceticus
Authors
Doo E.-H.Lee W.-H.Seo H.-S.Seo J.-H.Park J.-B.
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2009
Journal Title
Journal of Biotechnology
ISSN
0168-1656JCR Link
Citation
vol. 142, no. 2, pp. 164 - 169
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
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 ε-caprolactone to a concentration of 16.0 g l-1. The specific and volumetric productivity for cyclohexanone oxidation were 0.12 g g dry cells-1 h-1 (17.5 U g-1 of dry cells) and 2.3 g l-1 h-1 (330 U l-1), respectively. These values correspond to over 5.4- and 2.7-fold of recombinant Escherichia coli 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. © 2009 Elsevier B.V. All rights reserved.
DOI
10.1016/j.jbiotec.2009.04.008
Appears in Collections:
엘텍공과대학 > 식품공학전공 > Journal papers
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