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

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 epsilon-caprolactone to a concentration of 16.0 g l(-1). The specific and volumetric productivity for cyclohexanone oxidation were 0.12 g g drycells(-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.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Doo EH,Lee WH,Seo HS,Seo JH,Park JB

doi

10.1016/j.jbiotec.2009.04.008

subject

Has Abstract

pub_date

2009-06-15 00:00:00

pages

164-9

issue

2

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(09)00178-3

journal_volume

142

pub_type

杂志文章

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