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

Paper ID Volume ID Publish Year Pages File Format Full-Text
24589 43528 2009 6 PDF Available
Title
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 ɛ-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.

Keywords
Biocatalysis; Baeyer–Villiger oxidation; Corynebacterium glutamicum; Cyclohexanone monooxygenase; ɛ-Caprolactone
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Productivity of cyclohexanone oxidation of the recombinant Corynebacterium glutamicum expressing chnB of Acinetobacter calcoaceticus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 142, Issue 2, 15 June 2009, Pages 164–169
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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