NDLI: Microscale process evaluation of recombinant biocatalyst libraries: application to Baeyer–Villiger monooxygenase catalysed lactone synthesis

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Microscale process evaluation of recombinant biocatalyst libraries: application to Baeyer–Villiger monooxygenase catalysed lactone synthesis

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Microscale process evaluation of recombinant biocatalyst libraries: application to Baeyer–Villiger monooxygenase catalysed lactone synthesis

Content Provider	Springer Nature Link
Author	Ferreira Torres, C. Micheletti, M. Lye, G. J.
Copyright Year	2005
Abstract	Microscale processing techniques are rapidly emerging as a cost- effective means for parallel experimentation and hence the evaluation of large libraries of recombinant biocatalysts. In this work, the potential of an automated microscale process is demonstrated in a linked sequence of operations comprising fermentation, enzyme induction and bioconversion using three whole-cell biocatalysts each expressing cyclohexanone monoxygenase (CHMO). The biocatalysts, Escherichia coli TOP 10 [pQR239], E. coli JM107 and Acinetobacter calcoaceticus NCIMB 9871, were first produced in 96-deep square well fermentations at various carbon source concentrations (10 and 20 g L−1 glycerol). Following induction of CHMO activity biomass concentrations of up to 6 gDCW L−1 were obtained. Cells from each fermentation were subsequently used for the Baeyer–Villiger oxidation of bicyclo[3.2.0]hept-2-en-6-one, cyclohexanone and cyclopentanone. Each bioconversion was performed at two initial substrate concentrations (0.5 and 1.0 g L−1) in order to simultaneously explore both substrate specificity and inhibition. The microscale process sequences yielded quantitative and reproducible data for each biocatalyst on maximum growth rate, biomass yield, initial rate of lactone formation, specific biocatalyst activity and bioconversion yield. E. coli TOP 10 [pQR239] was demonstrated to be an efficient biocatalyst showing substrate specificities and substrate inhibition effects in line with previous studies. Finally, in order to show that the data obtained with E. coli TOP 10 [pQR239] at microwell scale (1,000 μL) could be related to larger scales of operation, the process was performed in a 2-L stirred-tank bioreactor. Using conditions designed to enable microwell kinetic measurements under none oxygen-limited conditions, the fermentation and bioconversion data obtained at the two scales showed good quantitative agreement. This study therefore confirms the potential of automated microscale experimentation for the whole-process evaluation of recombinant biocatalyst libraries and the specification of pilot and process scale operating conditions.
Starting Page	83
Ending Page	93
Page Count	11
File Format	PDF
ISSN	16157591
Journal	Bioprocess Engineering
Volume Number	28
Issue Number	2
e-ISSN	16157605
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-10-06
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Microscale processing E. coli bioconversion Cyclohexanone monoxygenase Baeyer–Villiger monoxygenase Food Science Waste Water Technology / Water Pollution Control / Water Management / Aquatic Pollution Waste Management/Waste Technology Industrial and Production Engineering Industrial Chemistry/Chemical Engineering Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Biotechnology

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Simultaneous biocatalyst production and baeyer-villiger oxidation for bioonversion of cyclohexanone by recombinant Escherichia coli expressing cyclohexanone monooxygenase

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Microscale process evaluation of recombinant biocatalyst libraries: application to Baeyer–Villiger monooxygenase catalysed lactone synthesis

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