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. 2021 Mar 10;26(6):1514.
doi: 10.3390/molecules26061514.

Production of Enantiopure Chiral Epoxides with E. coli Expressing Styrene Monooxygenase

Dominika Gyuranová  1 , Radka Štadániová  2 , Zuzana Hegyi  1 , Róbert Fischer  2 , Martin Rebroš  1
Affiliations

Production of Enantiopure Chiral Epoxides with E. coli Expressing Styrene Monooxygenase

Dominika Gyuranová et al. Molecules. .

Abstract

Styrene monooxygenases are a group of highly selective enzymes able to catalyse the epoxidation of alkenes to corresponding chiral epoxides in excellent enantiopurity. Chiral compounds containing oxirane ring or products of their hydrolysis represent key building blocks and precursors in organic synthesis in the pharmaceutical industry, and many of them are produced on an industrial scale. Two-component recombinant styrene monooxygenase (SMO) from Marinobacterium litorale was expressed as a fused protein (StyAL2StyB) in Escherichia coli BL21(DE3). By high cell density fermentation, 35 gDCW/L of biomass with overexpressed SMO was produced. SMO exhibited excellent stability, broad substrate specificity, and enantioselectivity, as it remained active for months and converted a group of alkenes to corresponding chiral epoxides in high enantiomeric excess (˃95-99% ee). Optically pure (S)-4-chlorostyrene oxide, (S)-allylbenzene oxide, (2R,5R)-1,2:5,6-diepoxyhexane, 2-(3-bromopropyl)oxirane, and (S)-4-(oxiran-2-yl)butan-1-ol were prepared by whole-cell SMO.

Keywords: chiral epoxides; styrene monooxygenase; whole-cell biocatalysis.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
HCD batch fermentation of E. coli expressing SMO performed on the 1.5 L scale.
Figure 2
Figure 2
Biocatalytic cascade of styrene epoxidation involving GDH cofactor regeneration system.
Figure 3
Figure 3
pH (a) and temperature (b) profile of purified SMO.
See this image and copyright information in PMC

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