Biocatalysts convert styrene into valuable epoxides with high selectivity

The discovery is part of the Micon research training group, focusing on microbial substrate conversion. The enzymes belong to the glutathione S-transferase (GST) family and were shown to favour the conversion of specific enantiomers of aromatic epoxides. This high enantioselectivity is especially relevant for the production of active pharmaceutical ingredients, where stereochemistry can determine biological function.

Tailor-made enzymes enable enantioselective epoxide synthesis

The newly characterised GST-type enzymes catalyse the transformation of styrene into epoxides with remarkable regio- and stereoselectivity. The research team demonstrated that these enzymes are capable of selectively enriching one enantiomer in a racemic mixture by catalysing the degradation of the undesired mirror-image form.

This approach enables the efficient production of optically pure epoxides—key intermediates in polymer synthesis, agrochemicals, and pharmaceuticals. Structural analyses, supported by protein crystallography, confirmed the molecular basis of the enantioselective activity.

Nature-inspired catalysis opens new paths for pharmaceutical production

The biological reaction mimics natural detoxification pathways of epoxides in the human body. By leveraging these systems, the researchers are tapping into nature’s catalytic toolkit to design green and efficient synthesis routes. The enzymes were isolated from microbial degradation pathways of styrene, a known environmental pollutant, transforming it into useful building blocks.

This work highlights the potential of biocatalysis to replace traditional chemical synthesis in complex molecule production. The high selectivity, low energy input, and environmentally friendly conditions offer significant advantages over conventional methods.

Quelle: ACS Catalysis, 2025

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