A novel ene-reductase from Halomonas elongata for flow biocatalytic synthesis of 3-phenylpropionaldehyde and sustainable indigo-carmine dyeing
Lauriane Pillet, Cristina Lía Fernández Reguerio, Markus Richard Busch, David Roura Padrosa, Francesca Paradisi
TL;DR
A new enzyme from Halomonas elongata efficiently reduces carbon-carbon double bonds and is used in a biocatalytic process to produce a chemical and a sustainable dye.
Contribution
A novel halophilic ene-reductase is characterized and applied in a flow biocatalytic system for efficient synthesis.
Findings
The ene-reductase from Halomonas elongata showed high activity across various substrates.
Flow biocatalytic reduction of cinnamaldehyde achieved a 62-fold process intensification compared to batch.
An enzymatic cascade converted indole to leuco-indigo with co-production of 2-oxindole.
Abstract
In order to broaden the toolbox of enzymes available for biocatalytic reductions of carbon-carbon double bonds, we investigated four promising ene-reductases (ERs) stemming from extremophilic organisms or showing homology with thermophilic ERs. The novel ene-reductase from the halophilic organism Halomonas elongata showed consistently high activity across a range of tested substrates. Upon immobilisation of the ERs, the flow biocatalytic ene-reduction of cinnamaldhehyde into 3-phenylpropionaldehyde was successfully achieved with an intensification of the process of 62-fold with respect to batch (2173.9 mg L−1 h−1 and 34.7 mg L−1 h−1, respectively). Additionally, to expand the scope of ERs applications, we describe a proof-of concept of a novel enzymatic cascade to convert indole to indigo using an unspecific peroxygenase, and its subsequent reduction to the water-soluble leuco-indigo.…
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Taxonomy
TopicsEnzyme Catalysis and Immobilization · Enzyme-mediated dye degradation · Biochemical and biochemical processes