Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes

Laccases are multi-copper oxidases that catalyze the oxidation of various electron-rich substrates with concomitant reduction of molecular oxygen to water. The multi-copper oxidase/laccase CueO of Escherichia coli is responsible for the oxidation of Cu+ to the less harmful Cu2+ in the periplasm. CueO has a relatively broad substrate spectrum as laccase, and its activity is enhanced by copper excess. The aim of this study was to trigger CueO activity in vivo for the use in biocatalysis. The addition of 5 mM CuSO4 was proven effective in triggering CueO activity at need with minor toxic effects on E. coli cells. Cu-treated E. coli cells were able to convert several phenolic compounds to the corresponding dimers. Finally, the endogenous CueO activity was applied to a four-step cascade, in which coniferyl alcohol was converted to the valuable plant lignan (-)-matairesinol.

Automated summary

The study demonstrated that triggering CueO activity by adding CuSO4 in vivo can facilitate the conversion of phenolic compounds by E. coli cells. Subsequently, a four-step cascade reaction was successfully used to convert coniferyl alcohol to the valuable plant lignan (-)-matairesinol.