Whole-cell catalyze L-dopa to dopamine via co-expression of transport protein AroP in Escherichia coli

Dopamine is high-value compound of pharmaceutical interest, but its industrial scale production mostly focuses on chemical synthesis, possessing environment pollution. Bio-manufacturing has caused much attention for its environmental characteristic. Resting cells were employed to as biocatalysts with extraordinary advantages like offering stable surroundings, the inherent presence of expensive cofactors. In this study, whole-cell bioconversion was employed to convert dopa to dopamine. To increase the titer and yield of dopamine production through whole-cell catalysis, three kinds of aromatic amino acid transport protein, AroP, PheP and TyrP, were selected to be co-expressed. The effects of the concentration of L-dopa, pyridoxal-5'- phosphate (PLP), reaction temperature and pH were characterized for improvement of bioconversion. Under optimal conditions, dopamine titer reached 1.44 g/L with molar yield of 46.3%, which is 6.62 times than that of initial conditions. The catalysis productivity of recombinant E. coli co-expressed L-dopa decarboxylase(DDC) and AroP was further enhanced by repeated cell recycling, which maintained over 50% of its initial ability with eight consecutive catalyses. This study was the first to successfully bioconversion of dopamine by whole-cell catalysis. This research provided reference for whole-cell catalysis which is hindered by cell membrane.

Automated summary

Resting cells were used as biocatalysts to convert L-dopa to dopamine through whole-cell bioconversion. The co-expression of three aromatic amino acid transport proteins, AroP, PheP, and TyrP, improved the titer and yield of dopamine production. Under optimal conditions, dopamine titer reached 1.44 g/L with a molar yield of 46.3%, which was 6.62 times higher than the initial conditions.