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

Author:

Gao Siyuan1,Ma Ding1,Wang Yongtao1,Zhang Alei1,Wang Xin1,Chen Kequan1

Affiliation:

1. Nanjing Tech University

Abstract

Abstract 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 co-expressed. The effects of the concentration of L-dopa, PLP, reaction temperature and pH were characterized for improvement of bioconversion. Under optimal conditions, dopamine titer reach to 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 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 and provided reference for whole-cell catalysis which is hindered by permeability.

Publisher

Research Square Platform LLC

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