Process development for efficient biosynthesis of l-DOPA with recombinant Escherichia coli harboring tyrosine phenol lyase from Fusobacterium nucleatum

Process development for efficient biosynthesis of l-DOPA with recombinant Escherichia coli... The tyrosine phenol lyase (TPL) catalyzed synthesis of L-DOPA was regarded as one of the most economic route for L-DOPA synthesis. In our previous study, a novel TPL from Fusobacterium nucleatum (Fn-TPL) was exploited for efficient biosyn- thesis of L-DOPA. However, the catalytic efficiency decreased when the reaction system expanded from 100 mL to 1 L. As such, the bioprocess for scale-up production of L-DOPA was developed in this study. To increase the stability of substrate and product, as well as decrease the by-product formation, the optimum temperature and pH were determined to be 15 °C and pH 8.0, respectively. The initial concentration of pyrocatechol, pyruvate and ammonium acetate was fixed at 8, 5 and 77 g/L and a fed-batch approach was applied with sodium pyruvate, pyrocatechol and ammonium acetate fed in a concentration of 5, 5 and 3.5 g/L, respectively. In addition, L-DOPA crystals were exogenously added to inhibit cell encapsulation by the precipitated product. The final L-DOPA concentration reached higher than 120 g/L with pyrocatechol conversion more than 96% in a 15-L stirred tank, demonstrating the great potential of Fn-TPL for industrial production of L-DOPA. Keywords L-DOPA · Tyrosine phenol lyase · Process development · Fed-batch reaction Introduction low productivity and with its catecholase activity, L-DOPA could be further http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bioprocess and Biosystems Engineering Springer Journals

Process development for efficient biosynthesis of l-DOPA with recombinant Escherichia coli harboring tyrosine phenol lyase from Fusobacterium nucleatum

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Publisher
Springer Berlin Heidelberg
Copyright
Copyright © 2018 by Springer-Verlag GmbH Germany, part of Springer Nature
Subject
Chemistry; Biotechnology; Industrial and Production Engineering; Environmental Engineering/Biotechnology; Industrial Chemistry/Chemical Engineering; Food Science
ISSN
1615-7591
eISSN
1615-7605
D.O.I.
10.1007/s00449-018-1962-8
Publisher site
See Article on Publisher Site

Abstract

The tyrosine phenol lyase (TPL) catalyzed synthesis of L-DOPA was regarded as one of the most economic route for L-DOPA synthesis. In our previous study, a novel TPL from Fusobacterium nucleatum (Fn-TPL) was exploited for efficient biosyn- thesis of L-DOPA. However, the catalytic efficiency decreased when the reaction system expanded from 100 mL to 1 L. As such, the bioprocess for scale-up production of L-DOPA was developed in this study. To increase the stability of substrate and product, as well as decrease the by-product formation, the optimum temperature and pH were determined to be 15 °C and pH 8.0, respectively. The initial concentration of pyrocatechol, pyruvate and ammonium acetate was fixed at 8, 5 and 77 g/L and a fed-batch approach was applied with sodium pyruvate, pyrocatechol and ammonium acetate fed in a concentration of 5, 5 and 3.5 g/L, respectively. In addition, L-DOPA crystals were exogenously added to inhibit cell encapsulation by the precipitated product. The final L-DOPA concentration reached higher than 120 g/L with pyrocatechol conversion more than 96% in a 15-L stirred tank, demonstrating the great potential of Fn-TPL for industrial production of L-DOPA. Keywords L-DOPA · Tyrosine phenol lyase · Process development · Fed-batch reaction Introduction low productivity and with its catecholase activity, L-DOPA could be further

Journal

Bioprocess and Biosystems EngineeringSpringer Journals

Published: Jun 5, 2018

References

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