Production of L-phenylalanine from phenylpyruvate using resting cells of Escherichia coli

Then, Johann; Doherty, Alice; Neatherway, H.; Marquardt, Rüdiger; Deger, H. M.; Voelskow, H.; Wöhner, Gerhard; Präve, Paul

doi:10.1007/bf01024597

Cited by 14 publications

(5 citation statements)

References 6 publications

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“…To reach more enhanced production of l ‐Phe, maintaining the substrate concentration as high as possible is necessary. However, aminotransferases are subject to substrate inhibition as shown in this study along with that of the other group (Then et al, 1987). To solve this problem, a continuous flow reaction should be considered.…”

Section: Discussionsupporting

confidence: 65%

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Enhanced Conversion Rate of L-Phenylalanine by Coupling Reactions of Aminotransferases and Phosphoenolpyruvate Carboxykinase in Escherichia coli K-12

et al. 1999

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In Escherichia coli, aspartate aminotransferase (encoded by aspC) and aromatic amino acid aminotransferase (encoded by tyrB) share overlapping substrate specificity in the syntheses of aromatic amino acids. Through the transamination reactions catalyzed by AspC or TyrB, L-phenylalanine (L-Phe) can be produced from phenylpyruvate with aspartic acid as the amino donor. To modulate and enhance the production levels of proteins, both aspC and tyrB were subcloned into a runaway-replication vector. As a result, the specific activities of AspC and TyrB obtained showed 65-fold and 50-fold increases, respectively, compared with the wild-type level. Employing resting cells of AspC- and TyrB-overproducing E. coli K-12 strains for L-Phe productions resulted in molar conversion yields of 70% and 55%, respectively. With an additional introduction of phosphoenolpyruvate carboxykinase (encoded by pck) into the transamination reactions, the conversion yields were improved to 93% from 70% and to 75% from 55% in a relatively short time. These results account for more than an 8-fold increase in productivity, as compared to the previous report (Calton et al., 1985). In addition, a four-run reuse of the recombinant cells for L-Phe production gave a total yield of 91 g/L with a 93% conversion.

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Section: Discussionsupporting

confidence: 65%

“…Moreover, the use of E. coli B 11303 and Z1196 for l ‐Phe production from PPA with aspartate (Asp) as an amino donor was reported to obtain roughly 15.4 and 17.3 g/L, respectively. The molar conversion yields of l ‐Phe obtained in these two cases exceeded 90% (Calton et al, 1985; Then et al, 1987).…”

Section: Introductionmentioning

confidence: 97%

Enhanced Conversion Rate of L-Phenylalanine by Coupling Reactions of Aminotransferases and Phosphoenolpyruvate Carboxykinase in Escherichia coli K-12

et al. 1999

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“…However, all previous studies on PLA production by lactobacilli have used Phe rather than PPA as substrate, and the possibility to increase PLA yield by an optimized supply of substrate needs to be elucidated. Traditionally, PPA has been used to produce L-Phe which is in high demand for the production of an artificial sweetener ''aspartame'' (Matsunaga et al 1987;Then et al 1987). Therefore, compared with Phe, PPA can be obtained easily at a lower price.…”

Section: Introductionmentioning

confidence: 99%

Biotransformation of phenylpyruvic acid to phenyllactic acid by growing and resting cells of a Lactobacillus sp.

Jiang

Pan

2007

Biotechnol Lett

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Phenyllactic acid (PLA) is a novel antimicrobial compound derived from phenylalanine (Phe). Lactobacillus sp. SK007, having high PLA-producing ability, was isolated from Chinese traditional pickles. When 6.1 mM phenylpyruvic acid (PPA) was used to replace Phe as substrate at the same concentration, PLA production increased 14-fold and the fermentation time decreased from 72 h to 24 h with growing cells. With resting cells, however, 6.8 mM PLA could be obtained as optimal yield using the following conditions: 12 mM PPA, 55 mM glucose, pH 7.5, 35 degrees C and 4 h.

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“…Therefore, numerous studies have already been performed focusing, for instance, on L-phe production with isolated enzymes [5,6,7,8], immobilized cells [9] or resting cells [10]. Fermentation processes have also been investigated using Corynebacterium glutamicum [11,12,13] or, most importantly, Escherichia coli [14,15,16,17,18,19].…”

Section: Introductionmentioning

confidence: 99%

Fully integrated L-phenylalanine separation and concentration using reactive-extraction with liquid-liquid centrifuges in a fed-batch process with E. coli

Rüffer

Heidersdorf

Kretzers

et al. 2004

Bioprocess Biosyst Eng

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A novel in situ product recovery (ISPR) approach for the (fully) integrated separation of L-phenylalanine (L-phe) from a 20 l fed-batch process with the recombinant L-tyrosine auxotrophic strain E. coli F-4/pF81 is presented. The strain was rationally constructed for the production of the aromatic amino acid. Glucose and tyrosine control is used. A reactive extraction system consisting of kerosene, the cation-selective carrier D(2)EHPA and sulphuric acid, all circulating in liquid-liquid centrifuges, is applied for the on-line L-phe separation from cell- and protein-free permeate. Permeate is drained off from the bioreactor bypass. Using the novel ISPR approach, a significantly extended product formation period at 0.25 mmol/(g*h) together with a reduced by-product formation and a 28% relative glucose/L-phe yield increase is observed. Thus, the ISPR approach is superior to the reference non-ISPR process and even offers extraction rates approximately three times higher than the published membrane-based process.

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Production of L-phenylalanine from phenylpyruvate using resting cells of Escherichia coli

Cited by 14 publications

References 6 publications

Enhanced Conversion Rate of L-Phenylalanine by Coupling Reactions of Aminotransferases and Phosphoenolpyruvate Carboxykinase in Escherichia coli K-12

Enhanced Conversion Rate of L-Phenylalanine by Coupling Reactions of Aminotransferases and Phosphoenolpyruvate Carboxykinase in Escherichia coli K-12

Biotransformation of phenylpyruvic acid to phenyllactic acid by growing and resting cells of a Lactobacillus sp.

Fully integrated L-phenylalanine separation and concentration using reactive-extraction with liquid-liquid centrifuges in a fed-batch process with E. coli

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