Effective production of 3,4-dihydroxyphenyl-l-alanine (l-DOPA) with Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR

Koyanagi, Takashi; Katayama, Takane; Suzuki, Hideyuki; Nakazawa, Hidetsugu; Yokozeki, Kenzo; Kumagai, Hidehiko

doi:10.1016/j.jbiotec.2004.08.016

Cited by 72 publications

(59 citation statements)

References 13 publications

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“…One such mutant, TyrR V67A Y72C E201G , was found to increase Tpl expression effectively, 10) and when the mutant gene was introduced into E. herbicola, the resulting strain showed improved L-dopa productivity. 11) However, the addition of L-tyrosine to the medium was still required to achieve the maximum productivity of the strain (Fig. 1B, tyrR NT , see below).…”

Section: Abstract: 34-dihydroxyphenyl-l-alaninementioning

confidence: 99%

Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

Koyanagi

Katayama

Suzuki

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Section: Abstract: 34-dihydroxyphenyl-l-alaninementioning

confidence: 99%

Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

Koyanagi

Katayama

Suzuki

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…Synthesis of this drug by a proprietary Monsanto process suffers from several disadvantages [1]. The Monsanto Process was the first commercialized catalytic asymmetric hydrogenation synthesis employing a chiral transition metal complex, and it has been in operation since 1974 [2,3]. However, this method suffers from disadvantages such as low overall yields, the need for separation of diastereomers, and the need for expensive chiral catalysts [4].…”

Section: Introductionmentioning

confidence: 99%

“…These processes are time-consuming and result in low conversion rates [5][6][7][8][9]. One promising approach is production of L-DOPA from the enzymatic conversion of the L-tyrosine by using tyrosinase.…”

Section: Introductionmentioning

confidence: 99%

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

Rahman

Gobikhrisnan

Gozan

et al. 2016

Korean Chemical Engineering Research

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− Levodopa or L-3,4-dihydroxyphenylalanine (L-DOPA) is the direct precursor of the neurotransmitter dopamine. L-DOPA is a well-known neuroprotective agent for the treatment of Parkinson's disease symptoms. L-DOPA was synthesized using the enzyme, tyrosinase, as a biocatalyst for the conversion of L-tyrosine to L-DOPA and an electrochemical method for reducing L-DOPAquinone, the product resulting from enzymatic synthesis, to L-DOPA. In this study, three electrode systems were used: A glassy carbon electrode (GCE) as working electrode, a platinum, and a Ag/ AgCl electrode as auxiliary and reference electrodes, respectively. GCE has been modified using electropolymerization of pyrrole to facilitate the electron transfer process and immobilize tyrosinase. Optimum conditions for the electropolymerization modified electrode were a temperature of 30 o C and a pH of 7 producing L-DOPA concentration 0.315 mM. After 40 days, the relative activity of an enzyme for electropolymerization remained 38.6%, respectively.

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“…Accordingly, the market size for L-DOPA is substantial; the world market of L-DOPA is about 250 ton per year and the total market volume is about 101 billion per year (Koyanagi et al 2005). Since Monsanto developed and introduced the commercial process for L-DOPA production by asymmetric hydrogenation for the first time, most L-DOPA has been supplied by chemical synthesis, mainly asymmetric synthesis (Knowles 2004).…”

Section: Introductionmentioning

confidence: 99%

Overview on the biotechnological production of l-DOPA

Min

Park

et al. 2014

Appl Microbiol Biotechnol

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L-DOPA (3,4-dihydroxyphenyl-L-alanine) has been widely used as a drug for Parkinson's disease caused by deficiency of the neurotransmitter dopamine. Since Monsanto developed the commercial process for L-DOPA synthesis for the first time, most of currently supplied L-DOPA has been produced by the asymmetric method, especially asymmetric hydrogenation. However, the asymmetric synthesis shows critical limitations such as a poor conversion rate and a low enantioselectivity. Accordingly, alternative biotechnological approaches have been researched for overcoming the shortcomings: microbial fermentation using microorganisms with tyrosinase, tyrosine phenol-lyase, or p-hydroxyphenylacetate 3-hydroxylase activity and enzymatic conversion by immobilized tyrosinase. Actually, Ajinomoto Co. Ltd commercialized Erwinia herbicola fermentation to produce L-DOPA from catechol. In addition, the electroenzymatic conversion system was recently introduced as a newly emerging scheme. In this review, we aim to not only overview the biotechnological L-DOPA production methods, but also to briefly compare and analyze their advantages and drawbacks. Furthermore, we suggest the future potential of biotechnological L-DOPA production as an industrial process.

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Effective production of 3,4-dihydroxyphenyl-l-alanine (l-DOPA) with Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR

Cited by 72 publications

References 13 publications

Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

Overview on the biotechnological production of l-DOPA

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