Overview on the biotechnological production of l-DOPA

Min, Kyoungseon; Park, Kyungmoon; Park, Don-Hee; Yoo, Young Je

doi:10.1007/s00253-014-6215-4

Cited by 90 publications

(84 citation statements)

References 30 publications

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“…In general, chemical synthesis and the enzymatic route are the most common methods employed for preparing UAAs. For example, L‐DOPA can be synthesized both chemically and enzymatically [42–45]. The chemical approach is often undesirable because it is complex and requires expensive metal catalysts, high temperatures, and harsh reaction conditions.…”

Section: Uaa Synthesis For Biosynthetic Incorporationmentioning

confidence: 99%

“…The chemical approach is often undesirable because it is complex and requires expensive metal catalysts, high temperatures, and harsh reaction conditions. In contrast, the enzymatic approach, which requires only mild reaction conditions, can potentially produce L‐DOPA in good yields, and the resulting waste products are often biodegradable – a huge advantage when it comes to industrial applications [45]. Here we will focus on the enzymatic route because it provides an easy, inexpensive way to synthesize UAA.…”

Section: Uaa Synthesis For Biosynthetic Incorporationmentioning

confidence: 99%

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Incorporating unnatural amino acids to engineer biocatalysts for industrial bioprocess applications

Ravikumar

Nadarajan

Yoo

et al. 2015

Biotechnology Journal

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The bioprocess engineering with biocatalysts broadly spans its development and actual application of enzymes in an industrial context. Recently, both the use of bioprocess engineering and the development and employment of enzyme engineering techniques have been increasing rapidly. Importantly, engineering techniques that incorporate unnatural amino acids (UAAs) in vivo has begun to produce enzymes with greater stability and altered catalytic properties. Despite the growth of this technique, its potential value in bioprocess applications remains to be fully exploited. In this review, we explore the methodologies involved in UAA incorporation as well as ways to synthesize these UAAs. In addition, we summarize recent efforts to increase the yield of UAA engineered proteins in Escherichia coli and also the application of this tool in enzyme engineering. Furthermore, this protein engineering tool based on the incorporation of UAA can be used to develop immobilized enzymes that are ideal for bioprocess applications. Considering the potential of this tool and by exploiting these engineered enzymes, we expect the field of bioprocess engineering to open up new opportunities for biocatalysis in the near future.

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Section: Uaa Synthesis For Biosynthetic Incorporationmentioning

confidence: 99%

Section: Uaa Synthesis For Biosynthetic Incorporationmentioning

confidence: 99%

Incorporating unnatural amino acids to engineer biocatalysts for industrial bioprocess applications

Ravikumar

Nadarajan

Yoo

et al. 2015

Biotechnology Journal

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“…L-DOPA is used for treating Parkinson's disease and also a precursor for synthesizing valued benzylisoquinoline alkaloids 27,28 . Various biotechnological approaches have been applied for L-DOPA production, including microbial fermentation, immobilized tyrosinase as well as electroenzymatic system 29 . Previous studies have revealed an over 3.5 mg L −1 of L-DOPA production from glucose in yeast, using a tyrosine hydroxylase developed from a cytochrome P450 L-DOPA oxidase 30,31 .…”

Section: Discussionmentioning

confidence: 99%

Developing a highly efficient hydroxytyrosol whole-cell catalyst by de-bottlenecking rate-limiting steps

Yao

et al. 2020

Nat Commun

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Hydroxytyrosol is an antioxidant free radical scavenger that is biosynthesized from tyrosine. In metabolic engineering efforts, the use of the mouse tyrosine hydroxylase limits its production. Here, we design an efficient whole-cell catalyst of hydroxytyrosol in Escherichia coli by de-bottlenecking two rate-limiting enzymatic steps. First, we replace the mouse tyrosine hydroxylase by an engineered two-component flavin-dependent monooxygenase HpaBC of E. coli through structure-guided modeling and directed evolution. Next, we elucidate the structure of the Corynebacterium glutamicum VanR regulatory protein complexed with its inducer vanillic acid. By switching its induction specificity from vanillic acid to hydroxytyrosol, VanR is engineered into a hydroxytyrosol biosensor. Then, with this biosensor, we use in vivo-directed evolution to optimize the activity of tyramine oxidase (TYO), the second ratelimiting enzyme in hydroxytyrosol biosynthesis. The final strain reaches a 95% conversion rate of tyrosine. This study demonstrates the effectiveness of sequentially de-bottlenecking rate-limiting steps for whole-cell catalyst development.

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“…The high cost of enzymes becomes one of the disadvantages of the enzyme-based process. Current biotechnological needs are enhanced enzyme productivity and development of techniques to increase the shelf-life of enzymes for various applications [10]. These requirements are essential to facilitate large-scale and economical formulation.…”

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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Overview on the biotechnological production of l-DOPA

Cited by 90 publications

References 30 publications

Incorporating unnatural amino acids to engineer biocatalysts for industrial bioprocess applications

Incorporating unnatural amino acids to engineer biocatalysts for industrial bioprocess applications

Developing a highly efficient hydroxytyrosol whole-cell catalyst by de-bottlenecking rate-limiting steps

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

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