Synthesis of l-dopa by escherichia intermedia cells immobilized in a polyacrylamide gel

Para, G.; Baratti, J.

doi:10.1007/bf00250445

Cited by 10 publications

(2 citation statements)

References 17 publications

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“…It lowers the production cost due to the reusability of the enzymes. The various techniques used for enzyme immobilization include entrapment in polymeric gels, adsorption onto insoluble materials, encapsulation in membranes, cross-linking with bifunctional or multifunctional reagents and linking to an insoluble carrier [16][17][18][19][20][21][22][23]. The substrate used for the synthesis of L-DOPA were catechol, sodium pyruvate and ammonium acetate.…”

Section: Enzymatic Synthesismentioning

confidence: 99%

Biological sources of L-DOPA: An alternative approach

Patil¹,

Apine²,

Surwase³

et al. 2013

APD

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Section: Enzymatic Synthesismentioning

confidence: 99%

Biological sources of L-DOPA: An alternative approach

Patil¹,

Apine²,

Surwase³

et al. 2013

APD

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“…In view of the pharmaceutical importance of L-DOPA, attempts have been made to find suitable microorganisms capable of producing L-DOPA on a commercial scale. Although microbial synthesis of L-DOPA was first detected from fungal sources in 1969 [1], the literature indicates that such work has mostly utilized bacteria [2][3][4][5][6]. Comparatively little information is available on [ungal production of L-DOPA, all from various studies of Aspergillus oryzae [7 9].…”

Section: Introductionmentioning

confidence: 99%

Production of ?-DOPA by Aspergillus terreus

Chattopadhyay¹

1990

FEMS Microbiology Letters

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Production of L-DOPA by the activity of tyrosinase from a strain of Aspergillus terreus 104 was investigated. Effects of substrate (L-tyrosine) concentrations, its mode of feeding to the assay mixture and also the effects of L-ascorbic acid and other antioxidants on the production rate of L-DOPA were studied. The parameters for optimal production of L-DOPA with a maximum conversion of 85% of 0.1% L-tyrosine were determined.

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Development of a multienzyme reactor for dopamine synthesis: I. Enzymology and kinetics

Anderson

Moo‐Young

Legge

1992

Biotech & Bioengineering

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The enzymology and kinetics of tyrosine phenol lyase (TPL) from Erwinia herbicola, and tyrosine decarboxylase (TDC) from Streptococcus faecalis have been investigated for potential use in a coimmobilized multienzyme biocatalytic system for the production of dopamine. In this multienzyme biotransformation using whole cells optimized for each of the respective enzymes, TPL catalyzes the production of 3,4-dihydroxyphenyl-L-alanine (L-dopa) from catechol, pyruvate, and ammonium, and this is subsequently decarboxylated by TDC to produce dopamine. Performing the reactions simultaneously, thereby removing L-dopa, is one option for overcoming the TPL equilibrium constraints. The enzymes have different optimal pH values, so the reaction kinetics at a compromise pH of 7.1, where both enzymes could be operated simultaneously, were investigated. For the concentration range investigated, TPL followed pseudo-first-order kinetics with respect to catechol, pyruvate, and ammonium. TDC exhibited significant product inhibition as well as inhibition by combinations of catechol and pyruvate.

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Synthesis of l-dopa by escherichia intermedia cells immobilized in a polyacrylamide gel

Cited by 10 publications

References 17 publications

Biological sources of L-DOPA: An alternative approach

Biological sources of L-DOPA: An alternative approach

Production of ?-DOPA by Aspergillus terreus

Development of a multienzyme reactor for dopamine synthesis: I. Enzymology and kinetics

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