Microbiological Synthesis of L-dopa

Rosazza, John P. N.; Foss, Paul; Lemberger, Michael; Sih, Charles J.

doi:10.1002/jps.2600630411

Cited by 17 publications

(9 citation statements)

References 11 publications

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“…Sahi et al [3] first reported the production of l ‐dopa from l ‐tyrosine by fungi. Haneda et al [4] used the fungus Aspergillus oryzae (grey rot mould) for the conversion of l ‐tyrosine into l ‐dopa, which is produced from l ‐tyrosine by the one‐step oxidation reaction catalysed by tyrosinase, tyrosine hydroxylase or α‐tyrosinase in living organisms [5,6]. Tyrosinases (EC 1.14.1.18.1) are widely distributed in Nature and have been purified to homogeneity from both microbial and plant sources [7].…”

Section: Introductionmentioning

confidence: 99%

Double mutant of Aspergillus oryzae for improved production of l‐dopa (3,4‐dihydroxyphenyl‐l‐alanine) from l‐tyrosine

Ali

Haq

Qadeer

et al. 2005

Biotech and App Biochem

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Aspergillus oryzae mutant strain UV-7 was further improved for the production of L-dopa from L-tyrosine using chemical mutation. Different putative mutant strains of the organism were tested for the production of L-dopa in triplicate shake-flask cultures. Among these putative mutants, the strain designated SI-12 gave a maximal production of L-dopa (444+/-14 mg of L-dopa/g of cells). The regulation of L-dopa from different carbon source solutions [initial substrate concentration (S(0))=30 g/l] by the mutant culture was investigated. At an initial pH (pH(0)) of 5.0 and a temperature (T) of 30 degrees C, 100% of sugars were utilized for product and cell mass formation, corresponding to final L-dopa product yield of 189+/-8 mg/g of substrate utilized and maximum volumetric and specific productivities of 145+/-5 mg/h per litre and 155+/-8 mg/h per g of cells respectively. There was up to 3-fold enhancement in product formation rate. This enhancement is, to our knowledge, the highest reported in the literature. To explain the kinetic mechanism of L-dopa formation and its thermal inactivation, the thermodynamic parameters were determined with the application of the Arrhenius model. Activation enthalpy and entropy for product formation, in the case of the mutant derivative, were 40 kJ/mol and 0.076 kJ.mol(-1).K(-1) for its production and 116 kJ/mol and 0.590 kJ.mol(-1).K(-1) for thermal inactivation respectively. The respective values for product formation and product de-activation were lower than the respective values for the parental culture. Therefore the mutant strain was thermodynamically more resistant to thermal denaturation during the product-formation process.

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Section: Introductionmentioning

confidence: 99%

Double mutant of Aspergillus oryzae for improved production of l‐dopa (3,4‐dihydroxyphenyl‐l‐alanine) from l‐tyrosine

Ali

Haq

Qadeer

et al. 2005

Biotech and App Biochem

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“…All previous results that pointed to the similarities in microbial and mammalian enzyme systems represented a foundation for establishing microbial models of mammalian metabolism. Our attention was initially focused on aromatic hydroxylation to test the feasibility of this proposal for three reasons: (a) it represents a commonly occurring mammalian biotransformation; (b) aryl hydroxylase activity similar to that displayed by mammalian cytochrome P-450 had been demonstrated in several microbial species (53, 55,56); and (c) phenol formation, vis-A-vis arene oxide intermediates, had been implicated in mechanisms of toxicity of certain aromatic compounds (27, 28,601. A literature survey indicated that a number of microorganisms possessed aromatic hydroxylating activity (18,55,56); 11 microorganisms [A. niger (ATCC1 9142), Penicillium chrysogenum (ATCC' 10002), Cunninghamella blakesleeana (ATCC' 8688a)) Aspergillus ochraceous (ATCC' 1008), Gliocladium deliquescens (1086), Streptomyces species (1158w), €2. stolonifer (NRRL2 1477), Curuularia lunata (NRRL2 2178), Streptomyces rimosus (ATCC' 23955), C. bainieri (ATCC' 9244)) and H. piriforme (QM3 6945)] were selected as microbial models of mammalian aromatic hydroxylation (9).…”

Section: Scheme Zvmentioning

confidence: 99%

“…Other examples of the use of microbial transformations for the production of hydroxylated metabolites are 5-anilino-1,2,3,4-thiatriazoles (89), fenclozic acid (go), 5-hydroxytryptophol (17), a-methylfluorene-2-acetic acid (911, and levodopa (18).…”

Section: Scheme Zvmentioning

confidence: 99%

Microbial Models of Mammalian Metabolism

Smith¹,

Rosazza

1975

Journal of Pharmaceutical Sciences

190

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“…Haneda et al (10) used Aspergillus oryzae for the conversion of L-tyrosine to L-DOPA. L-DOPA is produced from L-tyrosine by the one step oxidation reaction catalyzed by the enzyme tyrosinase, tyrosine hydroxylase or β-tyrosinase in living organisms (11,23). Tyrosinases (EC 1.14.1.18.1) are widely distributed in nature and have been purified to homogeneity level.…”

Section: Introductionmentioning

confidence: 99%

Mutation of Aspergillus oryzae for improved production of 3, 4-dihydroxy phenyl-L-alanine (L-DOPA) from L-tyrosine

Haq

Ali

2006

Braz. J. Microbiol.

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Aspergillus oryzae mutant strain UV-7 was further improved for the production of L-DOPA from L-tyrosine using chemical mutation. Different putative mutant strains of organism were tested for the production of L-DOPA in submerged fermentation. Among these putative mutant strains, mutant designated SI-12 gave maximum production of L-DOPA (300 mg L-DOPA.g -1 cells). The production of L-DOPA from different carbon source solutions (So= 30 g.l -1 ) by mutant culture was investigated at different nitrogen sources, initial pH and temperature values. At optimum pH (pHo= 5.0), and temperature (t=30ºC), 100% sugars were utilized for production and cell mass formation, corresponding to final L-DOPA product yield of 150 mg.g -1 substrate utilized, and maximum volumetric and specific productivities of 125 mg.l , respectively. There was up to 3-fold enhancement in product formation rate. This enhancement is the highest reported in literature. To explain the kinetic mechanism of L-DOPA formation and thermal inactivation of tyrosinase, the thermodynamic parameters were determined with the application of Arrhenius model: activation enthalpy and entropy for product formation, in case of mutant derivative, were 40 k j/mol and 0.076 k j/mol. K for L-DOPA production and 116 k j/mol and 0.590 k j/mol. K for thermal inactivation, respectively. The respective values for product formation were lower while those for product deactivation were higher than the respective values for the parental culture. Therefore, the mutant strain was thermodynamically more resistant to thermal denaturation.

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Microbiological Synthesis of L-dopa

Cited by 17 publications

References 11 publications

Double mutant of Aspergillus oryzae for improved production of l‐dopa (3,4‐dihydroxyphenyl‐l‐alanine) from l‐tyrosine

Double mutant of Aspergillus oryzae for improved production of l‐dopa (3,4‐dihydroxyphenyl‐l‐alanine) from l‐tyrosine

Microbial Models of Mammalian Metabolism

Mutation of Aspergillus oryzae for improved production of 3, 4-dihydroxy phenyl-L-alanine (L-DOPA) from L-tyrosine

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