Biosynthesis of l-DOPA by Aspergillus oryzae

Ikram-ul-Haq,; Ali, Sikander; Qadeer, M. A.

doi:10.1016/s0960-8524(02)00060-3

Cited by 32 publications

(16 citation statements)

References 2 publications

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“…L-DOPA is a precursor of the production of dopamine by the central nervous system. Thus, L-DOPA is used as a potent drug for the treatment of Parkinson's disease and is also used to control the myocardium neurogenic injury [84]. Production of L-DOPA using L-tyrosine as substrate and L-ascorbate as reducing agent with the enzyme tyrosinase (EC 1.14.18.1) as biocatalyst has been studied [85].…”

Section: Microbial Tyrosinase For Manufacture Of L-dopa In Pharmacmentioning

confidence: 99%

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Zaidi

Ali²,

Ali³

et al. 2014

Biochemistry Research International

143

111

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Tyrosinase is a natural enzyme and is often purified to only a low degree and it is involved in a variety of functions which mainly catalyse the o-hydroxylation of monophenols into their corresponding o-diphenols and the oxidation of o-diphenols to o-quinones using molecular oxygen, which then polymerizes to form brown or black pigments. The synthesis of o-diphenols is a potentially valuable catalytic ability and thus tyrosinase has attracted a lot of attention with respect to industrial applications. In environmental technology it is used for the detoxification of phenol-containing wastewaters and contaminated soils, as biosensors for phenol monitoring, and for the production of L-DOPA in pharmaceutical industries, and is also used in cosmetic and food industries as important catalytic enzyme. Melanin pigment synthesized by tyrosinase has found applications for protection against radiation cation exchangers, drug carriers, antioxidants, antiviral agents, or immunogen. The recombinant V. spinosum tryosinase protein can be used to produce tailor-made melanin and other polyphenolic materials using various phenols and catechols as starting materials. This review compiles the recent data on biochemical and molecular properties of microbial tyrosinases, underlining their importance in the industrial use of these enzymes. After that, their most promising applications in pharmaceutical, food processing, and environmental fields are presented.

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Section: Microbial Tyrosinase For Manufacture Of L-dopa In Pharmacmentioning

confidence: 99%

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Zaidi

Ali²,

Ali³

et al. 2014

Biochemistry Research International

143

111

View full text Add to dashboard Cite

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“…To increase L-DOPA production, A. oryzae strain GCB-6 was mutated by ultraviolet irradiation and the mutant strain UV-7 yielded 3.72-fold L-DOPA than the parental strain (Ikram-ul et al 2002). They further improved the mutant strain UV-7 by chemical mutation using nmethyl-L-3-nitro-n-nitrosoguanidine as the mutagen and consequently the double mutant maximally produced 444 mg of L-DOPA/g of cells.…”

Section: Based On Tyrosinase Activitymentioning

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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“…There were many biological soures reported for enantiometrically pure L-DOPA ( Table 1). Stemonitis herbicola 50 mg [25] Aspergillus oryzae ( mutant) 1.28 mg/ml [26] Aspergillus oryzae 1.28 mg/ml [27] Aspergillus oryzae UV7( double mutant) 1.28 mg ml [28] Aspergillus oryzae 1.86 mg/ml [29] Aspergillus oryzae UV-7 444 g cells [30] Aspergillus oryzae ME2 (Illite) 1.686 mg/ml [31] Aspergillus oryzae ME2 (Celite) 0.428 mg/ml [32] Aspergillus oryzae (Double mutant) 300 mg [33] Aspergillus oryzae IIB-6 1.34 mg/ml [34] Acremonium retilum 0.89 mg/ml [35] Aspergillus niger 0.365 mg/ml [36] Actinomycetes 28.6% [37] Yeast Yarrowia lipolytica NRRL-143 2.96 mg/ml [38] Egyptian halophilic black yeast 66 ug/ml [39] Bacteria Vibrio tyrosinaticus 4 mg/ml [40] Pseudomonas melanogenum 8 mg/ml [41] E. coli W(ATCC 11105) (p-hydroxyphenyl acetate 3-hydroxylase) 48 mM in reaction mixture [42] Bacillus sp. JPJ 0.497 mg/ml [7] Recombinant The production of L-DOPA from biological sources involves the oxidation of L-tyrosine by enzyme tyrosinase (E.C.1.14.18.1), which is copper containing enzyme widely distributed in plants, animals and microorganisms [13].…”

Section: Biological Sourcesmentioning

confidence: 99%

“…L-DOPA produced by the method was enantiometrically pure as well as it is cost effective. Similarly, biotransformation of L-DOPA from L-tyrosine was carried out using Acremonium reticulum by submerged fermentation process yields more amount of L-DOPA in the broth [24][25][26][27][28][29][30][31][32][33][34][35][36][37]. Production of L-DOPA also reported from yeast species [38,39].…”

Section: Fungal Sourcesmentioning

confidence: 99%