l-Dopa synthesis catalyzed by tyrosinase immobilized in poly(ethyleneoxide) conducting polymers

Yıldız, Hüseyin Bekir; Çalışkan, Salim; Kamacı, Musa; Çalışkan, Abdullah; Yılmaz, Haşim

doi:10.1016/j.ijbiomac.2013.01.031

Cited by 22 publications

(22 citation statements)

References 50 publications

(47 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our result confirmed the findings of Rahman et al, 2012 [16] that the optimum conditions for the electroenzymatic synthesis of L-DOPA and/or free enzyme were at pH 7 and 30 o C. Erdogan et al [21] and Yildiz et al [14] reported the optimum pH and temperature for L- DOPA synthesis using conducting polymers. Erdogan et al [21] changed pH between pH 6 and 7.5 and for all experiments using a free enzyme, polypyrrole, and Poly(3,4-ethylenedioxythiophene) (PEDOT) matrices; maximum activity was observed at pH 7.…”

Section: -3 Effect Of Ph and Temperature On Electroenzymatic Reactionsupporting

confidence: 91%

“…The electrode was rinsed thoroughly with Milli-Q water after electropolymerization to remove any loosely-bound enzyme. Electropolymerization of pyrrole was achieved by applying 1.0 V for 40 min [14]. After polymerization, a thin layer of dark polypyrrole was formed on the electrode surface.…”

Section: -2-1 Preparation Of Modified Electrodementioning

confidence: 99%

“…Yildiz et al [14] investigated the synthesis of L-DOPA by immobilizing tyrosinase on conducting polymers: thiophene-capped poly (ethyleneoxide)/polypyrrole (PEO-co-PPy) and 3-methylthienyl methacrylate-co-p-vinylbenzyloxy poly(ethyleneoxide)/pyrrole (CP-co-PPy). The optimum pH for both the conducting polymers was around pH 7.…”

Section: -3 Effect Of Ph and Temperature On Electroenzymatic Reactionmentioning

confidence: 99%

See 2 more Smart Citations

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

Rahman

Gobikhrisnan

Gozan

et al. 2016

Korean Chemical Engineering Research

View full text Add to dashboard Cite

− 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.

show abstract

Section: -3 Effect Of Ph and Temperature On Electroenzymatic Reactionsupporting

confidence: 91%

Section: -2-1 Preparation Of Modified Electrodementioning

confidence: 99%

Section: -3 Effect Of Ph and Temperature On Electroenzymatic Reactionmentioning

confidence: 99%

See 1 more Smart Citation

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

Rahman

Gobikhrisnan

Gozan

et al. 2016

Korean Chemical Engineering Research

View full text Add to dashboard Cite

show abstract

“…Therefore, operational and storage stabilities are essential parameters for an immobilized enzyme (Yildiz et al, 2013). The storage stabilities of the free and immobilized enzymes were investigated by storing in 0.1 M phosphate buffer (pH 7.0) at 4°C for a period of 20 days.…”

Section: Methodsmentioning

confidence: 99%

“…Enzyme immobilization has been found to be a promising way to overcome these limitations and to enhance the catalytic performance of enzymes (Ensuncho et al, 2005; Arica and Bayramoglu, 2006; Bayramoglu et al, 2012). Immobilization of enzyme has several advantages, such as improved stability by protecting the protein from deactivation, high reproducibility, improved thermal and storage stability, significant reduction in the production cost, easy recovery of the enzyme and continuous and repeated use (Cirpan et al, 2003; Yildiz et al, 2013). …”

Section: Introductionmentioning

confidence: 99%

Aspergillus niger PA2 Tyrosinase Covalently Immobilized on a Novel Eco-Friendly Bio-Composite of Chitosan-Gelatin and Its Evaluation for L-DOPA Production

et al. 2016

View full text Add to dashboard Cite

Tyrosinase (EC 1.14.18.1) a copper-containing monooxygenase, isolated from a fungal isolate Aspergillus niger PA2 was subjected for immobilization onto a composite consisting of chitosan and gelatin biopolymers. The homogeneity of the chitosan-gelatin biocomposite film was characterized by X-ray diffraction analyses. To evaluate immobilization efficiency, chitosan-gelatin-Tyr bio-composite films were analyzed by field emission scanning electron microscopy, atomic force microscopy and UV-spectroscopy. The rough morphology of the film led to a high loading of enzyme and it could retain its bioactivity for a longer period. The enzyme adsorbed onto the film exhibited 72% of its activity after 10 days and exhibited good repeatability for up to nine times, after intermittent storage. Moreover, the immobilized enzyme exhibited broader pH and temperature profile as compared to free counterpart. Immobilized enzyme was further evaluated for the synthesis of L-DOPA (2,4-dihydroxy phenylalanine) which is a precursor of dopamine and a potent drug for the treatment of Parkinson's disease and for myocardium neurogenic injury.

show abstract

Nanoparticles Mimicking Oxidase Activity and their Application in Synthesis of Neurodegenerative Therapeutic Drug L‐DOPA

et al. 2023

View full text Add to dashboard Cite

Nanozymes are nanomaterials with intrinsic enzyme‐like activity and show high operational stability as compared to native enzymes. They have gathered the attention of researchers due to their unique physico‐chemical properties and diverse applications. In the present study, screening of different nanoparticles (zinc oxide, iron oxide, selenium and titanium oxide) was performed to evaluate their polyphenol oxidase (PPO) activity. PPO is a biotechnologically important enzyme and its application includes wastewater treatment, food processing and synthesis of l‐3,4‐dihydroxyphenylalanine (L‐dopa, a precursor of dopamine neurotransmitter). Out of all nanoparticles used in this study, zinc oxide nanoparticles (ZnO NPs) showed maximum enzyme activity of 75 %. ZnO NPs demonstrated high thermal stability and can be used upto 80°C. The colloidal solution of nanoparticles showed storage stability upto 6 months at room temperature and showed high activity in the pH range of 6–9 as compared to free enzyme. The nanoparticles were reused till 6th cycle retaining more than 80 % oxidase activity. To study its potential as a catalyst, it was used for the synthesis of L‐dopa from L‐tyrosine and a good productivity of 100 mg/L (0.1 g/L) was obtained. Thus, ZnO nanozymes can be used as an alternate to oxidase enzyme for synthesis of this therapeutic drug.

show abstract

l-Dopa synthesis catalyzed by tyrosinase immobilized in poly(ethyleneoxide) conducting polymers

Cited by 22 publications

References 50 publications

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

L-DOPA Synthesis Using Tyrosinase-immobilized on Electrode Surfaces

Aspergillus niger PA2 Tyrosinase Covalently Immobilized on a Novel Eco-Friendly Bio-Composite of Chitosan-Gelatin and Its Evaluation for L-DOPA Production

Nanoparticles Mimicking Oxidase Activity and their Application in Synthesis of Neurodegenerative Therapeutic Drug L‐DOPA

Contact Info

Product

Resources

About