Development of Amperometric Biosensor for Phenolic Compounds Using a Modified Electrode with Poly(GMA-co-MTM) and Laccase

Sulak, Meral Topçu; Erhan, Elif; Keskinler, Bülent; Yılmaz, Faruk; Celik, Asuman

doi:10.1166/sl.2010.1260

Cited by 9 publications

(12 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Laccases catalyze the one-electron oxidation of a wide variety of organic and inorganic substrates, including mono-, di-and polyphenols, and aminophenols, with the concomitant four-electron reduction of oxygen to water. (47,48) In a previous work, we used Trametes Versicolor to modify electrodes, (36) and it was noted that the performance of the laccase-modified electrodes depended on the immobilization method and the immobilization matrix. Therefore, immobilization of laccase was carried out in one pot by entrapment within PPy film during its electrogeneration on the electrode.…”

Section: Response Of Laccase-based Working Electrodes To Phenolmentioning

confidence: 99%

“…In previous work, laccase was immobilized on different copolymer matrices. (19) Carbon nanotubes (CNTs) have received immense attention as an attractive new material with unique physical, electronic and chemical properties, and can be divided into multiwall carbon nanotubes (MWCNTs) and single-wall carbon nanotubes (SWCNTs). CNTs represent an important group of nanomaterials with attractive electronic, chemical, and mechanical properties.…”

Section: Introductionmentioning

confidence: 99%

“…(35) The original method of immobilization is based on enzyme incorporation into the structure of the PB film during its electrochemical growth process. (36)(37)(38) To the best of our knowledge, there is no report on the electropolymerization of PB with MWCNTs, laccase, and pyrrole carried out for phenol detection. To enhance electron transfer between the redox centre of the enzyme and the electrode surface, and hence to increase the biosensor sensitivity, in a simple fabrication procedure, the present work reports the evaluation of novel phenol biosensors based on PB, MWCNTs, and laccase.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Electrochemical Phenol Biosensor Configurations Based on Nanobiocomposites

2012

Sensors and Materials

View full text Add to dashboard Cite

Different biosensor configurations were constructed based on nanobiocomposites for the detection of phenol. The immobilization of laccase (TvLac) was achieved on a glassy carbon (GC) with polypyrrole (PPy), polypyrrole-multiwall carbon nanotube (PPy-MWCNT), and polypyrrole-multiwall carbon nanotube-Prussian blue (PPy-MWCNT-PB) composites via electrochemical polymerization. A comparative study was made of the analytical properties of the biosensors corresponding to the three configurations, namely, GC/PPy-TvLac, GC/PPy-TvLac-MWCNT, and GC/PPy-TvLac-MWCNT-PB. All the configurations indicated that the (TvLac-MWCNT-PB) nanobiocomposites were entrapped within the porous PPy film and resulted in a hybrid film that showed a high electrocatalytic ability toward the oxidation of phenol at a potential of −200 mV vs Ag/AgCl. The GC/PPy-TvLac-MWCNT-PB working electrode gave performance characteristics with high sensitivity (309.1 nA/μM), low detection limit, and good stability. This electrode allowed the determination of phenol in the 0.2-2.56 μM concentration range. The sensitivities (S/N = 3) for phenol obtained from the different working electrodes were found to be 4.56, 91.03, and 309.1 μM, respectively.

show abstract

Section: Response Of Laccase-based Working Electrodes To Phenolmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Electrochemical Phenol Biosensor Configurations Based on Nanobiocomposites

2012

Sensors and Materials

View full text Add to dashboard Cite

show abstract

“…In recent years, the usage of laccase enzyme has been greatly increased and its immobilization is a considerable issue. There are various methods for immobilization of laccase enzyme, including the use of nanoscale supports and a range of encapsulation and covalent methods [12][13][14]. Immobilized laccase in comparison with free enzyme has several advantages such as increased stability, facilitating recovery and purification of enzymes, enzyme reuse and continuous operation of enzymatic processes [4].…”

Section: Introductionmentioning

confidence: 99%

Investigation of Direct and Mediated Electron Transfer of Laccase-Based Biocathode

Jamshidinia

Mashayekhimazar

Ahmadi

et al. 2017

J. Electrochem. Sci. Technol

View full text Add to dashboard Cite

Enzymatic fuel cells are promising low cost, compact and flexible energy resources. The basis of enzymatic fuel cells is transfer of electron from enzyme to the electrode surface and vice versa. Electron transfer is done either by direct or mediated electron transfer (DET/MET), each one having its own advantages and disadvantages. In this study, the DET and MET of laccase-based biocathodes are compared with each other. The DET of laccase enzyme has been studied using two methods; assemble of needle-like carbon nanotubes (CNTs) on the electrode, and CNTs/Nafion polymer. MET of laccase enzyme also is done by use of ceramic electrode containing, ABTS (2,2'-azino-bis [3-ethylbenzthiazoline-6-sulphonic acid]) /sol-gel. Cyclic voltammetric results of DET showed a pair of well-defined redox peaks at 200 µA and 170 µA in a solution containing 5 and 10 µM o-dianisidine as a substrate for needle-like assembled CNTs and CNTs-Nafion composite respectively. In MET method using sol-gel/ABTS, the maximum redox peak was 14 µA in the presence of 15 M solution o-dianisidine as substrate. The cyclic voltammetric results showed that laccase immobilization on needle-like assembled CNTs or CNTs-Nafion is more efficient than the sol-gel/ABTS electrode. Therefore, the expressed methods can be used to fabricate biocathode of biofuel cells or laccase based biosensors.

show abstract

“…Laccases are able to catalyze direct oxidation of ortho-and para-diphenols, amino phenols, polyphenols, polyamines, and aryl diamines as well as some inorganic ions [2]. Due to its broad substrate specificity, laccase has great potential in varied environmental applications including pulp delignification, textile dye bleaching, xenobiotics degradation and biopolymer modification [3][4][5]. Deuteromycetes fungi possess more advantages in regards to producing laccase, such as simple life cycle, short growth phase and facility to genetic reconstruction.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Fermentation Parameters for Laccase Production by a Novel Deuteromycete Fungus Myrothecium Verrucaria NF-05 Using Response Surface Methodology

Zhao¹,

Sun²,

Du³

et al. 2015

Proceedings of the 2nd International Conference on Civil, Materials and Environmental Sciences

View full text Add to dashboard Cite

To obtain the maximum production of laccase from a novel deuteromycete fungus Myrothecium verrucaria NF-05, optimization of fermentation parameters was performed. Central composite design and response surface analysis revealed the optimum concentration of glucose, CuSO 4 and gallic acid to be 26.47 g L-1 , 236.3 µM, and 138.4 µM, respectively. This optimization strategy led to the enhancement of laccase production from 12.00 to 19.94 U mL-1 , 1.66-fold increase.

show abstract

Development of Amperometric Biosensor for Phenolic Compounds Using a Modified Electrode with Poly(GMA-co-MTM) and Laccase

Cited by 9 publications

References 0 publications

Electrochemical Phenol Biosensor Configurations Based on Nanobiocomposites

Electrochemical Phenol Biosensor Configurations Based on Nanobiocomposites

Investigation of Direct and Mediated Electron Transfer of Laccase-Based Biocathode

Optimization of Fermentation Parameters for Laccase Production by a Novel Deuteromycete Fungus Myrothecium Verrucaria NF-05 Using Response Surface Methodology

Contact Info

Product

Resources

About