Fatma Arslan

An Amperometric Biosensor for Uric Acid Determination Prepared From Uricase Immobilized in Polyaniline-Polypyrrole Film

A new amperometric uric acid biosensor was developed by immobilizing uricase by a glutaraldehyde crosslinking procedure on polyaniline-polypyrrole (pani-ppy) composite film on the surface of a platinum electrode. Determination of uric acid was performed by the oxidation of enzymatically generated H2O2 at 0.4 V vs. Ag/AgCl. The linear working range of the biosensor was 2.5×10-6 × 8.5×10-5 M and the response time was about 70 s. The effects of pH, temperature were investigated and optimum parameters were found to be 9.0, 55 °C, respectively. The stability and reproducibility of the enzyme electrode have been also studied.

An amperometric biosensor for uric acid determination prepared from uricase immobilized in polypyrrole film.

In order to prepare a biosensor for the determination of uric acid, electropolymerization of pyrrole on Pt surface was carried out with an electrochemical cell containing pyrrole, ferrocene (as a electron mediator) and tetrabutylammonium tetrafluoroborat in acetonitrile by cyclic voltammetry between 0.0 and 1.0 V (vs. Ag/AgCl) at a scan rate of 50 mV/s upon Pt electrode. Uricase was immobilized by a glutaraldehyde/gelatine croslinking procedure on to polypyrrole film after the electropolymerization processes. The response of the biosensor against uric acid was measured after 330 seconds following the application of a constant potential of +0.7 V (vs. Ag/AgCl). The resulting biosensor exhibits excellent electrocatalysis for the uric acid. The amperometric determination is based on the electrochemical detection of H2O2, which is generated in enzymatic reaction of uric acid. The sensor responds to uric acid with a detection limit of 5.0 × 10−7 M. The sensor remains relatively stable for 5 weeks. Interference effect were investigated on the amperometric response of the biosensor. Determination of uric acid was carried out in the biological fluids by biosensor.

Immobilization of invertase attached to a granular dimer acid-co-alkyl polyamine

Abstract Invertase was immobilized onto the granular dimer acid-co-alkyl polyamine after activation with carbodiimide. The Km value for immobilized enzyme (53.6 mM) was much greater than that of the free enzyme (20.6 mM). Vmax values were 6.44×10−5 mol dm−3 min−1 and 5.45×10−5 mol dm−3 min−1 for free and bound, respectively. The optimal pH values for free and covalently bonded enzymes were 4.56 and 5.50, respectively. The optimum temperature for both free and covalent invertase was 55°C. The enzyme activities, after storage for 1 month, were found to be 21.0 and 99.0% of the initial activity values for free and covalently bonded, respectively. The immobilized enzyme that was used 50 times in 5 days in repeated batch experiments showed 100% of its original activity.

An Amperometric Biosensor for Glucose Determination Prepared from Glucose Oxidase Immobilized in Polyaniline-Polyvinylsulfonate Film

In this study, a novel amperometric glucose biosensor with immobilization of glucose oxidase on electrochemically polymerized polyaniline-polyvinylsulphonate (Pani-Pvs) films has been accomplished via the entrapment technique. Electropolymerization of aniline on the Pt surface of the Pt electrode was carried out at constant potential (0.75 V, vs. Ag/AgCl) using an electrochemical cell containing aniline and polyvinylsulphonate. Firstly, the optimum working conditions for preparing polyaniline-polyvinylsulfonate films were investigated. Determination of glucose was carried out by the oxidation of enzymatically produced H2O2 at 0.4 V vs. Ag/AgCl. The effects of pH and temperature were investigated and the optimum pH value was found to be 7.5. The storage stability and operational stability of the enzyme electrode were also studied. The results show that 75% of the response current was retained after 16 activity assays. The prepared glucose biosensor retained 80.6% of initial activity after 40 days when stored in 0.1 M phosphate buffer solution at 4 °C.

An Amperometric Biosensor for Xanthine Determination Prepared from Xanthine Oxidase Immobilized in Polypyrrole Film

In order to prepare a biosensor for the determination of xanthine, electropolymerization of pyrrole on Pt surface was carried out with an electrochemical cell containing pyrrole, ferrocene (as a electron mediator) and tetrabutylamonium tetrafluoroborat in acetonitrile by cyclic voltammetry between 0.0 and 0.9 V (vs SCE) at a scan rate of 50 mV/s upon Pt electrode. Xanthine oxidase was immobilized by a glutaraldehyde/bovine serum albumin (BSA) crosslinking procedure on to polypyrrole film after the electropolymerization processes. The response of the biosensor against xanthine was measured after 3–4 min following the application of a constant potential of +0.7 V (vs SCE). The resulting biosensor exhibits excellent electrocatalysis for the xanthine. The amperometric determination is based on the electrochemical detection of H2O2, which is generated in enzymatic reaction of xanthine. The effect of various experimental conditions was examined for the determination of the analytical performance. The sensor responds to xanthine with a detection limit of 1.0 × 10−6 M. The response current increases linearly with xanthine concentration up to 4.0 × 10−4 M. The sensor remains relatively stable for 45 days.

The effect of gel composition on the adsorption of invertase on poly(acrylamide/maleic acid) hydrogels

Abstract The effects of external stimuli such as pH of solution, temperature, substrate concentration of solution and storage stability on the invertase adsorption capacity of poly(acrylamide/maleic acid) [P(AAm/MA)] hydrogels, synthesized by gamma irradiation of ternary mixtures of AAm/MA/Water, were investigated. The adsorption capacities of the hydrogels were found to increase from 4.0 to 13.3 mg invertase/g dry gel with increasing amount of MA in the gel system, while P(AAm) gel adsorbed only 3.1 mg invertase/g dry gel. Kinetic parameters were calculated as 20.6 mM for K m and 6.44×10 −5 mol/dm 3 min for V max for free enzyme and in the range of 23.6–57.7 mM for K m and 8.62×10 −5 –1.05×10 −4 mol/dm 3 min for V max , depending on the amount of MA in the hydrogel. Enzyme activities were found to increase from 50.0 to 74.0% with increasing amount of MA in the gel system and retained their activities for one month storage. The enzyme activities, after storage at 4°C for one month, were found to be 21.0 and 50.0–74.0% of the initial activity values for free and adsorbed enzyme, respectively. The optimal pH values for free and adsorbed enzymes were determined as 4.56 and 4.56–5.00. The optimum temperature for free and adsorbed enzymes was 55°C. Adsorption studies show that, not only gel composition but also the stimuli, temperature and pH of the solution, play important roles on the invertase adsorption capacity of poly(AAm/MA) hydrogels.

Synthesis, characterization, antibacterial activities and carbonic anhydrase enzyme inhibitor effects of new arylsulfonylhydrazone and their Ni(II), Co(II) complexes

Ethane sulfonic acide hydrazide (esh: CH(3)CH(2)SO(2)NHNH(2)) derivatives as 5-methylsalicyl-aldehydeethanesulfonylhydrazone (5msalesh), 5-methyl-2-hydroxyacetophenoneethane sulfonylhydrazone (5mafesh) and their Ni(II), Co(II) complexes have been synthesized for the first time. The structure of these compounds has been investigated by elemental analysis, FT-IR, (1)H NMR, (13)C NMR, LC/MS, UV-vis spectrophotometric method, magnetic susceptibility, thermal studies and conductivity measurements. The antibacterial activities of synthesized compounds were studied against Gram positive bacteria; Staphylococcus aureus, Bacillus subtilis, Bacillus magaterium and Gram negative bacteria; Salmonella enteritidis, Escherichia coli by using the microdilution broth method. The biological activity screening showed that ligands have more activity than complexes against the tested bacteria. The inhibition activities of these compounds on carbonic anhydrase II (CA II) have been investigated by comparing IC(50) and K(i) values and it has been found that 5msalesh and its complexes have more enzyme inhibition efficiency than other compounds.

Preparation of carbon paste electrodes including poly(styrene) attached glycine-Pt(IV) for amperometric detection of glucose.

In this study, a novel carbon paste electrode that is sensitive to glucose was prepared using the nanoparticles modified (4-Formyl-3-methoxyphenoxymethyl) with polystyren (FMPS) with L-Glycine-Pt(IV) complexes. Polymeric nanoparticles having Pt(IV) ion were prepared from (4-Formyl-3-methoxyphenoxymethyl) polystyren, glycine and PtCl4 by template method. Glucose oxidase enzyme was immobilized to a modified carbon paste electrode (MCPE) by cross-linking with glutaraldehyde. Determination of glucose was carried out by oxidation of enzymatically produced H2O2 at 0.5 V vs. Ag/AgCl. Effects of pH and temperature were investigated, and optimum parameters were found to be 8.0 and 55°C, respectively. Linear working range of the electrode was 5.0×10(-6)-1.0×10(-3) M, R(2)=0.997. Storage stability and operational stability of the enzyme electrode were also studied. Glucose biosensor gave perfect reproducible results after 10 measurements with 2.3% relative standard deviation. Also, it had good storage stability (gave 53.57% of the initial amperometric response at the end of 33th day).

New aromatic/heteroaromatic propanesulfonylhydrazone compounds: Synthesis, physical properties and inhibition studies against carbonic anhydrase II (CAII) enzyme

Some new aromatic/heteroaromatic propanesulfonylhydrazone derivatives (1-8) were synthesized and characterized by elemental analyses, FT-IR, (1)H NMR, (13)C NMR, LC/MS techniques. The geometry optimizations and spectral calculations were performed by using DFT/B3LYP/6-311G(d,p) basis set in Gaussian 09 program. The inhibition activities of the synthesized compounds on carbonic anhydrase II (CAII) isoenzyme have been investigated by comparing IC50 values. Acetazolamide (5-acetamido-1,3,4-thiadiazole-2-sulfonamide) AAZ, a clinically used in CAII inhibition has also been investigated as standard inhibitor. The best aromatic/heteroaromatic propanesulfonylhydrazone inhibitors of this isoform were o-aminobenzaldehydepropanesulfonylhydrazone (1) and thiophenecarboxyaldehyde propanesulfonylhydrazone (5) having the same IC50 (0.55 mM) value. The molecular descriptors for propanesulfonylhydrazones were obtained to develop structure activity relationship (SAR) model between experimental IC50 values and the molecular descriptors calculated by PM3-based SAR models in Hyperchem 8, respectively. The obtained models confirm the good carbonic anhydrase II (CAII) inhibition activity of the propanesulfonylhydrazone derivatives. The selected descriptors are sensitive both to the imine (CH=N) and NH2 groups that are responsible from higher activities of (1) and (5) in their series.

Glucose biosensor based on the immobilization of glucose oxidase on electrochemically synthesized polypyrrole-poly(vinyl sulphonate) composite film by cross-linking with glutaraldehyde

Abstract In this study, a novel amperometric glucose biosensor was developed by immobilizing glucose oxidase (GOX) by cross-linking via glutaraldehyde on electrochemically polymerized polypyrrole-poly(vinyl sulphonate) (PPy–PVS) films on the surface of a platinum (Pt) electrode. Electropolymerization of pyrrole and poly(vinyl sulphonate) on the Pt surface was carried out with an electrochemical cell containing pyrrole and poly(vinyl sulphonate) by cyclic voltammetry between −1.0 and + 2.0 V (vs.Ag/AgCl) at a scan rate of 50 mV/s upon the Pt electrode. The amperometric determination was based on the electrochemical detection of H2O2 generated in enzymatic reaction of glucose. Determination of glucose was carried out by the oxidation of enzymatically produced H2O2 at 0.4 V vs. Ag/AgCl. The effects of pH and temperature were investigated and optimum parameters were found to be 7.5 and 65°C, respectively. The effect of working potential was investigated and optimum potential was determined to be 0.4 V. The operational stability of the enzyme electrode was also studied. The response of the PPy/PVS-GOX glucose biosensor exhibited good reproducibility with a relative standard deviation (RSD) of 2.48%. The glucose biosensor retained 63% of initial activity after 93 days when stored in 0.1 M phosphate buffer solution of pH 7.5 at 4°C. With the low operating potential, the biosensor demonstrated little interference from the possible interferants.