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Biomedical subjects

Suna Timur

Publications and source records attributed to Suna Timur.

9 recordsLinked to original sources

Electrical wiring of Pseudomonas putida and Pseudomonas fluorescens with osmium redox polymers.

Two different flexible osmium redox polymers; poly(1-vinylimidazole)12-[Os-(4,4'-dimethyl-2,2'-di'pyridyl)2Cl2](2+/+) (osmium redox polymer I) and poly(vinylpyridine)-[Os-(N,N'-methylated-2,2'-biimidazole)3](2+/3+) (osmium redox polymer II) were investigated for their ability to efficiently "wire" Pseudomonas putida ATCC 126633 and Pseudomonas fluorescens (P. putida DSM 6521), which are well-known phenol degrading organisms, when entrapped onto cysteamine modified gold electrodes. The two Os-polymers differ in redox potential and the length of the side chains, where the Os(2+/3+)-functionalities are located. The bacterial cells were adapted to grow in the presence of phenol as the sole source of organic carbon. The performance of the redox polymers as mediators was investigated for making microbial sensors. The analytical characteristics of the microbial sensors were evaluated for determination of catechol, phenol and glucose as substrates in both batch analysis and flow analysis mode.

2,2'-Dipyridyl↗

Graphite epoxy composite electrodes modified with bacterial cells.

The modification of a graphite-epoxy composite electrode (GECE) with bacterial cells along with an analytical application are presented. Pseudomonas putida DSM 50026 was used as a biological component and the measurement was based on the respiratory activity of the cells. The optimization of working conditions of resulting biosensor (including pH and temperature) was conducted and the limit of detection was calculated as 7 microM phenol based on the signal to noise ratio. Then the system was applied for xenobiotic detection. Resulting sample signals were found to be very similar with the standard solutions having the same concentration while the recoveries of the spiked samples were close to 100%.

Biosensing Techniques↗

Effects of mediators on the laccase biosensor response in paracetamol detection.

An enzyme electrode suitable for paracetamol detection was developed by immobilizing laccase on a dissolved-oxygen probe surface. The immobilization procedure was achieved by means of gelatin, which was then cross-linked with glutaraldehyde. The measurement was based on the detection of oxygen consumption in relation to analyte oxidation. The optimum experimental conditions for the biosensor were investigated and the system was calibrated for paracetamol. Also the effects of three different mediators, namely HBT (1-hydroxybenzotriazole), VLA [violuric acid (5-isonitrosobarbituric acid)] and TEMPO (2,2',6,6'-tetramethylpiperidine-N-oxyl radical) were tested for the biosensor's response. As a result, it was observed that HBT has a remarkable effect on the signal by providing more oxygen consumption during the enzymatic reaction. A linear relationship between sensor responses and analyte concentrations was obtained over the concentration range 2.0-15.0 microM, whereas, in the presence of the mediator HBT, this range became 0.5-3.0 microM.

Acetaminophen↗

Laccase biosensors based on mercury thin film electrode.

A biosensor was developed by immobilizing laccase onto mercury thin film electrode (MTFE) by means of gelatin that is then crosslinked with glutaraldehyde. Mercury thin film (MTF) was deposited onto glassy carbon electrode (GCE) and the obtained biosensor was utilized for the determination of phenolic compounds. The measurement was based on the amperometric detection of oxygen consumption in relation to analyte oxidation. The optimum experimental conditions for the biosensor were investigated and the system was calibrated for both catechol and phenol. A linear relationship between sensor responses and analyte concentrations was obtained in concentration range between 0.5 x 10(-6)-5.0 x 10(-6)M for catechol and 2.5 x 10(-6)-2.0 x 10(-6)M for phenol, respectively. Mercury thin film was also formed onto the surface of screen printed graphite electrodes and applied for the catechol detection. The linearity was observed in concentration range between 2.5 x 10(-6)-3.0 x 10(-5)M.

Biosensing Techniques↗

Inhibition of alpha-glucosidase by aqueous extracts of some potent antidiabetic medicinal herbs.

Diabetes mellitus is one of the most prevalant diseases of adults. Agents with alpha-glucosidase inhibitory activity have been useful as oral hypoglycemic drugs for the control of hyperglycemia in patients with type 2; noninsulin-dependent, diabetes mellitus (NIDDM). Investigation of some medicinal herbs: Urtica dioica, Taraxacum officinale, Viscum album, and Myrtus communis with alpha-glucosidase inhibitor activity was conducted to identify a prophylactic effect for diabetes in vitro. All plants showed differing potent alpha-glucosidase inhibitory activity. However, Myrtus communis strongly inhibited the enzyme (IC50 = 38 microg/mL). The inhibitory effect of these plants and some common antidiabetic drugs against the enzyme source (baker's yeast, rabbit liver, and small intestine) were also searched. Approximately all inhibitors used in this study showed quite different inhibitory activities, according to alpha-glucosidase origins. Furthermore, subsequent separation of the active material from Myrtus communis by HPLC showed that only one fraction acted as an a-glucosidase inhibitor.

Enzyme Activation↗

Immobilized jerusalem artichoke (Helianthus tuberosus) tissue electrode for phenol detection.

A tissue based biosensor for the determination of phenol was developed by using Jerusalem artichoke (Helianthus tuberosus) in combination with a dissolved oxygen (DO) probe. The tissue electrode response depends linearly on phenol concentration between 0.002 and 0.0101 microM in 10 min response time. Maximum electrode response was found in phosphate buffer at pH 8.0 and 35 degrees C. The reproducibility of the enzyme electrode was also tested by using standard phenol solutions (0.005 microM). The standard deviation (SD) and variation coefficient (cv) were calculated as +/- 1.4 x 10(-4) microM and 3.1%, respectively.

Biosensing Techniques↗

Acetylcholinesterase (AChE) electrodes based on gelatin and chitosan matrices for the pesticide detection.

Enzyme electrodes for the determination of organophosphate pesticides were developed by using acetylcholinesterase (AChE) in combination with a pH electrode. AChE was immobilized on the surface of pH electrode by using gelatin and chitosan membranes, respectively. The measurement system is based on potentiometric detection of the inhibiting properties of organophosphates on enzyme activity. The phosphate buffer (2.5mM, pH 8.0) and the borate buffer (2.5mM, pH 8.5) at 25 degrees C were established as providing the optimum conditions for the gelatin and chitosan based biosensor systems, respectively. Furthermore, operational, thermal, and organic phase stabilities were also tested. Linear ranges for different organophosphates such as malathion, parathion-methyl, and methamidophos were detected by using both types of biosensor system. Moreover, as well as accuracy, the regeneration conditions by using pyridine-2-aldoximethiodide (PAM-2) as a reactivating agent for the inhibited electrodes were also investigated.

Acetylcholinesterase↗

An enzyme electrode based on lipoxygenase immobilized in gelatin for selective determination of essential fatty acids.

An enzyme electrode for the specific determination of omega-3 and omega-6 fatty acids from the mixture of essential fatty acids (EFAs) was developed by using lipoxygenase (LOX) (EC 1.13.11.12) from soy beans in combination with a dissolved oxygen (DO) probe. The enzyme electrode showed different sensitivities for linoleic (LA) and alpha-linolenic acids (ALA), the most common essential fatty acids. Enzyme electrode response depends linearly on LA concentration between 12.8-160.5 microM and ALA concentration between 3.8-18.9 microM in borate buffer, 0.2 M at pH 9.0. However, in phosphate buffer 0.2 M at pH 6.0 linearity is in the range of 7.5-22.5 microM of ALA concentration at 5 minutes response times. Moreover, maximum electrode response was found in borate buffer at pH 9.0 and 30 degrees C.

Biosensing Techniques↗

Arginine selective biosensor based on arginase-urease immobilized in gelatin.

Arginase and urease enzymes were immobilized on the surface of pH electrode by using gelatin membrane which is then cross-linked with glutaraldehyde. Sensor response was maximum when 2.5 mM, Tris-HCl buffer (pH 8.5) was used at 25 degrees C. The biosensor response depends linearly on arginine concentration between 0.025-0.310 mM with response time 10 min. Furthermore, application of the system for the arginine detection in serum samples was also tested.

Arginase↗