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PubMed2003

Studies on the electrochemical performance of glucose biosensor based on ferrocene encapsulated ORMOSIL and glucose oxidase modified graphite paste electrode.

The electrochemical performance of a new glucose biosensor is reported. The glucose biosensor is developed using glucose oxidase (GOD) and ferrocene encapsulated palladium (Pd)-linked organically modified sol-gel glass (ORMOSIL) material incorporated within graphite paste electrode. The ORMOSIL material incorporated within graphite paste electrode behaves as an excellent electrocatalyst for the oxidation of enzymatically reduced GOD. The electrochemical behavior of new glucose biosensor has been examined by cyclic volammetry and amperometric measurements. The bioelectrocatalysis of ORMOSIL embedded within graphite paste as a function of storage time and varying concentration of ORMOSIL is reported. The initial amperometric response on glucose sensing is recorded to be 145 microA at 15% (w/w) concentration of the ORMOSIL which is decreased to 20 microA at 5% of the same keeping GOD concentration constant. The variation of electrochemical behavior of the ORMOSIL embedded within graphite paste as a function of time has also been studied based on cyclic voltammetry. The voltammograms showing the reversible electrochemistry of ORMOSIL encapsulated ferrocene is changed into a plateau shape as a function of time, however, the electrocatalytic behavior is still retained. The practical usability of new glucose sensor has been compared with earlier developed glucose sensor. The sensitivity, response time and linearity of the new glucose biosensor are found to be excellent over earlier reported glucose biosensor. The amperometric response, calibration curve and practical applications of new glucose sensor are reported.

Biosensing Techniques↗
PubMed2006

Purification and thermodynamic characterization of glucose oxidase from a newly isolated strain of Aspergillus niger.

An intracellular glucose oxidase (GOD) was isolated from the mycelium extract of a locally isolated strain of Aspergillus niger NFCCP. The enzyme was partially purified to a yield of 28.43% and specific activity of 135 U mg(-1) through ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The enzyme showed high specificity for D-glucose, with a K(m) value of 25 mmol L(-1). The enzyme exhibited optimum catalytic activity at pH 5.5. Optimum temperature for GOD-catalyzed D-glucose oxidation was 40 degrees C. The enzyme displayed a high thermostability having a half-life (t(1/2)) of 30 min, enthalpy of denaturation (H*) of 99.66 kJ mol(-1), and free energy of denaturation (G*) of 103.63 kJ mol(-1). These characteristics suggest that GOD from A. niger NFCCP can be used as an analytical reagent and in the design of biosensors for clinical, biochemical, and diagnostic assays.

Aspergillus niger↗
PubMed2005

An electrochemical investigation of glucose oxidase at a CdS nanoparticles modified electrode.

The direct electrochemistry of glucose oxidase (GOD) adsorbed on a CdS nanoparticles modified pyrolytic graphite electrode was investigated, where the enzyme demonstrated significantly enhanced electron-transfer reactivity. GOD adsorbed on CdS nanoparticles maintained its bioactivity and structure, and could electro-catalyze the reduction of dissolved oxygen, which resulted in a great increase of the reduction peak current. Upon the addition of glucose, the reduction peak current decreased, which could be used for glucose detection. Performance and characteristics of the fabricated glucose biosensor were assessed with respect to detection limit, sensitivity, storage stability and interference exclusion. The results showed that the fabricated biosensor was sensitive and stable in detecting glucose, indicating that CdS nanoparticle was a good candidate material for the immobilization of enzyme in glucose biosensor construction.

Biosensing Techniques↗
PubMedDate not supplied

[Isolation and properties of glucose oxidase from Penicillum funiculosum 433].

A method for isolation of extracellular glucose oxidase from Penicillium funiculosum 433 and its purification is proposed. The enzymatic preparation was produced with a yield of 56% and a specific activity of 3730 AU per 1 mg protein. The enzyme studied displayed a high thermostability, resistance to metal ions, and performance in a wide pH range and was equal in its properties to foreign analogues.

Chromatography, Liquid↗
PubMed2001

[Cloning and expression of Aspergillus niger glucose oxidase gene in methylotrophic yeast].

The DNA fragment encoding A. niger glucose oxidase was amplified by PCR using A. niger genomic DNA as template, and was cloned into vector of pPIC9 for expression in Pichia pastoris. When transformed into methylotrophic yeast Pichia pastoris GS115, The constructed plasmid pPICGOD1 directed the synthesis and secretion of functionally active GOD. After induction in MM medium for 4 days, the GOD activity in the medium reached 30-40 u/mL. SDS-PAGE revealed that recombinant yeast GOD was expressed up to 60%-70% of the total soluble protein, and the secreted GOD could be purified to electrophoretic homogeneity with one purification step using Q Sepharose Fast Flow ion exchange chromatography. The recombinant yeast GOD had very high catalytic activity, showed about 1.6-fold increase of specific activity over the commercial A. niger GOD. Kinetic analysis clearly demonstrated that recombinant yeast GOD showed similar substrate affinity for glucose to A. niger GOD, but the turnover number of the GOD from yeast was determined to be much higher than that of A. niger GOD. In addition, the linear range of glucose electrode made with recombinant yeast GOD was efficiently widened due to the high catalytic activity of yeast GOD.

Aspergillus niger↗
PubMed1990

Targeted killing of yeast expressing a HIV-1 peptide by antibody-conjugated glucose oxidase and horseradish peroxidase.

The epitope recognized by monoclonal antibody directed against the HIV-1 recombinant gp160 protein was precisely delineated by using a number of peptides comprising amino acid positions 302-330 of the protein. Two different enzymes, glucose oxidase and horseradish peroxidase, were then coupled to distinct antibody molecules and the efficacy of the immunoenzymes in killing yeast cells which express the recognized peptide was evaluated by flow cytometry analysis. The antibody-glucose oxidase conjugate alone was cytotoxic only at large doses (over 35 micrograms/ml) while in the presence of the antibody-horseradish peroxidase conjugate, killing was observed at nine times lower concentrations (4 micrograms/ml). The procedure described here may provide a new immunotherapy tool for microbial infection.

Amino Acid Sequence↗
PubMed2006

Designing an enzymatic oscillator: bistability and feedback controlled oscillations with glucose oxidase in a continuous flow stirred tank reactor.

The reaction of glucose with ferricyanide catalyzed by glucose oxidase from Aspergillus niger gives rise to a wide range of bistability as the flow rate is varied in a continuous flow stirred tank reactor. Oscillations in pH can be obtained by introducing a negative feedback on the autocatalytic production of H+ that drives the bistability. In our experiments, this feedback consists of an inflow of hydroxide ion at a rate that depends on [H+] in the reactor as k0[OH-]0[H+]/(K+[H+]). pH oscillations are found over a broad range of enzyme and ferricyanide concentrations, residence times (k0 (-1)), and feedback parameters. A simple mathematical model quantitatively accounts for the experimentally found oscillations.

Aspergillus niger↗
PubMed2004

Effect of a modification site on the electron-transfer reaction of glucose oxidase hybrids modified with phenothiazine via a poly(ethylene oxide) spacer.

Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. A fast oxidation of FADH2/FADH by PT+ with the aid of the local motion of a hydrophilic, long, flexible PEO spacer is achieved for the GOx-(PT-PEONH2) hybrids and yields greater electron-transfer (ET) rates than that for GOx-(PTNH2) hybrids, in which the PT groups are directly bonded to the GOx surface. The ET rate of GOx-(PT-PEONH2) hybrids depends on the molecular weight of PT-PEONH2, and the maximum is obtained at a molecular weight of 3000. The ET rates of GOx hybrids are compared in terms of the location of the PT modification and the length and structure of the spacer chain connection of the PT mediator to a surface amino acid residue. Greater ET rates are obtained for the modification at aspartic and glutamic acid residues than for the lysine modification when the PT groups are bonded directly or via a short PEO spacer chain. In contrast, no advantage of aspartic and glutamic acid residues over lysine residues in generating a fast oxidation of FADH2/FADH by PT+ is observed for GOx hybrids in which the PT groups are attached via longer PEO spacers. The long PEO spacer is able to compensate the disadvantage of lysine residues locating far from the FAD center in GOx hybrids whose mediation reactions are based on the so-called wipe mechanism.

Electron Transport↗
PubMed2005

A novel glucose biosensor based on the nanoscaled cobalt phthalocyanine-glucose oxidase biocomposite.

We report on the utilization of a novel nanoscaled cobalt phthalocyanine (NanoCoPc)-glucose oxidase (GOD) biocomposite colloid to create a highly responsive glucose biosensor. The biocomposite colloid is constructed under enzyme-friendly conditions by adsorbing GOD molecules on CoPc nanoparticles via electrostatic interactions. The glucose biosensor can be easily achieved by casting the biocomposite colloid on a pyrolytic graphite electrode (PGE) without any auxiliary matter. It has been found that GOD can be firmly immobilized on PGE surface and maintain its bioactivity after conjugating with NanoCoPc. NanoCoPc displays intrinsic electrocatalytic ability to the oxidation of the product of enzymatic reaction H2O2 and shows a higher catalytic activity than that of bulk CoPc. Under optimal conditions, the biosensor shows a wide linear response to glucose in the range of 0.02-18 mM, with a fast response (5s), high sensitivity (7.71 microA cm(-2) mM(-1)), as well as good thermostability and long-term life. The detection limit was 5 microM at 3 sigma. The general interferences coexisted in blood except ascorbic acid and L-cysteine do not affect glucose determination, and further coating Nafion film on the surface of the biosensor can effectively eliminate the interference from ascorbic acid and L-cysteine. The biosensor with Nafion film has been used for the determination of glucose in serum with an acceptable accuracy.

Biosensing Techniques↗
PubMed1991

Enhancement of the antitumor effect of glucose oxidase by combined administration of hydrogen peroxide decomposition inhibitors together with an oxygenated fluorocarbon.

Glucose oxidase (GO) catalyzes the conversion of beta-D-glucose and molecular oxygen to D-glucono-delta-lactone and H2O2. H2O2 produced by GO was effective in preventing tumor growth in mice bearing not only ascites tumor but also solid tumor. The effect of GO was enhanced by the combined administration of catalase inhibitors such as 3-aminotriazole, hydroxylamine and sodium azide or the GSH synthesis inhibitor buthionine-(S,R)-sulfoximine in vivo. The cytolytic activity of GO against T-24 cultured cells in vitro was also enhanced by addition of these inhibitors together with GO. In the peritoneal cavity of mice the antitumor effect of GO seemed to be dependent on the amount of oxygen released from oxygenated fluorocarbon-43 (FC-O2), an oxygen-supplying substance. Furthermore, the combined administration of H2O2-decomposing enzyme inhibitors and FC-O2 synergistically enhanced the antitumor effect of GO. These results suggest that GO is suitable for antitumor chemotherapy and that the use of inhibitors of H2O2-decomposing enzymes and FC-O2 potentiated the GO therapy.

Animals↗
PubMed1985

Glucose oxidase sticks and cerebrospinal fluid rhinorrhea.

The recognition of cerebrospinal leakage from a fistula is an important consideration for any physician caring for a head-injured population. Several procedures including radiographic, intrathecal dye, nuclear medicine tracer studies, computerized tomography with metrizamide injection, and immunological fixation have been reported to help in the diagnosis. Introduction of glucose oxidase test sticks has been traditionally touted to be a reliable bedside indicator of CSF rhinorrhea; this case study demonstrates a falsely negative result from glucose oxidase sticks.

Adult↗
PubMed1981

Glucose oxidase immunoenzyme methodology as a substitute for fluorescence microscopy in the clinical laboratory.

Enzymes as markers for antigens or antibodies in immunohistochemical procedures have several advantages over commonly used fluorochrome labels. These include use of a regular light microscope and the ability to get permanently stable slide preparations. Glucose oxidase (EC 1.1.2.3.4), being absent in mammalian tissue, provides no background staining, such as that seen with the commonly used horseradish peroxidase (EC 1.11.1.7) owing to peroxidase-like activity in tissues. A glucose oxidase histochemical method is detailed that is useful for detection of human antibodies; it can be easily used in clinical laboratories as a substitute for fluorescent techniques.

Animals↗
PubMed2001

Layer-by-layer self-assembly of glucose oxidase and Os(Bpy)2CIPyCH2NH-poly(allylamine) bioelectrode.

The uptake of glucose oxidase (GOx) onto a polycationic redox polymer (PAA-Os)-modified surface, by adsorption from dilute aqueous GOx solutions, was followed by the quartz crystal microbalance (QCM) and shows double exponential kinetics. The electrochemistry of the layer-by-layer-deposited redox-active polymer was followed by cyclic voltammetry in glucose-free solutions, and the enzyme catalysis mediated by the redox polymer was studied in beta-D-glucose-containing solutions. AFM studies of the different layers showed the existence of large two dimension enzyme aggregates on the osmium polymer for 1 microM GOx and less aggregation for 50 nM GOx solutions. When the short alkanethiol, 2,2'-diaminoethyldisulfide was preadsorbed onto gold, a monoexponential adsorption law was observed, and single GOx enzyme molecules could be seen on the surface where the enzyme was adsorbed from 50 nM GOx in water.

Biosensing Techniques↗
PubMed2001

A stable glucose biosensor prepared by co-immobilizing glucose oxidase into poly(p-chlorophenol) at a platinum electrode.

An amperometric glucose biosensor was successfully developed by electrochemical polymerization of p-chlorophenol (4-CP) at a Pt electrode in the presence of glucose oxidase. The amperometric response of this biosensor to hydrogen peroxide, formed as the product of enzymatic reaction, was measured at a potential of 0.6 V (vs. SCE) in phosphate buffer solution. The performances of sensors, prepared at different monomer concentrations and polymerization potentials, were investigated in detail. The biosensor prepared under optimal conditions had a linear response to glucose ranging from 2.5 x 10(-4) to 1.5 x 10(-2) mol L(-1) with a correlation coefficient of 0.997 and a response time of less than 2 s. Substrate selectivity of the polymer-based enzyme electrode was tested for coexisting interferents such as uric acid and ascorbic acid, and no discernible response was observed. After 90 days, the response of the biosensor remained almost unchanged, indicating very good stability.

Biosensing Techniques↗
PubMed2005

Determination of serum glucose using co-immobilized glucose oxidase and peroxidase onto arylamine glass beads affixed on a plastic strip.

Glucose oxidase (GOD) from Aspergillus niger and horseradish peroxidase (POD) were co-immobilized onto arylamine glass beads affixed on a plastic strip with a conjugation yield of 28.2 mg/g and 43% retention of their initial specific activity. The coimmobilized enzymes showed maximum activity at pH 7.5 when incubated at 37 degrees C for 15 min. A simple, specific and sensitive method for discrete analysis of the serum glucose was developed employing this strip. The minimum detection limit of the method was 5 mg/dl. Within and between assay coefficient of variations for the serum were <5.6% and <10.6% (n = 6) respondely. A good correlation (r = 0.943) was found between the glucose values obtained by the enzyme colorimetric method employing free GOD and POD and the present method. The strip lost 50% of its initial activity after its 150 regular uses for a period of one month, when stored in reaction buffer at 4 degrees C. The method is cost-effective than the enzymic colorimetric method, as the enzyme strip is reusable.

Adult↗