Effect of periodate oxidation on the structure and properties of glucose oxidase

Hayashi, Sueko; Koga, Kunimasa

doi:10.1016/0005-2744(76)90084-x

Cited by 112 publications

(69 citation statements)

References 25 publications

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“…Glucose oxidase (GOD, EC 1.1.3.4), with a molecular weight of 152 000 -186 000 Da, is the typical representative of flavo enzymes, and consists of two identical subunits, each containing a redox center of flavin adenine dinucleotide (FAD) [10]. Mainly because of its biocatalytic activity toward glucose oxidation and commercial availability, GOD has been used as a model enzyme for designing and fabricating electrochemical biosensors [11,12].…”

Section: Introductionmentioning

confidence: 99%

Study on Direct Electrochemistry of Glucose Oxidase Stabilized by Cross‐Linking and Immobilized in Silica Nanoparticle Films

Liu

2007

Electroanalysis

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Glucose oxidase (GOD) in SiO 2 nanoparticle films was cross-linked by glutaraldehyde (GA), forming GOD-GA-SiO 2 films on the surface of pyrolytic graphite (PG) electrodes. GOD in the GOD-GA-SiO 2 films showed a pair of well defined and quasi-reversible cyclic voltammetric peaks at À 0.48 V vs. SCE in pH 7.0 buffers. Scanning electron microscopy of the films demonstrated that the interaction between GOD and GA/SiO 2 would make the morphology of dry GOD-GA-SiO 2 films very different from that of SiO 2 and GOD-SiO 2 films. IR spectroscopy confirms that the GODs in the films are indeed cross-linked through GA, and GA in the films greatly improves the film stability. UVvis and IR spectroscopy suggest that the enzyme is not denatured by cross-linking in the films. The comparative bioelectrocatalytic study with free flavin adenine dinucleotide (FAD) in SiO 2 films indicates that GOD in the films retains its biocatalytic activity toward glucose oxidation. All these results show that SiO 2 nanoparticle films not only provide a favorable microenvironment for the native GOD to exchange electrons directly with underlying electrodes, but also supply a matrix for stabilizing GOD when combined with GA.

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Section: Introductionmentioning

confidence: 99%

Study on Direct Electrochemistry of Glucose Oxidase Stabilized by Cross‐Linking and Immobilized in Silica Nanoparticle Films

Liu

2007

Electroanalysis

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“…or ca. 4.3 nm in diameter) (27)(28)(29) were present in these films, the enzyme would leak freely into the analyte soluzion. However, no glucose oxidase could be, detected (electrochemically) in the analyte solution, even after overnight expommI of the sensor to this solution.…”

Section: Resultsmentioning

confidence: 99%

Biosensors Based on Ultrathin Film Composite Membranes

Martin¹,

Ballarin²,

Brumlik³

et al. 1994

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“…At temperatures greater than 40"C, the enzyme glucose oxidase is reported to be unstable. 33 Fortier et al l 8 have investigated the effect of temperatures greater than 40°C for glucose oxidase immobilized in polypyrrole on a platinum electrode and reported a decrease in sensor current due to temperature-induced denaturation of the enzyme; the effect was found to be reversible up to a temperature of 50°C.…”

Section: Effect Of Temperature and Phmentioning

confidence: 97%

An autoclavable glucose biosensor for microbial fermentation monitoring and control

Phelps¹,

Hobbs²,

Kilburn³

et al. 1995

Biotech & Bioengineering

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The design, construction, and characterization of a prototype-regenerable glucose biosensor based on the reversible immobilization of glucose oxidase (GOx) using cellulose binding domain (CBD) technology is described. GOx, chemically linked to CBD, is immobilized by binding to a cellulose matrix on the sensor-indicating electode. Enzyme immobilization can be reversed by perfusing the cellulose matrix with a suitable eluting solution. An autocavable sensor membrane system is employed which is shown to be practical for use in real microbial fermentations. The prototype glucose biosensor was used without failure or deterioration during fed-batch fermentations of Escherichia coli reaching a maximum cell density of 85 g (dry weight)/L. Medium glucose concentration based on sensor output correlated closely with off-line glucose analysis and was controlled manually at 0.44 +/- 0.2 g/L for 2 h based on glucose sensor output. The sensor enzyme component could be eluted and replaced without interrupting the fermentation. To our knowledge, no other in situ biosensor has been used for such an extended period of time in such a high-cell-density fermentation.

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Effect of periodate oxidation on the structure and properties of glucose oxidase

Cited by 112 publications

References 25 publications

Study on Direct Electrochemistry of Glucose Oxidase Stabilized by Cross‐Linking and Immobilized in Silica Nanoparticle Films

Study on Direct Electrochemistry of Glucose Oxidase Stabilized by Cross‐Linking and Immobilized in Silica Nanoparticle Films

Biosensors Based on Ultrathin Film Composite Membranes

An autoclavable glucose biosensor for microbial fermentation monitoring and control

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