Immobilization of glucose oxidase using acrylonitrile copolymer membranes

Godjevargova, Tzonka; Dimov, A.; Vasileva, N.

doi:10.1016/0376-7388(94)87014-4

Cited by 26 publications

(25 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Due to the basic nature of the unreacted amino groups on the surface, favorable conditions of active sites at solid-liquid interface could be attained at lower pH. Such results have been already reported in the literatures [37]. As shown in Fig.…”

Section: Effect Of Ph On the Activity Of God And God-mnpssupporting

confidence: 53%

See 1 more Smart Citation

Silica-encapsulated magnetic nanoparticles: Enzyme immobilization and cytotoxic study

Ashtari

Khajeh

Fasihi

et al. 2012

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Section: Effect Of Ph On the Activity Of God And God-mnpssupporting

confidence: 53%

“…It also plays an important role in ionization state of the amino acids in the active site and maintaining the proper conformation of an enzyme [37]. Therefore, the effect of pH on the GOD activity was investigated through varying the pH from 3.0 to 8.0.…”

Section: Effect Of Ph On the Activity Of God And God-mnpsmentioning

confidence: 99%

Silica-encapsulated magnetic nanoparticles: Enzyme immobilization and cytotoxic study

Ashtari

Khajeh

Fasihi

et al. 2012

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…The influence of the pH was checked in PBS solution with 6.5 mM glucose over the range 5.5 -8.0, at 25 8C. The electrode response versus sample pH (not reported) shows a bell-shaped curve with a maximum between 6.0 and 7.0 that corresponds fairly well with the value reported in literature for the free enzyme [30]. This behavior confirms that the immobilization of the enzyme does not affect its catalytic function.…”

Section: Effect Of Ph and Temperaturesupporting

confidence: 50%

Glucose Biosensor Mediated by 1,2‐Diferrocenylethane in a Sono‐Gel Composite Electrode

et al. 2007

View full text Add to dashboard Cite

An amperometric glucose biosensor was constructed based on a renewable carbon composite sono-gel matrix incorporating 1,2-diferrocenylethane as electron transfer mediator between the electrode and the active site of glucose oxidase. The enzyme was immobilized on the electrode surface by cross-linking with glutaraldehyde and bovine serum albumin. The process parameters for the fabrication of the biosensor and the influence of various experimental conditions (i.e., pH, temperature, operating potential) were investigated. Cyclic voltammetry and amperometric measurements were used to study the response of the glucose sensor, which displayed fast response time and good reproducibility. The analytical performances and the apparent Michaelis-Menten constant of the biosensor were evaluated.

show abstract

“…The results were compared with those of nonmodified GOD. The T opt of the native GOD reported earlier 15,16 was 28°C. In the presence of HPAN and POE the optimum was shifted to a higher value (30°C) and, at temperatures higher than 30°C, the enzyme activity was higher than that for polymer without water.…”

Section: Resultsmentioning

confidence: 99%

Study of the thermal stability of glucose oxidase in the presence of water‐soluble polymers

Godjevargova¹,

Vasileva²,

Letskovska³

2003

J of Applied Polymer Sci

View full text Add to dashboard Cite

ABSTRACT:The thermal stability of glucose oxidase (GOD) in solutions containing water-soluble hydrolyzed polyacrylonitrile (HPAN) and polyoxyethylene (POE) was studied as a function of time and temperature between 28 and 60°C. The results were compared with the thermal stability of GOD in solutions without polymers. The polymers studied were found to increase the enzyme thermal stability. The influence of the concentration of the watersoluble polymers on enzyme thermal stability was also studied. The best protection effect on enzyme thermal stability had 3 wt % solution of HPAN and 1 wt % solution of polyoxyethylene. Solutions with higher concentrations led to a quick deactivation of the enzyme. It was proved that the effect of 3 wt % HPAN solution was stronger than the effect of 1 wt % POE (59.0 versus 52.0%). The thermal transition of the enzyme was studied in both the presence and the absence of HPAN by DSC. The melting temperature of GOD in the presence of HPAN was shifted to an 11°C higher value. This sustained the supposition that HPAN increases the thermostability of GOD.

show abstract

Immobilization of glucose oxidase using acrylonitrile copolymer membranes

Cited by 26 publications

References 6 publications

Silica-encapsulated magnetic nanoparticles: Enzyme immobilization and cytotoxic study

Silica-encapsulated magnetic nanoparticles: Enzyme immobilization and cytotoxic study

Glucose Biosensor Mediated by 1,2‐Diferrocenylethane in a Sono‐Gel Composite Electrode

Study of the thermal stability of glucose oxidase in the presence of water‐soluble polymers

Contact Info

Product

Resources

About