Immobilization of glucose oxidase by acrylonitrile copolymer coated silica supports

Godjevargova, Tzonka; Nenkova, Ruska; Konsulov, Vitan

doi:10.1016/j.molcatb.2005.11.010

Cited by 26 publications

(13 citation statements)

References 22 publications

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“…GOx immobilization and stabilization in various carrier matrices has been extensively studied. Once covalently immobilized on polyacrylonitrile films, 80% of the original activity remained after 50 days of storage at 4 °C [47]. When GOx was entrapped in a photosensitive crosslinking film, enzyme activity decreased to 23% of the original level after 6 months storage at 4°C [48].…”

Section: Discussionmentioning

confidence: 99%

Stabilization of Enzymes in Silk Films

et al. 2009

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Material systems are needed that promote stabilization of entrained molecules, such as enzymes or therapeutic proteins, without destroying their activity. We demonstrate that the unique structure of silk fibroin protein, when assembled into the solid state, establishes an environment that is conducive to the stabilization of entrained proteins. Enzymes (glucose oxidase, lipase and horseradish peroxidase) entrapped in these films over ten months retained significant activity, even when stored at 37°C, and in the case of glucose oxidase did not lose any activity. Further, the mode of processing of the silk protein into the films could be correlated to the stability of the enzymes. The relationship between processing and stability offers a large suite of conditions within which to optimize such stabilization processes. Overall, the techniques reported here result in materials that stabilize enzymes to a remarkable extent, without the need for cryoprotectants, emulsifiers, covalent immobilization or other treatments. Further, these systems are amenable to optical characterization, environmental distribution without refrigeration, are ingestible, and offer potential use in vivo, since silk materials are biocompatible and FDA approved, degradable with proteases and currently used in biomedical devices.

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Section: Discussionmentioning

confidence: 99%

Stabilization of Enzymes in Silk Films

et al. 2009

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“…Yang et al used an organic–inorganic sol–gel silicate network with a primary amine functional backbone to provide a carbodiimide reaction with GOx . Others have covalently bound enzymes using supports such as copolymers of acrylonitrile and polyaniline (PANI) and chitosan‐coupled carbon nanotubes (CS‐CNTs) . Here, we used polymer brushes as a scaffold to anchor GOx to our device surface.…”

Section: Introductionmentioning

confidence: 99%

A glucose sensor via stable immobilization of the GOx enzyme on an organic transistor using a polymer brush

Welch

Doublet

Bernard

et al. 2014

J. Polym. Sci. Part A: Polym. Chem.

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Recently, there has been significant research in the area of organic electrochemical transistors (OECTs) because of their superior aptitude of chemical and biological sensing. Here it is shown for the first time the incorporation of polymer brushes to a transistor. Polymer brushes were chosen for their biocompatible properties and their ability to covalently tether enzymes and other biomolecules to different surfaces. OECTs were fabricated from the conducting polymer poly(3,4‐ethylenedioxythiophene) doped with poly(styrene sulfonate), PEDOT:PSS, and polymerized from the surface a mixed polymer brush of poly(glycidyl methacrylate) and poly(2‐hydroxyethyl methacrylate). The brushes were functionalized with glucose oxidase and measured in terms of electrical performance and long‐term stability. © 2014 Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2015, 53, 372–377

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“…Enzyme immobilization is considered as one of the most popular biotechnological applications of different synthetic polymers including PVC 1–9. Enzyme immobilization facilitates the purification of the reaction system and the recovery of enzyme and makes it possible to use the enzyme repetitively or continuously.…”

Section: Introductionmentioning

confidence: 99%

Covalent immobilization of β‐galactosidase onto amino‐functionalized PVC microspheres

Eldin

El-Aassar

Elzatahry

et al. 2012

J of Applied Polymer Sci

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β‐Galactosidase enzyme, from Aspergillus oryzae, was covalently immobilized onto amino‐functionalized PVC microspheres after activation with gultaraldehyde. PVC microspheres were functionalized by introducing terminal amine groups via amination process with ethylene diamine (EDA). Furthermore, verifications of amination process were obtained using TGA, FT‐IR, and SEM analysis. Different factors affecting the amination process were investigated and their impact on the activity and the retention of immobilized enzyme's activity was monitored. Concentration of ethylene diamine, amination temperature, and time were found for a determined effect. Reaction with EDA (0.025%) at 30°C for 40 minutes was found for optimum conditions. Variation of PVC : EDA mass ratio over 1 : 1 was found with neglectable effect. Thermal stability of immobilized enzyme was recognized where the immobilized form kept 80% of its original activity compared with 20% for the free form. Denaturation tolerance against pH was observed where immobilized form kept 60% of its original activity after 300 minutes incubation at pH 7.0 in the absence of substrate while the free form kept only 15% of its activity under the same conditions. Moreover, immobilized form show storage stabilities where immobilized form kept 40% of its original activity after four weeks while the free form kept only 25% of its initial activity. Under optimum conditions for enzyme immobilization, 1 kg of immobilized enzyme retains 87% of its native activity and has 11,000 activity units. © 2012 Wiley Periodicals, Inc. J Appl Polym Sci, 2012

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Immobilization of glucose oxidase by acrylonitrile copolymer coated silica supports

Cited by 26 publications

References 22 publications

Stabilization of Enzymes in Silk Films

Stabilization of Enzymes in Silk Films

A glucose sensor via stable immobilization of the GOx enzyme on an organic transistor using a polymer brush

Covalent immobilization of β‐galactosidase onto amino‐functionalized PVC microspheres

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