Dependence of catalytic activity and long-term stability of enzyme hydrogel films on curing time

Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time incre...

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Published inBioelectrochemistry (Amsterdam, Netherlands) Vol. 79; no. 1; pp. 142 - 146
Main Authors Lehr, Joshua, Williamson, Bryce E., Barrière, Frédéric, Downard, Alison J.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.08.2010
Elsevier
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Abstract Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time increases resulted in the highest catalytic activity for films cured for 24 h at 25 °C. Weekly electrochemical measurements established that the long-term stabilities of all hydrogels cured for 24–72 h were similar, with close to half of the initial catalytic activity being retained after immersion for 3 months in agitated phosphate buffer solution at 25 °C.
AbstractList Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time increases resulted in the highest catalytic activity for films cured for 24 h at 25 °C. Weekly electrochemical measurements established that the long-term stabilities of all hydrogels cured for 24–72 h were similar, with close to half of the initial catalytic activity being retained after immersion for 3 months in agitated phosphate buffer solution at 25 °C.
Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time increases resulted in the highest catalytic activity for films cured for 24h at 25 degrees C. Weekly electrochemical measurements established that the long-term stabilities of all hydrogels cured for 24-72 h were similar, with close to half of the initial catalytic activity being retained after immersion for 3 months in agitated phosphate buffer solution at 25 degrees C.
Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time increases resulted in the highest catalytic activity for films cured for 24 h at 25 C. Weekly electrochemical measurements established that the long-term stabilities of all hydrogels cured for 24-72 h were similar, with close to half of the initial catalytic activity being retained after immersion for 3 months in agitated phosphate buffer solution at 25 C.
Author Williamson, Bryce E.
Downard, Alison J.
Barrière, Frédéric
Lehr, Joshua
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Issue 1
Keywords Glucose oxidase
Hydrogel
Hydroxymethylferrocene
Poly(ethylene glycol) diglycidyl ether
Carbon
Language English
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Snippet Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found...
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SubjectTerms Aspergillus niger - enzymology
Biocatalysis
Carbon
Carbon - chemistry
Chemical Sciences
Electrodes
Enzyme Stability
Glucose oxidase
Glucose Oxidase - chemistry
Glucose Oxidase - metabolism
Hydrogel
Hydrogel, Polyethylene Glycol Dimethacrylate
Hydroxymethylferrocene
Organic chemistry
Poly(ethylene glycol) diglycidyl ether
Temperature
Time Factors
Title Dependence of catalytic activity and long-term stability of enzyme hydrogel films on curing time
URI https://dx.doi.org/10.1016/j.bioelechem.2009.12.004
https://www.ncbi.nlm.nih.gov/pubmed/20051328
https://search.proquest.com/docview/733958905
https://search.proquest.com/docview/754539043
https://hal.science/hal-00502106
Volume 79
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