Time‐dependent inactivation of immobilized glucose oxidase and catalase
Abstract
Homogeneous membranes containing immobilized glucose oxidase and catalase were stored in buffered solutions at 37°C to determine the mechanisms and rates of catalyst inactivation. The experiments were designed so that inactivation occurred homogeneously throughout the membrane, thereby simplifying the analysis. The mechanism of inactivation is consistent with the reaction of hydrogen peroxide and certain catalytic intermediates of both enzymes. Based on this information, numerical simulations were developed that incorporate spatially heterogeneous catalytic and inactivation processes.
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Deactivation by endogenously produced hydrogen peroxide from oxidase reactions also contributes to loss of enzyme activity.
“However, deactivation by endogenously produced hydrogen peroxide from oxidase reactions also contributes to the loss of activity.71”
From Biocompatible Materials for Continuous Glucose Monitoring Devices (2013) · cites this paper as [71]
Enzyme activity in glucose sensors begins to decrease immediately due to polymer entrapment and exposure to reactive oxidative species from sensor operation and the foreign body response.
“Enzyme activity begins to decrease immediately both due to polymer entrapment and exposure to reactive oxidative species from sensor operation and the FBR (exposure to hydrogen peroxide and other reactive radicals).71–72”
From Biocompatible Materials for Continuous Glucose Monitoring Devices (2013) · cites this paper as [71]
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Strobl, A. L. (2010) · eScholarship (California Digital Library)
Li, H. (2009) · Springer eBooks · doi:10.1007/978-3-642-02368-2_6
Bringer, J., Costalat, G., Jaffiol, C., & Renard, É. (2003) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)33910-x
Reaction engineering of radical-mediated polymerizations at surfaces and interfaces
Shenoy, R. (2012) · CU Scholar (University of Colorado Boulder)
Grubecki, I., Miłek, J., Trawczyńska, I., & Wójcik, M. (2015) · Inżynieria i Aparatura Chemiczna
Wpływ temperatury na kinetykę dezaktywacji katalazy z Aspergillus niger przez substrat
Miłek, J., & Kwiatkowska-Marks, S. (2016) · Inżynieria i Aparatura Chemiczna
- Authors
- Tse, P. H. S., & Gough, D. A.
- Affiliations
- University of California San Diego (US)
- Venue
- Biotechnology and Bioengineering
- Publisher
- Wiley
- Published
- 1987-04-20
- Volume
- 29
- Issue
- 6
- Pages
- 705-713
- ISSN
- 0006-3592 (ISSN-L)
- 1097-0290
- OpenAlex
- W2099051493
- Cited by
- 95
- References
- 32
- Citations by year
- 2026: 1 · 2023: 4 · 2022: 1 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 4
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biotechnology and Bioengineering (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Keywords
- enzyme immobilization, glucose oxidase, catalase, enzyme inactivation, time-dependent inactivation, homogeneous membranes, hydrogen peroxide, catalytic intermediates, inactivation mechanism, numerical simulation
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