Glucose oxidase immobilization on a novel cellulose acetate–polymethylmethacrylate membrane

Rauf, Sakandar; Ihsan, Ayesha; Akhtar, Kalsoom; Ghauri, Muhammad Afzal; Rahman, Md Jamilur; Anwar, Munir A.; Khalid, Ahmad Mukhtar

doi:10.1016/j.jbiotec.2005.08.019

Cited by 103 publications

(60 citation statements)

References 32 publications

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“…Being V 0 max directly related to the efficiency of the enzyme's active site and K 0 M inversely related to the affinity of the enzyme for the substrate, the variation of those values due to the immobilization procedure indicate that the efficiency of GOx's active site and GOx affinity for glucose is reduced with respect to free GOx in solution. This finding can be explained taking into account that the presence of Nafion leads to substrate diffusion and charge transfer limitations in the immobilized form of GOx, in agreement with previous reports [42][43][44]. This becomes particularly evident if kinetic parameters of the two immobilized GOx samples (with and without MWCNTs) are compared.…”

Section: Effect Of Mwcnts On Electron-transfer and Bioelectrocatalytisupporting

confidence: 91%

Development of glucose oxidase-based bioanodes for enzyme fuel cell applications

et al. 2012

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We fabricated an enzyme fuel cell (EFC) device based on glucose as fuel and glucose oxidase (GOx) as biocatalyst. As a strategy to improve GOx stability, preserving at the same time the enzyme catalytic activity, we propose an immobilization procedure to entrap GOx in a polymer matrix based on Nafion and multiwalled carbon nanotubes. Circular dichroism (CD) spectra were recorded to study changes in the 3D structure of GOx that might be generated by the immobilization procedure. The comparison between the CD features of GOx immobilized and free in solution indicates that the shape of the spectra and position of peaks do not significantly change. The bioelectrocatalytic activity toward glucose oxidation of immobilized GOx was studied by cyclic voltammetry and chronoamperometry experiments. Such electrochemical experiments allow monitoring the rate of GOx-catalyzed glucose oxidation and extrapolating GOx kinetic parameters. Results demonstrate that immobilized GOx has high catalytic efficiency, due the maintaining of regular and well-ordered structure of the immobilized enzyme, as indicated by spectroscopic findings. Once investigated the electrode structure-property relationship, an EFC device was assembled using the GOx-based bioanode, and sulfonated poly ether ether ketone as electrolyte membrane.Polarization and power density curves of the complete EFC device were acquired, demonstrating the suitability of the immobilization strategy and materials to be used in EFCs.

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Section: Effect Of Mwcnts On Electron-transfer and Bioelectrocatalytisupporting

confidence: 91%

Development of glucose oxidase-based bioanodes for enzyme fuel cell applications

et al. 2012

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“…However, this decreasing slope in bioactivity of the immobilized GOD in the nanochannels is much slower than the results reported for the free GOD. [37][38][39] In the present system, the immobilized GOD still retains 85 % of the optimum activity of GOD, even at pH 9.0, thus demonstrating that the bioactivity of the immobilized GOD can be protected by the nanochannel system. The present result demonstrates that bioassays of GOD immobilized in the nanochannel array of the PAA membrane can be operated over a wide range of solution pH values without sacrificing the activity significantly.…”

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confidence: 59%

Real‐Time Monitoring of Mass‐Transport‐Related Enzymatic Reaction Kinetics in a Nanochannel‐Array Reactor

Wang

et al. 2010

Chemistry A European J

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To understand the fundamentals of enzymatic reactions confined in micro-/nanosystems, the construction of a small enzyme reactor coupled with an integrated real-time detection system for monitoring the kinetic information is a significant challenge. Nano-enzyme array reactors were fabricated by covalently linking enzymes to the inner channels of a porous anodic alumina (PAA) membrane. The mechanical stability of this nanodevice enables us to integrate an electrochemical detector for the real-time monitoring of the formation of the enzyme reaction product by sputtering a thin Pt film on one side of the PAA membrane. Because the enzymatic reaction is confined in a limited nanospace, the mass transport of the substrate would influence the reaction kinetics considerably. Therefore, the oxidation of glucose by dissolved oxygen catalyzed by immobilized glucose oxidase was used as a model to investigate the mass-transport-related enzymatic reaction kinetics in confined nanospaces. The activity and stability of the enzyme immobilized in the nanochannels was enhanced. In this nano-enzyme reactor, the enzymatic reaction was controlled by mass transport if the flux was low. With an increase in the flux (e.g., >50 microL min(-1)), the enzymatic reaction kinetics became the rate-determining step. This change resulted in the decrease in the conversion efficiency of the nano-enzyme reactor and the apparent Michaelis-Menten constant with an increase in substrate flux. This nanodevice integrated with an electrochemical detector could help to understand the fundamentals of enzymatic reactions confined in nanospaces and provide a platform for the design of highly efficient enzyme reactors. In addition, we believe that such nanodevices will find widespread applications in biosensing, drug screening, and biochemical synthesis.

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“…[27] Most important is the application of GOD in biosensors for the quantitative determination of glucose, e.g., in body fluids or food products. [27][28][29] For all these processes, immobilization and encapsulation of GOD is desired, in order to enhance reusability and operational stability.…”

Section: Preparation Of Polyelectrolyte Complex Capsulesmentioning

confidence: 99%

Interaction of Ionic Liquids with Polysaccharides, 8 – Synthesis of Cellulose Sulfates Suitable for Polyelectrolyte Complex Formation

Gericke

Liebert

Heinze

2009

Macromolecular Bioscience

106

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Water-soluble CS with different DS were synthesized by homogeneous conversion of cellulose (microcrystalline cellulose and spruce sulfite pulp) with different sulfating agents in the ionic liquids BMIMCl, AMIMCl and EMIMAc. N,N-Dimethylformamide was used as a dipolar aprotic co-solvent in order to improve the miscibility of the reaction mixture. The CS prepared by the new homogeneous reaction pathway were studied towards the formation of PEC capsules. CS obtained from SSP formed mechanically stable PEC capsules with PolyDADMAC. Exploiting this method, the microencapsulation of glucose oxidase was studied and enzyme activity tests were performed with encapsulated GOD.

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Glucose oxidase immobilization on a novel cellulose acetate–polymethylmethacrylate membrane

Cited by 103 publications

References 32 publications

Development of glucose oxidase-based bioanodes for enzyme fuel cell applications

Development of glucose oxidase-based bioanodes for enzyme fuel cell applications

Real‐Time Monitoring of Mass‐Transport‐Related Enzymatic Reaction Kinetics in a Nanochannel‐Array Reactor

Interaction of Ionic Liquids with Polysaccharides, 8 – Synthesis of Cellulose Sulfates Suitable for Polyelectrolyte Complex Formation

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