Enzymatic activity of glucose oxidase covalently wired via viologen to electrically conductive polypyrrole films

Liu, X; Neoh, K. G.; Chen, Lian; Kang, En‐Tang

doi:10.1016/j.bios.2003.08.010

Cited by 66 publications

(27 citation statements)

References 33 publications

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“…There are several methods by which biosensors can be constructed using a mediator. Commonly used mediators are organic dyes [5][6][7], ferrocene/ferrocene derivatives [8][9][10], metal complexes [11,12], and similar compounds. Mediators are efficient at promoting a good response from an enzyme reaction under low overpotential.…”

Section: Introductionmentioning

confidence: 99%

Amperometric determination of glucose, based on the direct electron transfer between glucose oxidase and tin oxide

Park

Kim

Seong³

et al. 2008

Biotechnol Bioproc E

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An amperometric glucose biosensor was designed for the detection of glucose in blood, urine, beverages, and fermentation systems. In typical glucose biosensors that employ enzymes, mediators are used for efficient electron transfer between the enzymes and the electrode. However, some of these mediators are known to be toxic to the enzymes and also must be immobilized on the surface of the electrode. We propose a mediator-free glucose biosensor that uses a glucose oxidase immobilized on a tin oxide electrode. Direct electron transfer is possible in this system because the tin oxide has redox properties similar to those of mediators. The method for immobilization of the glucose oxidase onto the tin oxide is also very simple. Tin oxide was prepared by the anodization and annealing of pure tin, and this provides a large surface area for the immobilization step because of its porosity. Glucose oxidase was immobilized onto the tin oxide using the membrane entrapment method. The proposed method provides a simple process for fabricating the enzyme electrode. Glucose oxidase immobilized onto the tin oxide, prepared in accordance with this method, has a relatively large current response when compared to those of other glucose biosensors. The sensitivity of the biosensor was 19.55 µA/mM, and a linear response was observed between 0~3 mM glucose. This biosensor demonstrated good reproducibility and stability. © KSBB hÉóïçêÇëW=ÄáçëÉåëçêI=ÇáêÉÅí=ÉäÉÅíêçå=íê~åëÑÉêI=ÖäìÅçëÉI=ÖäìÅçëÉ=çñáÇ~ëÉI=íáå=çñáÇÉ= = = = =

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Section: Introductionmentioning

confidence: 99%

Amperometric determination of glucose, based on the direct electron transfer between glucose oxidase and tin oxide

Park

Kim

Seong³

et al. 2008

Biotechnol Bioproc E

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“…This is higher than the results previously reported in the literature for covalently bonded enzymes. 10,15,16 One explanation can be that, in the present case, the enzyme was immobilized in a monolayer using the COOH groups on the latex fi lm surface, and that this led to less conformational constraint than in previous cases 15,16 where the enzymes were bonded to COOH-containing polymer chains that were grafted onto fi lm surfaces. When the enzyme activities of the various samples were normalized with respect to fi lm surface area, the fi lms with the immobilized enzyme in the dispersion and the entrapped enzyme showed a higher enzyme activity than the sample with enzyme immobilized on the surface ( Figure 6).…”

Section: Immobilization and Entrapment Of Enzymementioning

confidence: 65%

“…Enzyme immobilization was performed using a previous method, 10,15,16 with some modifi cations. In the present study, the enzyme was immobilized to the carboxylic groups on the surface of the latex particles or on the surface of the polymer fi lms formed from the latex dispersions (see Figure 1).…”

Section: Methodsmentioning

confidence: 99%

“…This enzyme catalyses the reaction between glucose and oxygen, forming gluconolactone and hydrogen peroxide. 8,10,11 Often, this enzyme is used together with another enzyme, catalase, which removes the hydrogen peroxide formed. 8,11,12 Other enzyme-based active packages include lysozyme in anti-microbial packaging 13 and naringinase to remove the bitter components naringin and limonin found in citric juices.…”

Section: Introductionmentioning

confidence: 99%

“…In the current study, carboxylated styrene acrylate latex samples have been functionalized by GOx immobilization using a technique previously used for enzyme immobilization in biosensor applications 10,15,16,26 and anti-microbial packaging. 27 The infl uence of the immobilization and entrapment of enzyme on the enzyme activity in the fi nal latex fi lms has been studied.…”

Section: Introductionmentioning

confidence: 99%

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Enzyme immobilization in latex dispersion coatings for active food packaging

et al. 2007

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Carboxylated styrene acrylate latex samples have been functionalized by the immobilization and entrapment of the enzyme glucose oxidase (GOx), which can be used as an oxygen scavenger in food packaging. GOx was covalently immobilized both on the surface of already formed fi lms and on the latex particles in dispersion, as well as entrapped within the polymer matrix. In the latter two cases, polymer fi lms were formed after the enzyme had been added to the latex dispersion. The storage stability of the enzyme and the infl uence of adding clay were also studied. For a given amount of enzyme, the enzyme immobilized on the fi lm surface showed an enzyme activity about 10 times higher than that of the enzyme present within the polymer matrix. This is probably due to the diffusion limitations of the substrate in the polymer matrix. The fi lms with the enzyme present within the polymer matrix, however, showed a higher total oxygen-removal capacity than fi lms with the enzyme immobilized on the surface. Entrapped enzyme showed a slightly higher activity than enzyme immobilized in the dispersion due to the negative effect of the activating chemicals used during the immobilization and on conformational constraints upon covalent bonding. Low amounts of clay added to the dispersion decreased the enzyme activity, but with higher amounts of clay the enzyme activity increased, probably because of the increased porosity and thus higher substrate accessibility. The most suitable storage condition for all the enzyme-containing fi lms was +8°C, which is just above the glass transition temperature of the polymer used.

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