Electrochemical studies of single-wall carbon nanotubes as nanometer-sized activators in enzyme-catalyzed reaction

Gan, Zhenhai; Zhao, Qiang; Zhi, Gu; Zhuang, Qiya

doi:10.1016/j.aca.2004.01.055

Cited by 33 publications

(19 citation statements)

References 30 publications

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“…In other words, the reactivity of the enzyme-substrate in the CNT/d-Pro dH immobilized electrode was higher than those of the other carbon material/d-Pro dH immobilized electrodes. The smaller Km value for the CNT immobilized electrode is consistent with previous reports for CNT-modified enzyme sensors, such as CNT and lactate dehydrogenase (enzyme cofactor NAd), 27 HRP (enzyme cofactor heme), 17 and GOx (enzyme cofactor FAd) electrodes. 28,29 …”

Section: Comparison Of the Current Response Of D-proline With Differesupporting

confidence: 79%

An Amperometric d-Amino Acid Biosensor Prepared with a Thermostable D-Proline Dehydrogenase and a Carbon Nanotube-Ionic Liquid Gel

et al. 2009

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Carbon nanotube (CNT) gel, which is composed of a mixture of single-wall CNT, an ionic liquid, and a thermostable d-proline dehydrogenase (d-Pro dH) immobilized electrode was utilized for the determination of d-amino acids (dAAs) in food samples. When a critical comparison with CNT, Ketjen Black (KB), and carbon powder (CP) was also carried out, the CNT/d-Pro dH immobilized electrode showed the highest sensitivity and the lowest detection limit of d-proline. In addition, the CNT/d-Pro dH immobilized electrode was applied to detection of dAAs in rice wine and vinegar samples. The concentrations of dAAs in rice wine and vinegar samples were 0.0210 ± 0.0001 and 0.55 ± 0.05 mmol L -1 , respectively.

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Section: Comparison Of the Current Response Of D-proline With Differesupporting

confidence: 79%

An Amperometric d-Amino Acid Biosensor Prepared with a Thermostable D-Proline Dehydrogenase and a Carbon Nanotube-Ionic Liquid Gel

et al. 2009

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“…It could be concluded that there might be another factor dominating a critical role in determining K app m , namely, biocompatibility. CNTs could retain the native conformation of heme protein (Karajanagi et al, 2004;Zhao et al, 2006) and well interact with lactate dehydrogenase (Gan et al, 2004), which proved that CNTs provided biocompatible microenvironment for enzymes. As a result, the surface biocompatibility might be attributed to two aspects: on one hand, blending with the biocompatible materials could render the bulk nanofiber mesh with biocompatible property, which was supported by literatures (Li et al, 2006;Uchiyama et al, 2002;Ye et al, 2002); on the other hand, the surface-oxidized MWCNT formed complexes with -CN: that was disfavored by hydrophilic protein.…”

Section: Storage Stabilities Of the Free And Immobilized Catalasesmentioning

confidence: 95%

Covalent immobilization of redox enzyme on electrospun nonwoven poly(acrylonitrile‐co‐acrylic acid) nanofiber mesh filled with carbon nanotubes: A comprehensive study

Wang

2007

Biotech & Bioengineering

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In this work, novel conductive composite nanofiber mesh possessing reactive groups was electrospun from solutions containing poly(acrylonitrile-co-acrylic acid) (PANCAA) and multi-walled carbon nanotubes (MWCNTs) for redoxase immobilization, assuming that the incorporated MWCNTs could behave as electrons transferor during enzyme catalysis. The covalent immobilization of catalase from bovine liver on the neat PANCAA nanofiber mesh or the composite one was processed in the presence of EDC/NHS. Results indicated that both the amount and activity retention of bound catalase on the composite nanofiber mesh were higher than those on the neat PANCAA nanofiber mesh, and the activity increased up to 42%. Kinetic parameters, K(m) and V(max), for the catalases immobilized on the composite nanofiber mesh were lower and higher than those on the neat one, respectively. This enhanced activity might be ascribed to either promoted electron transfer through charge-transfer complexes and the pi system of carbon nanotubes or rendered biocompatibility by modified MWCNTs. Furthermore, the immobilized catalases revealed much more stability after MWCNTs were incorporated into the polymer nanofiber mesh. However, there was no significant difference in optimum pH value and temperature, thermal stability and operational stability between these two immobilized preparations, while the two ones appeared more advantageous than the free in these properties. The effect of MWCNTs incorporation on another redox enzyme, peroxidase, was also studied and it was found that the activity increased by 68% in comparison of composite one with neat preparation.

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“…Furthermore, glucose oxidase has been immobilized on aligned carbon nanotubes modified with a gold thin film [13,14]. Gan et al [15] have studied the immobilization of lactic dehydrogenase of mouse muscle. Recently, Yu et al [16] have shown that the myoglobine and horseradish peroxidase can be immobilized on carbon nanotubes using promoters in the media to favour the formation of amide bond between the terminal carboxylic and the lysine residue.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of β-Glucosidase on carbon nanotubes

2005

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Carbon nanotubes are demonstrated as a good support for the immobilization of b-Glucosidase. This is an enzyme with high molecular weight (ca. 135 kDa). A high enzyme loading of 630 mg per gram of support was achieved in 12 h. The link between the enzyme and the carbon nanotubes surface was by electrostatic interactions due to the different charges of the enzyme and the support at the pH of the immobilization. Immobilized b-Glucosidase showed a catalytic activity above 400 U/g on the hydrolysis of 4-nitrophenyl-b-D-glucopyranoside (p-NPG).

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Electrochemical studies of single-wall carbon nanotubes as nanometer-sized activators in enzyme-catalyzed reaction

Cited by 33 publications

References 30 publications

An Amperometric d-Amino Acid Biosensor Prepared with a Thermostable D-Proline Dehydrogenase and a Carbon Nanotube-Ionic Liquid Gel

An Amperometric d-Amino Acid Biosensor Prepared with a Thermostable D-Proline Dehydrogenase and a Carbon Nanotube-Ionic Liquid Gel

Covalent immobilization of redox enzyme on electrospun nonwoven poly(acrylonitrile‐co‐acrylic acid) nanofiber mesh filled with carbon nanotubes: A comprehensive study

Immobilization of β-Glucosidase on carbon nanotubes

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