Enzymes immobilized on carbon nanotubes

Feng, Wei; Ji, Peijun

doi:10.1016/j.biotechadv.2011.07.007

Cited by 432 publications

(234 citation statements)

References 76 publications

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“…They demonstrated that a strong π -π interaction existed between the individual hexagonal cells of the GO basal planes and the glucose oxidase. This is similar to the interactions between the protein molecules and CNTs where the π -π stacking interaction is a dominated factor [112,120] . Apparently, the enzyme immobilization onto GO might be a result of the synergic effect of the different interactions.…”

Section: Noncovalent Adsorption Of the Protein/ Enzyme Molecules On Tsupporting

confidence: 57%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

198

105

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This review selectively describes the recent progress in the interactions of proteins (enzymes) and shortchain peptides with graphene and graphene oxide (GO). Particularly, the advances of the immobilization mechanisms of enzymes on graphene and GO, the catalytic properties of the immobilized enzymes, and their applications are summarized in detail. The interfacings of the peptides with graphene and GO, the as assembled conjugates, and their potential applications are discussed briefly. The possible ongoing development for the assembly of conjugates of graphene and GO with proteins and peptides in a controlled manner is speculated upon.

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Section: Noncovalent Adsorption Of the Protein/ Enzyme Molecules On Tsupporting

confidence: 57%

Interactions of graphene and graphene oxide with proteins and peptides

Zhang

Guo³

et al. 2013

Nanotechnology Reviews

198

105

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“…[221] CNTs have unique properties of electrical conductivity and have a size that is suitable for enzyme interactions, preventing their leaching and offering multipoint linkage. [222,223] They also develop large surface areas. Multi-walled (MWCNTs) or singlewalled CNTs (SWCNTs) can be used, although they display very different properties, with the former being considered as a flat material from the enzyme point of view.…”

Section: Carbon Nanomaterialsmentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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Among sustainable alternatives to fossil fuel, proton exchange membrane fuel cells are promising devices that deliver electricity from hydrogen and oxygen, producing only water. The transformation of the fuel and oxidant however relies on rare‐metal catalysts. H2/O2 enzymatic biofuel cells thus emerge as sustainable biotechnological devices in which chemical catalysts are replaced by hydrogenases at the anode and multicopper oxidases at the cathode. This review discusses the recent breakthroughs and the limitations in all the components of H2/O2 biofuel cells: 1) Catalytic mechanisms involved in multicopper oxidases and hydrogenases, in addition to the new potential of enzymes from the biodiversity pool, which exhibit outstanding properties. 2) The molecular basis for oriented enzyme immobilization on the electrochemical interfaces as a prerequisite for a fast direct electron‐transfer rate. 3) The requirement for 3D networks to enhance current densities. 4) The production of H2 from biomass. 5) The history of H2/O2 biofuel cells and recent devices, which also highlights the remaining issues that will allow the use of such devices in low‐power applications.

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“…Among these, multi-walled carbon nanotubes (MWCNTs) have gained great interest. They have excellent conducting properties and are flexible nanomaterials that seem to mimic an "enzyme friendly" environment [7]. Moreover, MWCNTs can be functionalized before enzyme incorporation with different strategies depending on the desired immobilization method and the individual protein [8].…”

Section: Introductionmentioning

confidence: 99%

Comparative study of three lactate oxidases from Aerococcus viridans for biosensing applications

Taurino

Reiss

Richter

et al. 2013

Electrochimica Acta

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Keywords:l-Lactate oxidases from Aerococcus viridans Engineered and commercial enzymes Multi-walled carbon nanotubes Enzyme biosensor a b s t r a c t A comparison between engineered and commercially available l-lactate oxidases from Aerococcus viridans was conducted for biosensing applications. Enzymes were adsorbed onto the surfaces of graphite electrodes modified with multi-walled carbon nanotubes. Thermostable l-lactate oxidases were cloned with a (i) N-, (ii) a C-terminal His-tag and (iii) a wild-type enzyme. Subsequently to the heterologous expression in Escherichia coli and purification, we determined the kinetic parameters of these enzymes in solution. The kinetics of the wild-type, of the N-terminally His-tagged enzyme and of the commercial l-lactate oxidase from A. viridans were studied with a classical Michaelis-Menten as well as with a substrate inhibition model, while the enzyme carrying a C-terminal His-tag showed no activity. The active enzymes were used to fabricate and comparatively investigate multi-walled carbon nanotubes-based biosensors. The enzyme kinetic results were compared with electrochemical studies. By using both spectrophotometric and amperometric techniques, the inhibition phenomenon fits better to the data especially those data related with Lox-His-N. The electrochemical data of the fabricated enzymatic biosensors showed that the N-terminally His-tagged l-lactate oxidase performed best on carboxyl-modified carbon nanotubes. The sensor based on this engineered enzyme showed the highest sensitivity and lowest detection limit in the range of l-lactate concentration 0-1 mM as well as long term stability over one month.

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Enzymes immobilized on carbon nanotubes

Cited by 432 publications

References 76 publications

Interactions of graphene and graphene oxide with proteins and peptides

Interactions of graphene and graphene oxide with proteins and peptides

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Comparative study of three lactate oxidases from Aerococcus viridans for biosensing applications

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Enzymes immobilized on carbon nanotubes

Cited by 432 publications

References 76 publications

Interactions of graphene and graphene oxide with proteins and peptides

Interactions of graphene and graphene oxide with proteins and peptides

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

Comparative study of three lactate oxidases from Aerococcus viridans for biosensing applications

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Product

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Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective