Kinetic and transport analysis of immobilized oxidoreductases that oxidize glycerol and its oxidation products

Arechederra, Robert L.; Minteer, Shelley D.

doi:10.1016/j.electacta.2009.09.083

Cited by 17 publications

(3 citation statements)

References 34 publications

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“…While it is difficult to engineer such interfaces, researchers can artificially bring individual catalytic domains in close proximity to provide similar benefits. Random chemical conjugation (Sletten and Bertozzi, ), physical adsorption onto surfaces (Arechederra and Minteer, ), and encapsulation within a matrix (Kim et al, ) have all been used to easily mimic protein complexes. These methods, however, lack the ability to control local catalytic or functional compositions, are prone to denaturation, and potentially disrupt native protein functionalities (Sheldon, ).…”

Section: Introductionmentioning

confidence: 99%

Bioengineering strategies to generate artificial protein complexes

Kim

Siu²,

Raeeszadeh‐Sarmazdeh³

et al. 2015

Biotech & Bioengineering

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For many applications, increasing synergy between distinct proteins through organization is important for the specificity, regulation, and overall reaction efficiency. Although there are many examples of protein complexes in nature, a generalized method to create these complexes remains elusive. Many conventional techniques such as random chemical conjugation, physical adsorption onto surfaces, and encapsulation within matrices are imprecise approaches and can lead to deactivation of protein native functionalities. More "bio-friendly" approaches such as genetically fused proteins and biological scaffolds often can result in low yields and low complex stability. Alternatively, site-specific protein conjugation or ligation can generate artificial protein complexes that preserve the native functionalities of protein domains and maintain stability through covalent bonds. In this review, we describe three distinct methods to synthesize artificial protein complexes (genetic incorPoration of unnatural amino acids to introduce bio-orthogonal azide and alkyne groups to proteins, split-intein based expressed protein ligation, and sortase mediated ligation) and highlight interesting applications for each technique.

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Section: Introductionmentioning

confidence: 99%

Bioengineering strategies to generate artificial protein complexes

Kim

Siu²,

Raeeszadeh‐Sarmazdeh³

et al. 2015

Biotech & Bioengineering

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“…3A). Similarly, m for glycerol (6.6 × 10 −5 cm s −1 ) was estimated based on a reported Nafion permeability of 2.9 × 10 −7 cm 2 /s, 45 and a methanol permeability of 1.9 × 10 −6 cm 2 /s. 44 However, in this case, the calculated n app values from Eq.…”

Section: Resultsmentioning

confidence: 99%

Screening of Catalysts for the Electrochemical Oxidation of Organic Fuels in A Multi-Anode Proton Exchange Membrane Cell

Brueckner

Wheeler

Chen

et al. 2019

J. Electrochem. Soc.

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A multi-anode, proton exchange membrane electrolysis cell has been used to evaluate commercial and developmental catalysts for the oxidation of methanol, ethanol, ethylene glycol, and glycerol at 80°C. By operating the cell in crossover mode, with the fuel supplied to the cathode, steady-state mass transport limited currents can be achieved. This provides a measure of the stoichiometry of the reaction, which is controlled by the product distribution. The method has been benchmarked by using commercial PtRu black and carbon supported catalysts with 20% and 70% Pt. In all cases, the PtRu alloy decreased onset and half-wave potentials relative to Pt. However, stoichiometries for ethanol, ethylene glycol, and glycerol oxidation were greatly decreased by the presence of Ru. This effect was mitigated by employing Ru as the core in Ru@Pt nanoparticles or in a mixed Ru + Sn oxide support material. Although not as effective as the PtRu alloy for promoting low potential activity, these catalysts exhibited selectivity similar to Pt. Use of alloyed Rh and a Rh core was also evaluated, but did not show any benefits over Pt alone.

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“…More commonly used enzymes for alcohol oxidation are NADdependent alcohol dehydrogenase and PQQ-dependent alcohol dehydrogenase (PQQ-ADH). NAD-dependent alcohol dehydrogenase is very specific, whereas PQQ-ADH is promiscuous; 12 however, it is a membrane-bound protein that is relatively unstable in solution of alkanes or alcohols in high concentrations. 13 For this study, we chose to test both AOx and NAD-dependent alcohol dehydrogenase to determine which produces larger bioelectrocatalytic current in a cascade with AMO.…”

Section: ■ Introductionmentioning

confidence: 99%

Bioelectrocatalytic Oxidation of Alkanes in a JP-8 Enzymatic Biofuel Cell

et al. 2014

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Alkanes are attractive fuels for fuel cells due to their high energy density, but their use has not transitioned to biofuel cells. This paper discusses the development of a novel enzyme cascade utilizing alkane monooxygenase (AMO) and alcohol oxidase (AOx) to perform mediated bioelectrocatalytic oxidation of hexane and octane. This was then applied for the bioelectrocatalysis of the jet fuel JP-8, which was tested directly in an enzymatic biofuel cell to evaluate performance. The enzymatic catalysts were shown to be sulfur tolerant and produced power densities up to 3 mW/cm 2 from native JP-8 without desulfurization as opposed to traditional metal catalysts, which require fuel preprocessing.

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Kinetic and transport analysis of immobilized oxidoreductases that oxidize glycerol and its oxidation products

Cited by 17 publications

References 34 publications

Bioengineering strategies to generate artificial protein complexes

Bioengineering strategies to generate artificial protein complexes

Screening of Catalysts for the Electrochemical Oxidation of Organic Fuels in A Multi-Anode Proton Exchange Membrane Cell

Bioelectrocatalytic Oxidation of Alkanes in a JP-8 Enzymatic Biofuel Cell

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