scholarly journals An enzymatic biofuel cell based on electrically wired polyphenol oxidase and glucose oxidase operating under physiological conditions

2012 ◽  
Vol 85 ◽  
pp. 278-282 ◽  
Author(s):  
Fabien Giroud ◽  
Chantal Gondran ◽  
Karine Gorgy ◽  
Vincent Vivier ◽  
Serge Cosnier
Keyword(s):  
Glucose Oxidase ◽  
Polyphenol Oxidase ◽  
Biofuel Cell ◽  
Physiological Conditions ◽  
Enzymatic Biofuel Cell

scholarly journals A Self-Powered Biosensor for the Detection of Glutathione

Biosensors ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 114 ◽  
Author(s):  
Brandon G. Roy ◽  
Julia L. Rutherford ◽  
Anna E. Weaver ◽  
Kevin Beaver ◽  
Michelle Rasmussen
Keyword(s):  
Detection Limit ◽  
Glucose Oxidase ◽  
Power Output ◽  
Low Cost ◽  
Linear Range ◽  
Biofuel Cell ◽  
Bilirubin Oxidase ◽  
Biological Molecule ◽  
Enzymatic Biofuel Cell ◽  
Self Powered

Glutathione is an important biological molecule which can be an indicator of numerous diseases. A method for self-powered detection of glutathione levels in solution has been developed using an enzymatic biofuel cell. The device consists of a glucose oxidase anode and a bilirubin oxidase cathode. For the detection of glutathione, the inhibition of bilirubin oxidase leads to a measurable decrease in current and power output. The reported method has a detection limit of 0.043 mM and a linear range up to 1.7 mM. Being able to detect a range of concentrations can be useful in evaluating a patient’s health. This method has the potential to be implemented as a quick, low-cost alternative to previously reported methods.

Starchy biomass-powered enzymatic biofuel cell based on amylases and glucose oxidase multi-immobilized bioanode

2013 ◽  
Vol 30 (5) ◽  
pp. 531-535 ◽  
Author(s):  
Kazuhiro Yamamoto ◽  
Takuya Matsumoto ◽  
Shota Shimada ◽  
Tsutomu Tanaka ◽  
Akihiko Kondo
Keyword(s):  
Glucose Oxidase ◽  
Biofuel Cell ◽  
Enzymatic Biofuel Cell

Amide group anchored glucose oxidase based anodic catalysts for high performance enzymatic biofuel cell

2017 ◽  
Vol 337 ◽  
pp. 152-158 ◽  
Author(s):  
Yongjin Chung ◽  
Yeonjoo Ahn ◽  
Do-Heyoung Kim ◽  
Yongchai Kwon
Keyword(s):  
Glucose Oxidase ◽  
High Performance ◽  
Amide Group ◽  
Biofuel Cell ◽  
Enzymatic Biofuel Cell

High power enzymatic biofuel cell based on naphthoquinone-mediated oxidation of glucose by glucose oxidase in a carbon nanotube 3D matrix

2013 ◽  
Vol 15 (14) ◽  
pp. 4892 ◽  
Author(s):  
Bertrand Reuillard ◽  
Alan Le Goff ◽  
Charles Agnès ◽  
Michael Holzinger ◽  
Abdelkader Zebda ◽  
...  
Keyword(s):  
Carbon Nanotube ◽  
Glucose Oxidase ◽  
High Power ◽  
Biofuel Cell ◽  
Enzymatic Biofuel Cell ◽  
3D Matrix ◽  
Oxidation Of Glucose ◽  
Mediated Oxidation

Enzyme precipitate coatings of glucose oxidase onto carbon paper for biofuel cell applications

2011 ◽  
Vol 109 (2) ◽  
pp. 318-324 ◽  
Author(s):  
Mike Fischback ◽  
Ki Young Kwon ◽  
Inseon Lee ◽  
Su Jeong Shin ◽  
Hyun Gyu Park ◽  
...  
Keyword(s):  
Glucose Oxidase ◽  
Biofuel Cell ◽  
Carbon Paper

scholarly journals Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks

2008 ◽  
Vol 105 (40) ◽  
pp. 15275-15280 ◽  
Author(s):  
Ian R. Wheeldon ◽  
Joshua W. Gallaway ◽  
Scott Calabrese Barton ◽  
Scott Banta
Keyword(s):  
Polyphenol Oxidase ◽  
Building Block ◽  
Leucine Zipper ◽  
Electrical Contact ◽  
Building Blocks ◽  
Coiled Coils ◽  
Biofuel Cell ◽  
Random Coil ◽  
Catalytic Current ◽  
And Function

Here, we present two bifunctional protein building blocks that coassemble to form a bioelectrocatalytic hydrogel that catalyzes the reduction of dioxygen to water. One building block, a metallopolypeptide based on a previously designed triblock polypeptide, is electron-conducting. A second building block is a chimera of artificial α-helical leucine zipper and random coil domains fused to a polyphenol oxidase, small laccase (SLAC). The metallopolypeptide has a helix–random-helix secondary structure and forms a hydrogel via tetrameric coiled coils. The helical and random domains are identical to those fused to the polyphenol oxidase. Electron-conducting functionality is derived from the divalent attachment of an osmium bis-bipyrdine complex to histidine residues within the peptide. Attachment of the osmium moiety is demonstrated by mass spectroscopy (MS-MALDI-TOF) and cyclic voltammetry. The structure and function of the α-helical domains are confirmed by circular dichroism spectroscopy and by rheological measurements. The metallopolypeptide shows the ability to make electrical contact to a solid-state electrode and to the redox centers of modified SLAC. Neat samples of the modified SLAC form hydrogels, indicating that the fused α-helical domain functions as a physical cross-linker. The fusion does not disrupt dimer formation, a necessity for catalytic activity. Mixtures of the two building blocks coassemble to form a continuous supramolecular hydrogel that, when polarized, generates a catalytic current in the presence of oxygen. The specific application of the system is a biofuel cell cathode, but this protein-engineering approach to advanced functional hydrogel design is general and broadly applicable to biocatalytic, biosensing, and tissue-engineering applications.

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