Enzyme Electrodes for Glucose Oxidation Prepared by Electropolymerization of Pyrrole

2007 ◽  
Vol 85 (5) ◽  
pp. 489-493 ◽  
Author(s):  
E.H. Yu ◽  
K. Sundmacher
2013 ◽  
Vol 43 ◽  
pp. 30-37 ◽  
Author(s):  
Peter Ó Conghaile ◽  
Sascha Pöller ◽  
Domhnall MacAodha ◽  
Wolfgang Schuhmann ◽  
Dónal Leech

2012 ◽  
Vol 25 (1) ◽  
pp. 94-100 ◽  
Author(s):  
Domhnall MacAodha ◽  
Peter Ó Conghaile ◽  
Brenda Egan ◽  
Paul Kavanagh ◽  
Christoph Sygmund ◽  
...  

2012 ◽  
Vol 14 (42) ◽  
pp. 14667 ◽  
Author(s):  
Domhnall MacAodha ◽  
Maria Luisa Ferrer ◽  
Peter Ó Conghaile ◽  
Paul Kavanagh ◽  
Dónal Leech

2021 ◽  
Vol 7 (10) ◽  
pp. 17-24
Author(s):  
N. Lakina ◽  
V. Doluda ◽  
V. Matveeva ◽  
A. Sidorov ◽  
G. Rabinovich

Abstract. To modify graphite electrodes with a conductive enzyme polymer matrix, the method of drip application of a liquid polymer solution of various compositions was used: polyvinylpyrrolidone (40%), chitosan (0.1%), glutaric dialdehyde (0.1%), glucoxidase and peroxidase in a ratio of 2:5. To assess the effect of the immobilization time (x1), the pH of immobilization (x2) and the enzyme/carrier ratio (x3) on the activity of the enzyme electrodes, a three-factor and three-level Box-Benken and RSM design was used. This model was able to adequately predict the results of immobilization within the range of variables used. The most favorable conditions and the largest number of molecules of the enzyme complex are in the electrochemically active state when they are immobilized on PVP using modifying agents chitosan and glutaraldehyde. The results demonstrate that the productivity of the enzymatic biofuel element is directly proportional to the activity of the immobilized GOX/HRP complex, since in this case the glucose oxidation reaction can proceed more efficiently.


2007 ◽  
Vol 115 (S 1) ◽  
Author(s):  
K Stadlbauer ◽  
B Brunmair ◽  
Z Szöcs ◽  
M Krebs ◽  
A Luger ◽  
...  

1997 ◽  
Vol 78 (5) ◽  
pp. 805-813 ◽  
Author(s):  
Kjell Holtenius ◽  
Paul Holtenius

The metabolic effects of a phlorizin-induced drainage of glucose were studied in six lactating ewes with or without peroral alanine drenches in a study of crossover design. Phlorizin gave rise to a small, but significant, elevation of plasma β-hydroxybutyrate. The plasma level of alanine decreased by about 30 % due to the phlorizin injections and alanine was negatively correlated to β-hydroxybutyrate. The plasma level of free fatty acids increased due to phlorizin. Plasma insulin and glucose concentrations were not significantly affected by phlorizin while glucagon level showed a small but significant increase. Peroral alanine drenches to phlorizin-treated ewes gave rise to a transitory elevation of alanine in plasma. The plasma level of free fatty acids was about 40 % lower in phlorizin-treated ewes receiving alanine and β-hydroxybutyrate tended to be lower (P < 0.08). We suggest that β-hydroxybutyrate, apart from its function as an oxidative fuel, might play an important role by limiting glucose oxidation and protein degradation in skeletal muscles during periods of negative energy balance in ruminants. Furthermore, it is suggested that alanine supplementation decreases lipolysis and ketogenesis in lactating ewes.


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