Development of amperometric biosensor for glucose based on a novel attractive enzyme immobilization matrix: Calcium carbonate nanoparticles

2007 ◽  
Vol 22 (8) ◽  
pp. 1612-1617 ◽  
Author(s):  
Dan Shan ◽  
Mingjuan Zhu ◽  
Huaiguo Xue ◽  
Serge Cosnier
2001 ◽  
Vol 73 (12) ◽  
pp. 1993-1999 ◽  
Author(s):  
P. V. Climent ◽  
M. L. M. Serralheiro ◽  
M. J. F. Rebelo

An amperometric biosensor based on the enzyme polyphenoloxidase (PPO), which makes the bioelectrocatalysis of phenolic compounds, was developed and optimized using cathecol as substrate. Polyethersulphone membranes were used for enzyme immobilization. Polyphenoloxidase oxidizes monophenols (cresolase activity) and diphenols (catecholase activity) into the corresponding o-quinones; the o-quinones formed in the enzymatic catalysis are then reduced back to cathecol at ­200 mV (vs. Ag, AgCl) at a platinum electrode. The polyphenoloxidase immobilized was from commercial origin or extracted from mushrooms. p-Cresol and phenol substrates were also tested. Reproducibility, response time, linearity, sensitivity, and stability of the biosensor were studied.


2001 ◽  
Vol 13 (18) ◽  
pp. 1469-1474 ◽  
Author(s):  
Manihar Situmorang ◽  
J. Justin Gooding ◽  
D. Brynn Hibbert ◽  
Donald Barnett

2014 ◽  
Vol 47 (8) ◽  
pp. 1361-1374 ◽  
Author(s):  
Tomoko Gessei ◽  
Takahiro Arakawa ◽  
Hiroyuki Kudo ◽  
Hirokazu Saito ◽  
Kohji Mitsubayashi

2014 ◽  
Vol 195 ◽  
pp. 58-62 ◽  
Author(s):  
Rodolfo Mundaca-Uribe ◽  
Francisca Bustos-Ramírez ◽  
Claudio Zaror-Zaror ◽  
Mario Aranda-Bustos ◽  
Jose Neira-Hinojosa ◽  
...  

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