By Topic

Amperometric ATP Biosensors Based on Coimmobilizations of p-Hydroxybenzoate Hydroxylase, Glucose-6-Phosphate Dehydrogenase, and Hexokinase on Clark-Type and Screen-Printed Electrodes

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

1 Author(s)
Yue Cui ; Dept. of Mech. & Aerosp. Eng., Princeton Univ., Princeton, NJ, USA

Two types of amperometric trienzyme ATP biosensors were developed based on new combinations of enzymes and electrodes by using the coimmobilizations of p-hydroxybenzoate hydroxylase (HBH), glucose-6-phosphate dehydrogenase (G6PDH), and hexokinase (HEX) on a Clark-type oxygen electrode and on a screen-printed electrode. The principles of the determinations are as follows: HEX transfers the phosphate group from ATP to glucose to form glucose-6-phosphate. G6PDH catalyzes the specific dehydrogenation of glucose-6-phosphate by consuming NADP+. The product, NADPH initiates the irreversible hydroxylation of p-hydroxybenzoate by HBH to consume dissolved oxygen which results in a detectable signal on a Clark-type electrode and generate 3, 4-dihydroxybenzoate which results in a detectable signal on a screen-printed electrode. Both sensors show high-performance characteristics with broad detection ranges, short measuring times and good specificities.

Published in:

Sensors Journal, IEEE  (Volume:10 ,  Issue: 5 )