Abstract
Two types of amperometric ATP biosensors were developed by using the coimmobilization of salicylate hydroxylase (SHL, EC 1.14.13.1), glucose-6-phosphate dehydrogenase (G6PDH, EC1.1.1.49), and hexokinase (HEX, EC 2.7.1.1) on a Clark-type oxygen electrode and on a screen-printed electrode. The principles of the determination schemes 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 NAD+. The product, NADH initiates the irreversible decarboxylation and hydroxylation of salicylate by SHL to consume dissolved oxygen and generate catechol. This results in a detectable signal on a Clark-type electrode due to the SHL-enzymatic consumption of oxygen, or a detectable signal on a screen-printed electrode due to the SHL-enzymatic generation of catechol in the measurement of ATP. Both sensors show high performance characteristics with broad detection ranges, short measuring times, and good specificities.
| Original language | English |
|---|---|
| Pages (from-to) | 1-4 |
| Number of pages | 4 |
| Journal | Sensors and Actuators, B: Chemical |
| Volume | 132 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 28 May 2008 |
Keywords
- ATP
- Biosensor
- Glucose-6-phosphate dehydrogenase
- Hexokinase
- Salicylate hydroxylase
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