Amperometric trienzyme ATP biosensors based on the coimmobilization of salicylate hydroxylase, glucose-6-phosphate dehydrogenase, and hexokinase

Yue Cui*, John P. Barford, Reinhard Renneberg

*Corresponding author for this work

Research output: Contribution to journalLetterpeer-review

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 languageEnglish
Pages (from-to)1-4
Number of pages4
JournalSensors and Actuators, B: Chemical
Volume132
Issue number1
DOIs
Publication statusPublished - 28 May 2008

Keywords

  • ATP
  • Biosensor
  • Glucose-6-phosphate dehydrogenase
  • Hexokinase
  • Salicylate hydroxylase

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