A bienzyme channeling glucose sensor with a wide concentration range based on co-entrapment of enzymes in SBA-15 mesopores

Zhihui Dai, Jianchun Bao, Xiaodi Yang, Huangxian Ju

Research output: Contribution to journalArticlepeer-review

100 Scopus citations

Abstract

A novel bienzyme-channeling sensor was constructed by entrapping glucose oxidase (GOD) and horseradish peroxidase (HRP) in the mesopores of well-ordered hexagonal mesoporous silica structures (SBA-15). The SBA-15 mesoporous materials accelerated the electron transfer between the entrapped HRP and electrode. Both HRP and GOD retained their catalytic activities in the bienzyme-entrapped SBA-15 film. In presence of glucose the enzymatic reaction of GOD-glucose-dissolved oxygen system generated hydrogen peroxide in the bienzyme-entrapped mesopores, which was immediately reduced at -0.40 V by an electrocatalytic reaction with the HRP entrapped in the same mesopore to lead to a sensitive and fast amperometric response. Thus the bienzyme channeling could be used for the detection of glucose with excellent performance without the addition of any mediator. Optimization of the experimental parameters was performed with regard to pH, operating potential and temperature. The detection limit was down to 2.7 × 10-7 M with a very wide linear range from 3.0 × 10-6 to 3.4 × 10-2 M. The constructed bienzyme channeling provided a strategy for amperometric detection of oxidase substrates by co-entrapping the corresponding oxidase and HRP in the mesoporous materials.

Original languageEnglish
Pages (from-to)1070-1076
Number of pages7
JournalBiosensors and Bioelectronics
Volume23
Issue number7
DOIs
StatePublished - 28 Feb 2008
Externally publishedYes

Keywords

  • Enzyme-channeling sensor
  • Glucose
  • Glucose oxidase
  • Horseradish peroxidase
  • SBA-15

Fingerprint

Dive into the research topics of 'A bienzyme channeling glucose sensor with a wide concentration range based on co-entrapment of enzymes in SBA-15 mesopores'. Together they form a unique fingerprint.

Cite this