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Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability

  • Dongxiang Li
  • , Qiang He
  • , Yue Cui
  • , Li Duan
  • , Junbai Li*
  • *Corresponding author for this work
  • Peking University
  • Max Planck Institute of Colloids and Interfaces

Research output: Contribution to journalArticlepeer-review

Abstract

Immobilized proteins and enzymes were widely investigated in medical field as well as in food and environmental fields. In this paper, glucose oxidase (GOD) monolayer was covalently immobilized on the surface of gold nanoparticles (AuNPs) to fabricate bioconjugate complex. The citrate-stabilized AuNPs were first functionalized by a carboxyl-terminated alkanethiol and the terminal carboxyl groups were subsequently bonded with side-chain amino groups of protein surface through EDC/NHS coupling reaction. The enzyme activity assays of the obtained bioconjugates display an enhanced thermostability and similar pH-dependence behavior in contrast with that of free enzyme. Such GOD/AuNPs bioconjugates can be considered as a catalytic nanodevice to construct nanoreactor based on glucose oxidation reaction for biotechnological purpose.

Original languageEnglish
Pages (from-to)488-493
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume355
Issue number2
DOIs
StatePublished - 6 Apr 2007
Externally publishedYes

Keywords

  • Bioconjugate
  • Enzyme activity
  • Glucose oxidase
  • Gold nanoparticles
  • Immobilization

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