Encapsulation hemoglobin in ordered mesoporous silicas: Influence factors for immobilization and bioelectrochemistry

  • Yuezhong Xian
  • , Yang Xian
  • , Lihui Zhou
  • , Fanghua Wu
  • , Yun Ling
  • , Litong Jin*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

101 Scopus citations

Abstract

The encapsulation of hemoglobin (Hb) on the mesoporous silicas SBA-15 and Au-doped SBA-15 (Au-SBA-15) has been studied as a model protein adsorption system. The influences of solution pH, structure of mesoporous silicas and gold nanoparticles incorporation on Hb immobilization are investigated in detail. The spectral characteristics of Hb/SBA-15 and Hb/Au-SBA-15 nanoconjugate show an absorption curve quite similar to that of native Hb, indicating that Hb retains its higher-order structure in the mesopores of SBA-15. Direct electrochemistry of Hb is obtained when Hb is adsorpted by mesoporous silicas SBA-15 or Au-SBA-15. Moreover, Hb/Au-SBA-15 exerts enhancing electron transfer ability because of the Au incorporation. Additionally, the Hb/Au-SBA-15 displays good electrocatalytic reduction of hydrogen peroxide with a detection limit of 1.0 μM, about 3 times as low as that for the Hb/SBA-15. The Hb/Au-SBA-15 exhibits higher peroxidase-like activity with the apparent Michaelis-Menton constant (Km) of 2.87 mM, significantly lower than the 7.78 mM value for the Hb/SBA-15.

Original languageEnglish
Pages (from-to)142-148
Number of pages7
JournalElectrochemistry Communications
Volume9
Issue number1
DOIs
StatePublished - Jan 2007

Keywords

  • Au-SBA-15
  • Direct chemistry
  • Hemoglobin
  • Hydrogen peroxide
  • SBA-15

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