Flow screen-printed amperometric detection of p-nitrophenol in alkaline phosphatase-based assays

Anal Bioanal Chem. 2006 Aug;385(7):1202-8. doi: 10.1007/s00216-006-0367-8. Epub 2006 Mar 11.

Abstract

p-Nitrophenyl phosphate is one of the most widely used substrates for alkaline phosphatase in ELISAs because its yellow, water-soluble product, p-nitrophenol, absorbs strongly at 405 nm. p-Nitrophenol is also electroactive; an oxidative peak at 0.97 V (vs. an Ag pseudoreference electrode) is obtained when a bare screen-printed carbon electrode is used. When an amperometric detector was coupled to a flow-injection analysis system the detection limit achieved for p-nitrophenol was 2x10(-8) mol L(-1), almost two orders of magnitude lower than that obtained by measuring the absorbance of the compound. By use of this electrochemical detection method, measurement of 7x10(-14) mol L(-1) alkaline phosphatase was achieved after incubation for 20 min. The feasibility of coupling immunoassay to screen-printed carbon electrode amperometric detection has been demonstrated by performing an ELISA for detection of pneumolysin, a toxin produced by Streptococcus pneumoniae, which causes respiratory infections. The method is simple, reproducible, and much more sensitive than traditional spectrophotometry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase*
  • Bacterial Proteins / analysis
  • Electrochemistry / methods*
  • Electrodes
  • Enzyme-Linked Immunosorbent Assay / methods*
  • Feasibility Studies
  • Methods
  • Nitrophenols / analysis*
  • Streptolysins / analysis

Substances

  • Bacterial Proteins
  • Nitrophenols
  • Streptolysins
  • plY protein, Streptococcus pneumoniae
  • Alkaline Phosphatase
  • 4-nitrophenol