Study of bi-enzyme immobilization onto layered double hydroxides nanomaterials for histamine biosensor application

J Nanosci Nanotechnol. 2011 Oct;11(10):8798-803. doi: 10.1166/jnn.2011.3461.

Abstract

In this work, we present the development of a hybrid biomembrane based on the immobilization of diamine oxidase (DAO) into LDH thin films for histamine detection. The LDHs preselected as host matrixes are: hydrotalcites (Mg2Al(CO3)0.5(OH)6), lowaite (Mg4Fe(OH)10Cl) and hydrocalumite (Ca2Al(OH)6Cl). The immobilized probes were characterized by atomic force microscopy (AFM) and attenuated total reflection infrared spectroscopy (IR-ATR mode). The analysis of these results shows that the immobilization of DAO occurs with all type of selected LDH and is stable after a 7 day-immersion in phosphate buffer solution. The LDH incorporating magnesium or calcium divalent cations present high-quality surface topology for DAO immobilization and the ability to keep the enzyme in a well conformation for biogenic amines catabolism and histamine detection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aluminum Hydroxide / chemistry
  • Amine Oxidase (Copper-Containing) / chemistry*
  • Biosensing Techniques*
  • Calcium / chemistry
  • Enzymes, Immobilized / chemistry*
  • Histamine / chemistry*
  • Hydroxides / chemistry*
  • Magnesium / chemistry
  • Magnesium Hydroxide / chemistry
  • Microscopy, Atomic Force / methods
  • Nanostructures / chemistry*
  • Powders / chemistry
  • Spectrophotometry, Infrared / methods
  • Surface Properties

Substances

  • Enzymes, Immobilized
  • Hydroxides
  • Powders
  • hydrotalcite
  • Aluminum Hydroxide
  • Histamine
  • Amine Oxidase (Copper-Containing)
  • Magnesium
  • Magnesium Hydroxide
  • Calcium