Thermal stability of bioactive enzymatic papers

Colloids Surf B Biointerfaces. 2010 Jan 1;75(1):239-46. doi: 10.1016/j.colsurfb.2009.08.042. Epub 2009 Sep 3.

Abstract

The thermal stability of two enzymes adsorbed on paper, alkaline phosphatase (ALP) and horseradish peroxidase (HRP), was measured using a colorimetric technique quantifying the intensity of the product complex. The enzymes adsorbed on paper retained their functionality and selectivity. Adsorption on paper increased the enzyme thermal stability by 2-3 orders of magnitude compared to the same enzyme in solution. ALP and HRP enzymatic papers had half-lives of 533 h and 239 h at 23 degrees C, respectively. The thermal degradation of adsorbed enzyme was found to follow two sequential first-order reactions, indication of a reaction system. A complex pattern of enzyme was printed on paper using a thermal inkjet printer. Paper and inkjet printing are ideal material and process to manufacture low-cost-high volume bioactive surfaces.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Alkaline Phosphatase / metabolism*
  • Buffers
  • Calibration
  • Coloring Agents
  • Enzyme Activation
  • Horseradish Peroxidase / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Paper*
  • Printing
  • Surface Properties
  • Temperature*
  • Time Factors

Substances

  • Buffers
  • Coloring Agents
  • Horseradish Peroxidase
  • Alkaline Phosphatase