1. Thermal stability of bioactive enzymatic papers.
- Author
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Khan MS, Li X, Shen W, and Garnier G
- Subjects
- Adsorption, Buffers, Calibration, Coloring Agents, Enzyme Activation, Hydrogen-Ion Concentration, Kinetics, Printing, Surface Properties, Time Factors, Alkaline Phosphatase metabolism, Horseradish Peroxidase metabolism, Paper, Temperature
- 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.
- Published
- 2010
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