Thermal stability of bioactive enzymatic papers.
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.
Australian Pulp and Paper Institute, Department of Chemical Engineering, Monash University, Clayton, VIC 3800, Australia.
Mohidus Samad
MS
Khan
Xu
X
Li
Wei
W
Shen
Gil
G
Garnier
D000327:Adsorption; D000469:Alkaline Phosphatase / Q000378:metabolism*; D002021:Buffers; D002138:Calibration; D004396:Coloring Agents; D004789:Enzyme Activation; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010209:Paper; D011327:Printing; D013499:Surface Properties; D013696:Temperature; D013997:Time Factors
D002021:Buffers; D004396:Coloring Agents; D006735:Horseradish Peroxidase; D000469:Alkaline Phosphatase