2009 Annual Meeting

(190a) Stability and Reactivity of Enzymatic Papers

Authors

Mohidus Samad Khan - Presenter, BioPRIA, Australian Pulp and Paper Institution, Monash University
Wei Shen - Presenter, Australian Pulp and Paper Institution, Monash University
Gil Garnier - Presenter, BioPRIA, Australian Pulp & Paper Institute, Monash University


Bioactive papers and paper diagnostics are getting a reality for their low cost, selectivity and application flexibility. Critical is the thermal stability of bioactive papers that need to be shipped and stored. This study quantifies the thermal stability and reactivity of enzymatic bioactive papers.

The reaction kinetics, thermal stability, functionality and selectivity of bioactive enzymatic papers were investigated. The Alkaline phosphatase (ALP) enzyme was stabilized on paper using a cationic polymer: polyacrylamide. The reactivity and thermal stability of ALP adsorbed on paper was measured using a colorimetric technique quantifying the intensity of the product complex. The ALP adsorbed on paper retains its functionality and selectivity. Adsorption of ALP on paper increased the enzyme thermal stability compared to the same enzyme in solution. Complex patterns of enzyme were also printed using a thermal inkjet printer to demonstrate the concept of paper-based bioassays manufacturing. Paper is an ideal material for functional bioactive surfaces.