Adsorption and inactivation behavior of horseradish peroxidase on various substrates.
To produce bioactive papers, i.e. papers incorporating biomolecules that are useful for analyte detection, adequate immobilization strategies should be devised. In this article, the physical immobilization behavior and activity of the enzyme horseradish peroxidase (HRP) on various papermaking substrates were studied. The papermaking substrates included amorphous and crystalline cellulose, calcium carbonate, styrene butadiene latex, polystyrene, and both negatively charged rayon and rayon with a positively charged layer. It was found that HRP adsorption improves as the hydrophobicity of the substrate increases; however, excessive hydrophobicity produces enzyme deactivation. HRP-calcium carbonate binding was weak and the enzyme loading was scant. These results provided a possible explanation for the poor analytical signals observed in pigment-coated papers when used as bioactive paper supports. Electrostatic effects played a minor role in HRP adsorption behavior.
Di Risio
Sabina
S
Dept. Chem. Eng. App. Chem., University of Toronto, 200 College St., Toronto, ON, M5S 3E5 Canada. sabina.dirisio@utoronto.ca
Yan
Ning
N
D000327:Adsorption; D004789:Enzyme Activation; D006735:Horseradish Peroxidase / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008855:Microscopy, Electron, Scanning; D013379:Substrate Specificity; D013499:Surface Properties
D006735:Horseradish Peroxidase