Stabilization of enzymes in nanoporous materials for biosensor applications.
In this study we present the results obtained from efforts to stabilize the inherently unstable m-AChE in nanoporous materials, for the development of biosensors with increased operational stability. Based on existing theoretical models, the entrapment of proteins into relatively small rigid cages drastically increases the stability of these proteins, as this is manifested by their decreased tendency to unfold. The use of two different meso/nanomaterials for the immobilization of the m-AChE shows that there is both a decrease in the leaching of the protein from the biosensor membrane to the test solution, as well as a drastic increase in the operational stability of the resulting biosensor.
Sotiropoulou
Sofia
S
Laboratory of Analytical Chemistry, Department of Chemistry, University of Crete, Knossou Avenue, 71 409 Iraklion, Crete, Greece.
Vamvakaki
Vicky
V
Chaniotakis
Nikos A
NA
D000110:Acetylcholinesterase / Q000032:analysis* / Q000737:chemistry*; D015374:Biosensing Techniques / Q000379:methods*; D020099:Coated Materials, Biocompatible / Q000032:analysis / Q000737:chemistry; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000032:analysis / Q000737:chemistry; D008422:Materials Testing; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D016062:Porosity
D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D000110:Acetylcholinesterase