A QCM study of the immobilization of beta-galactosidase on polyelectrolyte surfaces: effect of the terminal polyion on enzymatic surface activity.

@article{Hamlin2007AQS,
  title={A QCM study of the immobilization of beta-galactosidase on polyelectrolyte surfaces: effect of the terminal polyion on enzymatic surface activity.},
  author={Rebecca E Hamlin and Talya L. Dayton and Lewis E. Johnson and Malkiat S. Johal},
  journal={Langmuir : the ACS journal of surfaces and colloids},
  year={2007},
  volume={23 8},
  pages={4432-7}
}
This work describes the immobilization of beta-galactosidase onto polyelectrolyte multilayer assemblies of the polyanion poly[1-[4-(3-carboxy-4-hydroxyphenylazo)benzenesulfonamido]-1,2-ethanediyl, sodium salt] (PAZO) and the polycation poly(ethylenimine) (PEI) constructed by electrostatic self-assembly (ESA). A single layer of beta-galactosidase was deposited over a precursor film comprising up to five bilayers of the PEI/PAZO polyelectrolyte pair. The enzyme was deposited on both the… CONTINUE READING