Biocolloids with Ordered Urease Multilayer Shells as Enzymatic Reactors
The preparation of biocolloids with organized enzyme-containing multilayer shells for exploitation as colloidal enzymatic nanoreactors is described. Urease multilayers were assembled onto submicrometer-sized polystyrene spheres by the sequential adsorption of urease and polyelectrolyte, in a predete...
Saved in:
Published in | Analytical chemistry (Washington) Vol. 73; no. 17; pp. 4212 - 4217 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
01.09.2001
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | The preparation of biocolloids with organized enzyme-containing multilayer shells for exploitation as colloidal enzymatic nanoreactors is described. Urease multilayers were assembled onto submicrometer-sized polystyrene spheres by the sequential adsorption of urease and polyelectrolyte, in a predetermined order, utilizing electrostatic interactions for layer growth. The catalytic activity of the biocolloids increased proportionally with the number of urease layers deposited on the particles, demonstrating that biocolloid particles with tailored enzymatic activities can be produced. It was further found that precoating the latex spheres with nanoparticles (40-nm silica or 12-nm magnetite) enhanced both the stability (with respect to adsorption) and enzymatic activity of the urease multilayers. The presence of the magnetite nanoparticle coating also provided a magnetic function that allowed the biocolloids to be easily and rapidly separated with a permanent magnet. The fabrication of such colloids opens new avenues for the application of bioparticles and represents a promising route for the creation of complex catalytic particles. |
---|---|
Bibliography: | istex:FAB6FFB08FBD3CB1312BCB00B3FE540BE89C2825 ark:/67375/TPS-XPBM6Q90-2 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0003-2700 1520-6882 |
DOI: | 10.1021/ac010118d |