Encapsulation of recombinant Escherichia coli cells expressing a biocatalyst has the potential to produce stable, long-lasting enzyme activity that can be used for numerous applications. The current study describes the use of this technology with recombinant E. coli cells expressing the atrazine-dechlorinating enzyme AtzA in a silica/polymer porous gel. This novel recombinant enzyme-based method utilizes both adsorption and degradation to remove atrazine from water. A combination of silica nanoparticles (Ludox TM40), alkoxides, and an organic polymer was used to synthesize a porous gel. Gel curing temperatures of 23 or 45 A degrees C were used either to maintain cell viability or to render the cells non-viable, respectively. The enzymatic activity of the encapsulated viable and non-viable cells was high and extremely stable over the time period analyzed. At room temperature, the encapsulated non-viable cells maintained a specific activity between (0.44 A +/- 0.06) mu mol/g/min and (0.66 A +/- 0.12) mu mol/g/min for up to 4 months, comparing well with free, viable cell-specific activities (0.61 A +/- 0.04 mu mol/g/min). Gels cured at 45 A degrees C had excellent structural rigidity and contained few viable cells, making these gels potentially compatible with water treatment facility applications. When encapsulated, non-viable cells were assayed at 4 A degrees C, the activity increased threefold over free cells, potentially due to differences in lipid membranes as shown by FTIR spectroscopy and electron microscopy.