The significant activation of subtilisin Carlsberg for catalysis in hexane by immobilization on fumed silica nanoparticles has been shown by us previously. Since the results for this activation were similar to the best published activation method at the time (lyophilization in presence of inorganic salts) we were interested if fumed silica activation can be generalized to other enzymatically catalyzed reactions in solvents. Here we apply fumed silica activation to a model esterification catalyzed by crude C. Antarctica Lipase B in hexane and we compare to a commercial preparation of the same enzyme (Novozyme 435). The activity of our fumed silica activated enzyme preparation for the model esterification appears on the same order as that of Novozyme 435 (normalized by active units of enzyme). The activity also depends on the amount of silica available for protein immobilization. It appears that fumed silica activation for enzymatic catalysis in solvents can be applied to enzymes other than S. Carlsberg. This appears to support our previous hypothesis that the area available for enzyme immobilization is crucial for enzyme activation.