Cytochrome c (cyt. c, molecular size of 2.5 nm © 2.5 nm © 3.7 nm) was immobilized on six types of mesoporous silicates (MPS), having pore sizes from 2.8 to 15.0 nm, and their catalytic activities were evaluated by oxidation of thioanisol with H 2 O 2 . Among the silica materials, cyt. c immobilized on MPS pore size of 3.4 nm) showed the best catalytic activity, and its relative activity was improved 1.7 times over that of cyt. c solution. Enhancement of catalytic activity was obtained by immobilization on MPS having a similar size (mesopore) to the molecular size of cyt. c. Activity stability of cyt. c was also evaluated under the various conditions that caused protein inactivation, like HCl, urea, methanol, and guanidine. As results, stability was improved by the immobilization on silica material having a larger pore size (15.0 nm), offered an environment for encapsulating entire cyt. c molecules, inhibiting cyt. c from unfolding and irreversible decomposition.