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Bovine carbonic anhydrase H retains its overall conformation when encapsulated in silica monoliths by the sol-gel method. Upon gradual heating the enzyme in solution precipitates at 64 °C, whereas the encapsulated enzyme does not; it unfolds, with the nominal melting temperature of 51 ± 3 °C. Even at 74.0 °C, the encapsulated enzyme is only ca. 77 % unfolded, but it does not refold upon cooling. Upon treatment with guanidinium chloride, the degree of enzyme unfolding is 100 % in solution but only ca. 83 % within the silica matrix. Again, the enzyme does not refold upon removal of the denaturing agent from the glass. The glass matrix constrains the motions of the encapsulated protein molecules and prevents both their full unfolding and refolding. The former may be taken for "stabilization," the later for

Characterization of sol-gel silica glass and its composites through study of physical and chemical properties of entrapped molecules