The sol-gel method is a synthetic method that allows to form porous solid matrices. Such matrices have been used in the fields of organic chemistry and inorganic chemistry for a variety of applications. For silica based starting material the resulting matrix is a -Si-O-Si-O- amorphous network which is transparent, chemically and mechanically stable and nontoxic. In particular these matrices can serve to encapsulate proteins/enzymes entrapping them sterically without covalent bonding that could alter the protein structure. Once the sol-gel has solidified, the large encapsulated protein is effectively immobilized not able to diffuse out of its trapping site. However, when the sol-gel matrix is bathed in a buffer the extensive network of pores that run through the sol-gel is filled with water and small molecules such that the encapsulated protein is fully solvated. Since, small molecules are able to diffuse in and out of the sol-gel, ligands, substrates can reach the encapsulated enzyme and the enzyme remains active within the sol-gel matrix. More over some earlier studies have suggest that depending on the encapsulation conditions such encapsulated enzymes remain intact and functional. Here we present results of our studies characterizing the enzymatic activity and the stability of heme-proteins in buffer, organic solvents and when encapsulated within sol-gel matrices and bathed in buffer vs. organic solvents.

Catalytic activity and stability of heme proteins encapsulated within sol-gel matrices

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