Biocatalytic silicates, composite materials composed of α-chymotrypsin and a silicate prepolymer, were prepared via a two-step polymerization process following solubilization of the enzyme in the polymerization media. This new approach resulted in active and stable composites, and a calculated half-life of over 350 days in aqueous buffer at 30°C. The high stability and activity of this biocatalytic silicate was likely due to the covalent attachment between α-chymotrypsin and the silicate matrix. The protease-containing silicate was resistant to fouling by nonselective protein binding, as demonstrated by the dramatically reduced binding of human serum albumin to the silicate material when compared to that of a silicate containing pre-inactivated α-chymotrypsin.
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