Abstract

Adsorption of model proteins bovine serum albumin (BSA), myoglobin (MYO) and lysozyme (LSZ) from Tris and phosphate buffer solutions were examined using tobermorite with a layered structure consisting of CaO polyhedral and silicate tetrahedral layers. BSA was easily adsorbed on tobermorite from Tris buffer, compared with MYO and LSZ. In contrast, the amount of LSZ adsorbed by tobermorite from phosphate buffer was more than fourfold higher than the amounts of the other proteins. Phosphate ions adsorbed on the surface of tobermorite caused selective adsorption of basic proteins on tobermorite.

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