Abstract
The lyophilization of proteins in the presence of template molecules has been suggested as a means of creating “de novo” binding and catalytic sites. The bio-imprinting of bovine serum albumin (BSA) was investigated using the binding of p-hydroxybenzoic acid ( pHBA) and the β-elimination of 4-fluoro-4-( p-nitrophenyl)butan-2-one as model systems. It was found that both binding and catalytic activity could be enhanced by a factor of approximately 3 over that of the native protein but that no specificity was introduced. It was also found that activity was restricted to active groups on the surface of the imprinted proteins which could be influenced by this technique. A synergistic effect between lysine and aspartic acid groups was observed. This suggested that ionised carboxylic acid and amine groups are involved in bio-imprinting and further suggests ways in which the technique could be developed to produce novel protein based catalysts.
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