Biocompatible surfaces are of considerable interest in biotechnology, with application in the immobilization of, inter alia , proteins, [1] (including enzymes [2] ) and DNA. [3] Commonly used substrates for such immobilization include silicon, [4] mica, [5] gold, [6] and polymeric matrices. [7] Amongst the methods available for enzyme immobilization, adsorption appears attractive because of its simplicity and low cost. However, adsorption generally does not lead to very stable immobilization, and enzymes tend to become desorbed during catalysis and recycling, leading to decreased activity over time. Furthermore, since there is a lack of control over the enzyme positioning, only a fraction of the enzyme may be available for catalysis, reducing significantly the support efficiency.
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Fernández‐Trillo et al. (2008) studied this question.
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