Protein conformation plays a crucial role in determining both the catalytic efficiency and the chemo-, regio- and enantioselectivity of enzymes, thus eventually influencing their exploitability in biotechnological applications. Inevitably, immobilisation processes alter the natural molecular environment of enzymes, and quite often affect their catalytic activity through different mechanisms such as reduced accessibility of the substrate to the catalytic active centre, loss of the enzyme dynamic properties and alteration of the conformational integrity of the enzyme. This tutorial review outlines first the most common spectroscopic techniques used for investigating the conformation of immobilized proteins, and then examines how protein loading and polar and hydrophobic/hydrophilic interactions with the carrier affect the structural and dynamic features of enzymes. The nanoscale-level studies in which protein conformational changes, determined either by experimental approaches or by homology modelling, are correlated with the size and shape of the support are also discussed. Altogether, these results should provide useful information on how supports and/or enzymes have to be tailored to improve biocatalyst performance.
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