Enzymes are versatile catalysts in the laboratory and on an industrial scale. To broaden their applicability in the laboratory and to ensure their (re)use in manufacturing the stability of enzymes can often require improvement. Immobilisation can address the issue of enzymatic instability. Immobilisation can also help to enable the employment of enzymes in different solvents, at extremes of pH and temperature and exceptionally high substrate concentrations. At the same time substrate-specificity, enantioselectivity and reactivity can be modified. However, most often the molecular and physical–chemical bases of these phenomena have not been elucidated yet. This tutorial review focuses on the understanding of enzyme immobilisation.

Mesoporous silicates (MPS) are attractive materials for the immobilisation of enzymes. They possess ordered pore structures, narrow pore size distributions, large surface areas, high stability and can be chemically modified with various functional groups. The properties of MPS materials are reviewed in terms of their ability to act as supports for enzymes for use in biocatalysis with a particular focus on the ability to tailor the surface functionalization of the MPS to suit a specific enzyme. While many reports of the immobilisation of enzymes on MPS have been described, their use as biocatalytic supports is limited. Large scale reactors based on MPS will require continuous flow systems where the properties of the support can be tailored while allowing fluid flow at reasonable low pressure.