Enzyme Immobilization

Dear Collegues,

The immobilization of enzymes and proteins is a seemingly ancient research area that still attracts great interest. The initial interest in enzyme immobilization was motivated by a desire to simplify the reuse of these expensive biocatalysts. However, at present, immobilization has developed into a very powerful tool that has been used to overcome many enzyme limitations. Applications include improving enzyme stability, activity, selectivity or specificity, reducing inhibition problems, and even coupling immobilization and purification, etc.

To date, many immobilization protocols have been reported. However, research is still the cornerstone of obtaining full control of the orientation of the enzyme on the support surface, and of the intensity of the support-enzyme interactions. Moreover, immobilization should not be considered an alternative to any other enzyme improvement strategy. For example, genetic and chemical tools may be utilized to produce a better enzyme that maintain improved properties after immobilization, or to improve immobilization; in both situations, alternative techniques produce an improved biocatalyst.

Thus, the efforts to design strategies involving the coupled use of immobilization with microbiological (e.g., the use of thermophilic enzymes), chemical or genetic modifications are of special interest. Enzymes are co-immobilized to catalyze cascade reactions; however, this process may produce additional complications. This special issue invites submissions (i.e., research or review papers) discussing the design of new immobilization protocols, especially when the control of the enzyme orientation is intended by design of the support, or modification of the enzyme. Papers related to the modification of immobilized enzymes, or to the modification of the support surface after enzyme immobilization, are also welcome.

Dr. Roberto Fernandez-Lafuente
Guest Editor

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