Enzyme co-immobilization: Always the biocatalyst designers' choice ... or not? ...

The increasing relevance of cascade reactions in biocatalysis has sparked a great interest for enzyme coimmobilization. Enzyme co-immobilization allows access to some kinetic advantages that in some instances are necessary to get the desired product, avoiding side-reactions. However, the kinetic effect is very relevant mainly at the initial reaction rates, while it may be less relevant in the whole reaction course, depending on the kinetic parameters of the involved enzymes. This review not only critically discusses the advantages but also the drawbacks of enzymes co-immobilization: immobilization on the same support and surface, under similar conditions, discarding the whole biocatalyst when one of the co-immobilized enzymes is inactivated. We will discuss when co-immobilization is almost compulsory, when the advantages of co-immobilization may not be enough to compensate their problems and when it should be fully discarded. The co-immobilization of cofactors and enzymes bears special interest, as this can open up the opportunity to the building of artificial cells and extremely complex one-pot transformations. Finally, some recent strategies to overcome some the co-immobilization problems will be presented.

Automated summary

Enzyme co-immobilization offers kinetic advantages but also drawbacks, such as the need to discard the entire biocatalyst if one enzyme becomes inactivated. The co-immobilization of cofactors and enzymes is of particular interest for the construction of artificial cells and complex one-pot transformations.