Recent developments in compartmentalization of chemoenzymatic cascade reactions
Daniel Kracher, Robert Kourist
Abstract
Uniting the unparalleled stereoselectivity of enzymes with the efficiency of chemical catalysis offers high product yields and atom economy while limiting downstream processing efforts. However, despite an impressive series of proof-of-concept studies, the field has not yet achieved broad applicability, especially in regard to industrial requirements. Although the focus has been mostly on proof-of-concept studies with well-established model enzymes such as lipases, transaminases, and alcohol dehydrogenases, we expect that the catalytic diversity will soon increase. However, this means that several challenges such as the stability and compatibility of the catalysts, their preference for different solvents, and their possible cross-reactivities in complex reactions need to be tackled. A powerful strategy to overcome these frequently observed ‘incompatibility problems’ of multistep cascade reactions is by physical separation of individual reaction steps through compartmentalization.