Co-compartmentalization of Enzymes and Cofactors within Pickering Emulsion Droplets for Continuous-Flow Catalysis.

Abstract

Co-immobilization of enzymes and cofactors in a manner suitable for use in continuous flow catalysis remains a great challenge because of the difficulty in ensuring the free accessibility of immobilized enzymes and cofactors. Herein, we present a continuous flow catalysis system based on co-compartmentalization of enzymes and cofactors within Pickering emulsion droplets, enabling regeneration of cofactors within the droplets. As exemplified by enzyme-catalyzed ketone enantioselective reduction and enantioselective transamination, our systems exhibit long-term stability (300-400 h), outstanding total turnover number (TTN, 59204 mol mol-1 ) and several-fold enhancement in the enzyme catalytic efficiency (CEe ) in comparison to conventional biphasic reactions. As well as giving insight into the co-compartmentalization effects, our system will provide the opportunity to significantly advance continuous-flow biocatalysis towards the level of practical applications.