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Catalysts 2013, 3(2), 401-417; doi:10.3390/catal3020401
Review

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

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Received: 18 January 2013 / Revised: 11 March 2013 / Accepted: 26 March 2013 / Published: 9 April 2013
(This article belongs to the Special Issue Biomimetic Catalysts)
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Abstract

Several important enzymatic reactions occurring in nature, such as, e.g., the digestion of fat, proceed only at the interface of two immiscible phases. Typically, these systems consist of an organic substrate, dispersed in an aqueous continuous phase, with a specialized enzyme capable of working at the interface. For adopting such a system for organic synthesis, a stable heterophase system with a large interfacial area is required. These prerequisites can be found in so-called miniemulsions. Such liquid-liquid heterophase systems feature droplets with sizes smaller than 500 nm, and more importantly, these emulsions do not suffer from Ostwald ripening, as conventional emulsions do. Consequently, the droplets show long-term stability, even throughout reactions conducted in the droplets. In this review, we will briefly discuss the physicochemical background of miniemulsions, provide a comprehensive overview of the enzymatically catalyzed reactions conducted in miniemulsions and, as data are available, to compare the most important features to conventional systems, as reverse microemulsions, (macro)emulsions and solvent-based systems.
Keywords: enzymes; emulsion; miniemulsion enzymes; emulsion; miniemulsion
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Weiss, C.K.; Landfester, K. Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action. Catalysts 2013, 3, 401-417.

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