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Lipase Catalysis in Mixed Micelles

Von Wiley-VCH zur Verfügung gestellt

The impact of mixed micelles, a novel reaction medium, on the catalytic performance of the interfacially active enzyme lipase is reviewed. Mixed micelles incorporating nonionic surfactants mostly enhanced lipase catalysis compared to micelles with only ionic surfactants. Lipase exhibited high catalytic activities also in mixed micelles of surfactants with ionic liquids, bile salts, and substrates.


Abstract

The catalytic performance of lipase, an interfacially active enzyme, depends on the reaction medium. Novel reaction media like mixed micelles affect lipase catalysis mostly by stabilizing the lipase structure and increasing the substrate solubilization. Nonionic surfactant addition in ionic micelles formed mixed micelles and increased lipase catalysis by lowering detrimental lipase-ionic surfactant hydrophobic and electrostatic interactions. Nonionic/nonionic mixed micelles enhanced activity and enantiomeric selectivity of free lipase but reduced those for immobilized lipase. Nonconventional cationic/cationic, anionic/nonionic/ionic liquid, and substrate/nonionic mixed micelles also improved lipase catalysis. Lipase activity was high in bile salt/surfactant mixed micelles but was low in bile salt/phospholipid mixed micelle. Mixed micelles have advantages like improving lipase-substrate interaction, increasing water nucleophilicity, sometimes greater emulsion stability, and reduced product inhibition. In mixed micelles, increasing the lipase concentration can overcome the problem regarding inaccessibility of insoluble substrates.

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