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• W2069371320 abstract "Abstract Just a drop of water : Esterification in water is possible by confining the reactants in small miniemulsion droplets protected by nonionic surfactants. A lipase located at the interface between the droplet and aqueous surroundings catalyzes the esterification and expels generated water from the reaction site (see picture). High yields of the ester can be obtained after short reaction times under ambient conditions. magnified image Monoesters of various linear carboxylic acids (C7–C12) with ω ‐phenyl‐labeled primary alcohols (C1–C5) were synthesized in aqueous miniemulsions with various lipases as biocatalysts. The reactants were dispersed in an aqueous solution of a nonionic surfactant to form long‐term stable miniemulsions. The esterification of all of the systems could be catalyzed by the applied enzyme and yielded significant conversions of about 90 %. The hydrophilicity of the reactants and the specificity of the enzyme toward the substrates determine the reaction velocity and the final conversion. As a model system the reaction of nonanoic acid and 3‐phenylpropanol was extensively studied. Among various lipases, Lipase PS was determined to be the most effective, and for this reaction the parameters were optimized. A maximum conversion of 80 % could be obtained in less than one hour of reaction time. In comparison with an acid‐catalyzed esterification performed in miniemulsion with the same reaction parameters, the enzyme‐catalyzed reaction showed a significantly faster conversion. The reactions proved that the application of the miniemulsion technique enables efficient direct enzyme‐catalyzed esterification reactions from carboxylic acids and alcohols in the presence of large amounts of water." @default.
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• W2069371320 date "2009-02-12" @default.
• W2069371320 modified "2023-10-18" @default.
• W2069371320 title "Enzymatic Esterification in Aqueous Miniemulsions" @default.
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• W2069371320 doi "https://doi.org/10.1002/chem.200801691" @default.
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