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Biochim Biophys Acta ; 1073(3): 493-501, 1991 Apr 09.
Article in English | MEDLINE | ID: mdl-1707672

ABSTRACT

Lipase from three different sources has been immobilised in microemulsion-based gels (MBGs) with retention of catalytic activity. Such lipase-containing MBGs prove to be novel solid-phase catalysts for use in apolar organic solvents such as n-heptane. Using these systems, preparative-scale synthesis of a wide variety of esters under mild conditions was possible with products easily isolated and obtained in high yield. Stereoselective esterification of octan-2-ol was observed for all three lipases with Chromobacterium viscosum (CV) lipase yielding product with an enantiomeric excess of 92%. Repeated usage of a CV lipase-containing MBG resulted in a visually unchanged gel whose activity was 75% of the initial value after 30 days. The sectioned MBGs were well suited for use in column flow reactors and were also found to be effective esterification catalysts at temperatures as low as -20 degrees C.


Subject(s)
Dioctyl Sulfosuccinic Acid , Emulsions , Enzymes, Immobilized/metabolism , Gelatin , Lipase/metabolism , Catalysis , Chromatography, High Pressure Liquid , Chromobacterium/enzymology , Esterification , Freezing , Molecular Structure , Octanols/chemistry , Stereoisomerism
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