Lipases Enantioselectivity Alteration by Immobilization Techniques
Jose M. Palomo
Affiliation: Departamento de Biocatalisis.Instituto de Catalisis (CSIC), Campus UAM Cantoblanco, 28049 Madrid, Spain.
Lipases are the most used enzymes as biocatalyst in the resolution of chiral compounds. However many times the selectivity towards different intermediates is very low. A simple strategy has recently been reported to permit greatly enhancing the lipase selectivity. The strategy based on the great conformational changes of these enzymes during catalysis consists in the preparation of a library of lipase biocatalysts by using different immobilization protocols that may permit to immobilize them via different orientations, with different rigidity or generating different environments. This review examines how this solid phase strategy has permitted greatly modulated the enantioselectivity of lipases in kinetic resolutions of racemic mixtures.
Keywords: Conformational changes, lipases, immobilization, modulation, kinetic resolution, racemic mixtures, enantioselectivity
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