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Conformational Engineering of Lipases via Directed Immobilisation: Improving the Resolution of Chiral Drugs

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Abstract:

Lipases are the most used enzymes as biocatalyst in the resolution of chiral compounds. To improve the results, many different techniques have been proposed (protein engineering, random mutagenesis with selection pressure, screening in the nature, etc). However, bearing in mind that enzymes are commonly utilised in the industry in an immobilised form, a simple strategy has recently been reported to permitting greatly improvement in the results using lipases. The strategy is based in the dramatic conformational changes of lipases during catalysis and the use of a library of immobilisation protocols that may permit to immobilise the lipases via different orientations, with different rigidity levels or generating different environments. This may be combined with the experimental conditions to significantly alter the results. In this review, we include some examples, with lipases from different sources and different compounds, where the enantiomeric ratio has been moved from almost negligible value to more than 100 just by this very simple strategy, the so-called "conformational engineering of lipases".

Keywords: candida antarctica (cal-a); candida rugosa; conformational engineering; glycerol-ester-hydrolase; immobilisation strategies; rhizomucor (mucor) miehei

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/156720305774330494

Affiliations: Departamento de Biocatalisis. Instituto de Catalisis (CSIC), Departamento de CristalografĂ­a. Instituto de Quimica-Fisica (Rocasolano-CSIC), Campus UAM Cantoblanco, 28049 Madrid, Spain.

Publication date: October 1, 2005

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