Roger Sheldon (1942) received a PhD in organic chemistry from the University of Leicester (UK) in 1967. This was followed by post-doctoral studies with Prof. Jay Kochi in the U.S. From 1969 to 1980 he was with Shell Research in Amsterdam and from 1980 to 1990 he was R&D Director of DSM Andeno. In 1991 he moved to his present position as Professor of organic chemistry and catalysis at the Delft University of Technology (The Netherlands). His primary research interests are in the application of catalytic methodologies—homogeneous, heterogeneous and enzymatic—in organic synthesis, particularly in relation to fine chemicals production. He developed the concepts of E factors and atom utilization for assessing the environmental impact of chemical processes.

Biocatalysis in ionic liquids

Potential applications of enzymes immobilized on/in nano materials: A review

Different methods of preparing lipases for use in organic media are critically reviewed. Solid lipase preparations can be made by typical immobilisation methods such as adsorption, entrapment, covalent coupling or cross-linking. Immobilisation is especially attractive for lipases because, in addition to the normal benefits of enzyme immobilisation, it can also lead to a considerable increase in catalytic activity, probably caused by conformational changes in the lipase molecules. Activation can be achieved, for example, using hydrophobic support materials or surfactants during the immobilisation procedure. Surfactants can also be used to solubilise lipases in organic media via the formation of hydrophobic ion pairs, surfactant-coated lipase or reversed micelles. Lipase preparation methods are discussed with regard to potential lipase inactivation and activation effects, mass transfer limitations, lipase stability and other features important for applications. The practical applications of lipases in organic media reviewed include ester synthesis, modification of triacylglycerols and phospholipids, fatty acid enrichment, enantiomer resolution, biodiesel production and acylation of carbohydrates and bioactive compounds.

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Immobilisation and application of lipases in organic media.

The application of the B-component lipase from the yeast Candida antarctica in organic synthesis is reviewed. This enzyme has been found to be a particularly efficient and robust lipase catalyzing a surprising diversity of reactions including many different regio- and enantio-selec-tive syntheses. Furthermore, the C. antarctica B-lipase is an example of an enzyme for which its specificity has been predicted based on the crystal structure and modeling of the active site region. This prediction is compared to experimental observations and a very close correlation is found.

One Biocatalyst–Many Applications: The Use of Candida Antarctica B-Lipase in Organic Synthesis

Biocatalytic transformations in ionic liquids.

The surfactant, ethyl 6-O-decanoyl glucoside, was synthesized in microemulsion systems by lipase catalysis. The microemulsions were based on the two substrates for the reaction, ethyl glucoside and fatty acid, and either the sodium salt of the fatty acid or the glucoside ester was used as surfactant. The lipase used was component B from Candida antarctica. Reduced pressure was employed to eliminate the water of condensation. The reaction yield was good, with conversion of fatty acid and ethyl glucoside reaching 77 and 96%, respectively.

Karin M. Larsson

Papers

One Biocatalyst–Many Applications: The Use of Candida Antarctica B-Lipase in Organic Synthesis

Glucoside ester synthesis in microemulsions catalyzed by Candida antarctica component B lipase