This article reviews the application of enzymes in lipid modification. Lipases are the most established biocatalysts used for the synthesis of structured triacylglycerols, fats, and margarine and for the release of flavoring fatty acids for food applications. In addition, the various enzymes, such as P450 monooxygenases, hydratases, lipoxygenases, and certain lyases, used for oxyfunctionalization and the phospholipases used for degumming are covered. Basic aspects of enzyme catalysis and the modern tools used for their discovery and improvement by protein engineering provide insight into how suitable biocatalysts can be identified and optimized for an application. In addition to isolated enzymes, whole-cell engineered microorganisms are also used for lipid modification. Thus, the polyunsaturated fatty acid EPA (eicosapentaenoic acid) can be produced in a yeast using sugar as a renewable resource.

Enzymes in Lipid Modification

Organic and bioorganic reactions in microemulsions

Bioorganic reactions in microemulsions: the case of lipases.

Lipase from Rhizopus sp. has been immobilized covalently on tresyl activated silica. Three different coupling media were evaluated: aqueous buffer, n-hexane, and a microemulsion based on n-hexane, aqueous buffer, and the nonionic surfactant triethylene glycol monododecyl ether. In addition, coupling via a very long, hydrophilic spacer arm, polyethylene glycol 1500 (PEG 1500), was compared with attachment to the silica via a short silane bridge only. The enzyme preparations were tested in hydrolysis and transesterification reactions. In the hydrolysis no marked differences in activity were found between the coupling media used. In the transesterification, on the other hand, the choice of immobilization medium had a very large effect on lipase activity, the preparation from microemulsion being the most active one. The use of the hydrophilic spacer had a large effect on activity in the hydrolysis reaction. Whereas direct coupling gave an activity of immobilized lipase of 26-34% of that of free enzyme, depending on the reaction medium, lipase bound via the spacer exhibited 56-67% activity. The latter values are considerably higher than previously reported in the literature for covalently immobilized lipase. The hydrophilic spacer had no effect on enzyme activity in the transesterification, however, a fact which is attributed to the hydrophobic medium of this reaction. The spacer is incompatible with the reaction medium and will, therefore, adsorb on the particles rather than stretch out into the bulk phase. The stability of the bound lipase was extremely good, no loss in activity being observed after a period of three weeks in aqueous solution of 37 degrees C.

Covalent immobilization of lipase in organic solvents.

A series of triglycerides having varying degrees of unsaturation of the acyl groups has been transesterified with stearic acid. It is shown that the position of the double bonds, not the degree of unsaturation, is the decisive factor in the rate of reaction. A A-6 double bond, which is present in petroselinic acid and ylinolenic acid, prevents reaction. Unsymmetrical triglycerides containing only one acyl group with δ-6 unsaturation reacts regiospecifically with the A-6 acyl group facing away from the enzyme. γ-Linolenic acid can be incorporated into an unhindered triglyceride through lipase catalyzed transesterification, indicating that the active site can in fact accommodate a δ-6 fatty acid, although not the corresponding triglyceride.

Lipase Catalyzed Transesterification of Unsaturated Lipids in a Microemulsion

Lipase Catalyzed Hydrolysis

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Lipase Catalyzed Hydrolysis