Novel enzymes for lipid modification

Enzymes have received considerable and increasing attention in lipid modification over the last few years. In particular, hydrolases have a high potential for applications such as the lipases-catalyzed interestification [1, 2] as an alternative for the hydrogenation of fats or the preparation of designer-fats [3].
Many enzymes, however, do not fulfill all demands of a technical process. Properties such as stability under process conditions or the chemical selectivity leave often much to improve. Together with this growing demand for tailor-made lipases goes the increasing knowledge about the molecular structures. Considerable progress in molecular biology techniques has made the cloning and expression of lipases in bacteria and the subsequent improvement by techniques of state-of-the art protein design [4] possible.
An alternative for the improvement of enzymes by protein design represents the screening for novel enzymes. The limited number of commercially available lipases can be extended by high-throughput screening in enzyme collections. Enzymes from metagenome represent a rich source for this purpose.
Herein we present an outline and the scope of both techniques that can provide novel biocatalysts for new applications in lipid-modification.
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[1] Bornscheuer U. und Kazlauskas R., 2005: Hydrolases in Organic Synthesis, Regio- and Stereoselective Biotransformations. Monographie, Wiley-VCH, Weinheim. ISBN-10: 3-527-31029-0,ISBN-13: 978-3-527-31029-6
[2] Bornscheuer U., Adamczak M, Soumanou M. M., 2002: Lipase-catalyzed synthesis of modified lipids. In: Lipids as constituents of functional foods . Bridgwater, 149-182
[3] Soumanou M., 1997: Lipase-catalyzed synthesis of structured triglycerides containing medium-chain fatty acids in sn1 and sn3-position and a long-chain fatty acid in sn2-position. Stuttgart, Univ., Diss.

[4] Bornscheuer U., Lutz, S. (Eds.), 2008: Protein Engineering Handbook. Wiley-VCH, Weinheim. ISBN-10: 352731850X, ISBN-13: 9783527318506