Microorganisms or isolated enzymes can be applied as catalysts to create highly regio- and stereoselective conversions under mild conditions. Lipases (EC 188.8.131.52, triacylglycerol lipase) are lipid-hydrolysing enzymes, which are increasingly used in stereoselective reactions. Their industrial importance arises from the fact that they act on a variety of substrates promoting a broad range of biocatalytic reactions. Lipase stereoselectivity is exploited for the production of single enantiomers instead of racemic mixtures and will become snore important in the pharmaceutical and agrochemical industry because, in most cases only one of the two enantiomers has the desired activity, whereas no activity or even undesirable side effects reside in the other enantiomer. Enantiomer differentiation is due to the various diastereomeric interactions that occur between the enantiomers and the active site of the enzyme. The stereospecificity of a lipase depends largely on the structure of the substrate, interaction at the active site and on the reaction conditions. Stereoselectivity involves a wide range of factors such as differentiation of enantiotopes, differentiation of enantiomers, type of substrate, biochemical interaction of the substrate with the enzyme, steric interaction of the substrates, competition between two different substrates, nature and availability of the active site for stereoselective action, presence of water and nature of solvents based on polarity and supercritical state. This article reviews factors responsible for lipase stereoselectivity.
|Journal||World Journal of Microbiology and Biotechnology|
|Publication status||Published - Mar 2002|