Screening for Enantioselective Lipases

Many lipolytic enzymes are enantioselective thus being able to distinguish between two enantiomers of a given racemic substrate. This property together with ample availability and comparatively easy handling makes lipolytic enzymes the most widely used class of biocatalysts in the chemical and pharmaceutical industries. However, lipase activity as well as selectivity is often negligible towards typical industrial substrates which usually do not resemble natural ones. Therefore, suitable enzymes must first be identified, usually by activity-based screening methods which, however, differ in reliability, throughput and surrogate function. Here, we describe important parameters determining the reliability and reproducibility of such screening systems for five different assays in detail. Moreover, comprehensive protocols for the synthesis of enantiopure lipase substrates and their use for screening of enantioselective lipases are provided.

Source: Springer protocols feed by Microbiology - December 9, 2016 Category: Microbiology Source Type: news