Abstract
The kinetic resolution of 3-hydroxy fatty acid esters C8:0 to C16:0 with Candida antarctica lipase B shows common plots of the enantiomeric excesses of the product and substrate, respectively, versus the conversion and an enantiomeric ratio E of 27 calculated from ee(p). Differences in E, either calculated from the products or the substrates, could be explained by competing oligomerization as a second substrate-consuming process. This reaction is slow compared to acylation, and the remaining enantiomer was oligomerized.
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