Autor: |
Braner, Markus, Zielonka, Stefan, Auras, Sylvia, Hüttenhain, StefanH. |
Předmět: |
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Zdroj: |
Synthetic Communications; Apr2012, Vol. 42 Issue 7, p1019-1025, 7p, 3 Graphs |
Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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