Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
71099 | Journal of Molecular Catalysis B: Enzymatic | 2007 | 4 Pages |
Abstract
A study on a chemoenzymatic synthesis of model α-hydroxyamide was performed. Special attention was paid to the optimization of the enzymatic process, both on the selection of enzyme and cosolvent. An intriguing influence of cosolvent on the enantioselectivity of Wheat Germ Lipase and Amano PS Lipase catalyzed hydrolysis was observed, as the results obtained proved that enzyme's enantioselectivity is directly correlated with cosolvent's hydrophobicity. In the best example (Wheat Germ lipase, Et2O used as a cosolvent), the reaction proceeded with E = 55, and the target compound was obtained in 33% yield with 92.7%ee.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Wiktor Szymanski, Ryszard Ostaszewski,