Add time:08/23/2019         Source:sciencedirect.com

The enantioselective hydrolysis of (±)-trans-4-(4′-fluorophenyl)-6-oxo-piperidin-3-ethyl carboxylate using four different microbial lipases was examined. This ester was found to be a poor substrate for most lipases, the activity achieved with the lipase from Candida antarctica (fraction B) (CAL-B) being the highest. This enzyme was purified via adsorption on hydrophobic supports and immobilized using different protocols. The enzyme immobilized on octadecyl-Sepabeads was not enantioselective at all (E=1). In contrast, glyoxyl-CAL-B preparation gave the unreacted (3S,4R)-ester in enantiomerically pure form (enantiomeric excess >99%) at 50% conversion. No decrease in the enzyme activity, or alteration in the enantioselectivity were detected, even after ten reaction cycles.

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