Lipase-Catalyzed Transamidation of Urethane-Bond-Containing Ester

Significant improvement in mechanical properties and shape recovery in polyurethanes can be obtained by cross-linking, usually performed in a traditional chemical fashion. Here, we report model studies of enzymatic transamidations of urethane-bond-containing esters to study the principles of an enzymatic build-up of covalent cross-linked polyurethane networks via amide bond formation. The Lipase-catalyzed transamidation reaction of a urethane-bond-containing model ester ethyl 2-(hexylcarbamoyloxy)propanoate with various amines is discussed. A side product was formed, that could be successfully identified, and its synthesis reduced to a minimum (<1%). Furthermore, a noncatalyzed transamidation that is performed without CalB as the catalyst could be observed. Both observations are due to the known high reactivity of amines with urethane bonds.