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- W2995340141 abstract "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." @default.
- W2995340141 created "2019-12-26" @default.
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- W2995340141 date "2019-12-23" @default.
- W2995340141 modified "2023-10-17" @default.
- W2995340141 title "Lipase-Catalyzed Transamidation of Urethane-Bond-Containing Ester" @default.
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- W2995340141 doi "https://doi.org/10.1021/acsomega.9b03203" @default.
- W2995340141 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6990427" @default.
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