Enzymatic transesterification of urethane-bond containing ester

Here we demonstrate the feasibility and successful application of enzymes in polyurethane network synthesis as well as occurring hurdles that have to be addressed when using urethanes synthesis substrates. The enzymatic transesterification of an urethane-bond containing monofunctional ester and a model alcohol carbitol using lipases is discussed. The reaction is optimized in terms of transesterification time and temperature, the reaction solvent, the possibility of a cosolvent and the alcohol amount, the used transesterification environment, and the biocatalyst. Enzymatic cross-linking of polyurethanes can open up a pool of new possibilities for cross-linking and related polyurethane network properties due to the enzymes high enantio-, stereo-, and regioselectivity and broad substrate spectrum. [Figure not available: see fulltext.]