Enzymatic transesterification of urethane-bond containing ester

Abstract

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 urethanebond 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.

A comprehensive review on the pancreatic lipase inhibitory peptides: A future anti-obesity strategy

“…This so-called 'lid' was observed to form an α-helical structure covering the active site. This catalytic process starts with acylation leading to the formation of the acyl-enzyme complex via a nucleophilic attack at the activated serine on the carbonyl C-atom of the substrate ester bond and further diacylation reconstruct the enzyme during the second step of the reaction and releasing the substrate from the serine and thereby finalizing the hydrolysis reaction [40].…”