Lipase-Catalyzed Epoxy-Acid Addition and Transesterification: from Model Molecule Studies to Network Build-Up

Commercially available lipase from Pseudomonas stutzeri (lipase TL) is investigated as a biocatalyst for the formation of an acid-epoxy chemical network. Molecular model reactions are performed by reacting 2-phenyl glycidyl ether and hexanoic acid in bulk, varying two parameters: temperature and water content. Characterizations of the formed products by H-1 NMR spectroscopy and gas chromatography-mass spectrometry combined with enzymatic assays confirm that lipase TL is able to simultaneously promote acid-epoxy addition and transesterification reactions below 100 degrees C and solely the acid-epoxy addition after denaturation at T > 100 degrees C. A prototype bio-based chemical network with beta-hydroxyester links was obtained using resorcinol diglycidyl ether and sebacic acid as monomers with lipase TL as catalyst. Differential scanning calorimetry, attenuated total reflection, and swelling analysis confirm gelation of the network.

Automated summary

Commercially available lipase from Pseudomonas stutzeri (lipase TL) is studied as a biocatalyst for the formation of an acid-epoxy chemical network. The enzymatic assays confirm that lipase TL can promote acid-epoxy addition and transesterification reactions below 100 degrees C, and solely the acid-epoxy addition at temperatures above 100 degrees C. Gelation of the network is confirmed through various analyses.