Lipase-Catalyzed Epoxy–Acid Addition and Transesterification: from Model Molecule Studies to Network Build-Up
Authors/Creators
- 1. Molecular, Macromolecular Chemistry, and Materials, ESPCI Paris, PSL University, CNRS, Paris 75005, France
- 2. Department of Materials and Henry Royce Institute, The University of Manchester
- 3. i-Composites Lab, Department of Materials Science and Engineering, Department of Mechanical and Aerospace Engineering, Monash University, Clayton 3800, Australia
Description
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 1H 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 °C and solely the acid–epoxy addition after denaturation at T > 100 °C. A prototype bio-based chemical network with β-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.