Article Dans Une Revue Biomacromolecules Année : 2021

Lipase Catalyzed Epoxy-acid Addition and Transesterification: from Model Molecule Studies to Network Build-up

Résumé

Commercially available lipase from Pseudomonas stutzeri (Lipase TL) is investigated as 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 1 H NMR spectroscopy and GC-MS combined with enzymatic assays confirm that lipase TL is able to simultaneously promote acid-epoxy addition and transesterification reactions below 2 100°C and solely the acid-epoxy addition after denaturation at T > 100°C. A prototype biobased chemical network with β-hydroxyester links was obtained using resorcinol diglycidyl ether and sebacic acid as monomers and the lipase TL as catalyst. DSC, ATR-IR, and swelling analysis confirm gelation of the network.

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hal-03370512 , version 1 (08-10-2021)

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Camille Bakkali-Hassani, Quentin-Arthur Poutrel, Jakob Langenbach, Sélène Chappuis, Jonny J Blaker, et al.. Lipase Catalyzed Epoxy-acid Addition and Transesterification: from Model Molecule Studies to Network Build-up. Biomacromolecules, 2021, ⟨10.1021/acs.biomac.1c00820⟩. ⟨hal-03370512⟩
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