Epoxy Vitrimer Materials by Lipase-Catalyzed Network Formation and Exchange Reactions

The preparation and reprocessing of an epoxy vitrimer material is performed in a fully biocatalyzed process wherein network formation and exchange reactions are promoted by a lipase enzyme. Binary phase diagrams are introduced to select suitable diacid/diepoxide monomer compositions overcoming the limitations (phase separation/sedimentation) imposed by curing temperature inferior than 100 degrees C, to protect the enzyme. The ability of lipase TL, embedded in the chemical network, to catalyze efficiently exchange reactions (transesterification) is demonstrated by combining multiple stress relaxation experiments at 70-100 degrees C and complete recovery of mechanical strength after several reprocessing assays (up to 3 times). Complete stress relaxation ability disappears after heating at 150 degrees C, due to enzyme denaturation. Transesterification vitrimers thus designed are complementary to those involving classical catalysis (e.g., using the organocatalyst triazabicyclodecene) for which complete stress relaxation is possible only at high temperature.

Automated summary

In this study, a biocatalyzed process utilizing a lipase enzyme was used to prepare and reprocess an epoxy vitrimer material. By introducing binary phase diagrams and selecting suitable monomer compositions, the limitations imposed by low curing temperature were overcome, thus protecting the enzyme. The lipase TL embedded in the chemical network efficiently catalyzed exchange reactions, demonstrated by stress relaxation experiments and complete recovery of mechanical strength after reprocessing assays.