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

The preparation and reprocessing of epoxy vitrimer materials are performed using a fully biocatalyzed process with the aid of a lipase enzyme. Binary phase diagrams are used to select suitable monomer compositions to overcome the limitations imposed by low curing temperatures (below 100 degrees C) and protect the enzyme activity. The lipase TL embedded in the chemical network exhibits efficient catalysis for exchange reactions, as demonstrated by stress relaxation experiments and mechanical strength recovery after reprocessing assays.