Résumé
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 °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 °C and complete recovery of mechanical strength after several reprocessing assays (up to 3 times). Complete stress relaxation ability disappears after heating at 150 °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.