AbstractThe wide application of protein fibrils as functional materials has been restricted by the limited scalability of fibrillation methods, slow kinetics, and use of expensive purified proteins. Herein, inspired by the biological cooperativity of proteins in macro-molecularly crowded environments, these restrictions have been overcome. Using ionic liquid cholinium tosylate that acts as a fibrillation agent, instantaneous production of protein fibrils is shown directly from a real and low-cost matrix, i.e. egg white. The fibrillation of egg white proteome is confirmed by microscopy, whereas the fibrillation kinetics is monitored by fluorescence changes of the thioflavin T dye and secondary structural transitions. Spectroscopic and molecular docking studies are used to identify the proteins involved and to appraise the molecular-level mechanisms ruling the proteins structural changes upon fibrillation. The obtained fibrils have enhanced mechanical stiffness and cytocompatibility, demonstrating their potential to act as improved enzyme supports.