Amyloid fibrils are stable protein aggregates that have a highly ordered beta-sheet secondary structure. There is a growing interest in using protein amyloid fibrils (termed nanofibrils) for use in nanomaterials and food applications. Nanofibrils can be formed from many different proteins and under a variety of conditions, although the mechanism of their assembly is unclear. This study focused on comparing the effects of microwave and dry-bath heating to induce the formation of nanofibrils using hen egg-white lysozyme as a model for human lysozyme. In this study, it was found that using microwave versus conventional heating affected the kinetics, morphology, and peptide composition of hen egg white lysozyme nanofibrils. These results further highlight the sensitivity of nanofibril formation to environmental conditions and indicate that microwave heating might be used to engineer nanofibrils with unique properties.