In this initial study, the effect of hydrodynamic flow on lysozyme structure and function was investigated using a microchannel device. Protein was subjected to bubbly cavitation as well as noncavitating flow conditions at pH 4.8 and 25 °C. Interestingly, time course analyses indicated that the secondary structure content, the hydrodynamic diameter, and enzymatic activity of lysozyme were unaffected by cavitation. However, noncavitating flow conditions did induce a decrease of the hydrodynamic diameter. The corresponding structural change was subtle to the extent that bioactivity was marginally suppressed. Moreover, native diameter and bioactivity could be fully restored following a brief period of ultrasonication. The findings encouraged further study of various hydrodynamic flow conditions in order to better ascertain the potential risks and benefits of invasive hydrodynamic cavitation in medicine. The results also served to highlight the counter-intuitive notion that proteins need not necessarily be denatured in high-shear media, risks that typically correlate well with forcefully agitated solutions.