Reversibility of functional and structural changes of lysozyme subjected to hydrodynamic flow

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Official URL: http://dx.doi.org/10.1115/1.4006363

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 non-cavitating flow conditions at pH 4.8 and 25ºC. Interestingly, time-course analyses indicated that the secondary structure content, the hydrodynamic diameter and enzymatic activity of lysozyme were unaffected by cavitation. However, non-cavitating 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. These findings encouraged further study to better ascertain the risks and benefits of invasive hydrodynamic cavitation in medicine. The results also served to highlight the counterintuitive notion that proteins need not necessarily be denatured in high-shear media, risks that typically correlate well with forcefully agitated solutions.