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

Burcu Kaplan Türköz, Anastassia Zakhariouta, Muhsincan Sesen, Alpay Taralp*, Ali Koşar

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


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.

Original languageEnglish
Article number011006
JournalJournal of Nanotechnology in Engineering and Medicine
Issue number1
Publication statusPublished - Feb 2012


  • Bubbly cavitation
  • Hydrodynamic cavitation
  • Lysozyme
  • Lysozyme structure
  • Protein conformation

ASJC Scopus subject areas

  • General Medicine
  • General Materials Science
  • Electrical and Electronic Engineering


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