Laser ablation of the protein lysozyme

Jørgen Schou, Stela Canulescu, Salvatore Amoruso, X. Wang, R. Bruzzese, Andreea Matei, Catalin Constantinescu, M. Dinescu

Research output: Contribution to conferenceConference abstract for conferenceResearchpeer-review


Lysozyme is a well-known protein, which is used in food processing because of its bactericidal properties. The mass (14307 amu) is in the range in which it easily can be monitored by mass spectrometric methods, for example by MALDI (Matrix assisted laser desorption ionization). We have recently produced thin films of average thickness up to 300 nm, which not only contained a significant amount of intact molecules, but also maintained the bioactivity. These films were produced by a nanosecond laser in the UV regime at 355 nm with 2 J/cm2. The surprising fact that these molecules can be transferred to a substrate as intact molecules by the violent laser impact ( up to 50 mJ/pulse) has not yet been understood. One issue is that up to 150 ng/pulse is removed by the laser, and much of the material is ejected from the target in relatively large chunks. We have explored as well the excitation mechanics by laser impact. Samples of pressed lysozyme prepared in the same manner as in ns-experiments have been irradiated at 527 nm with >>300-fs pulses and at a similar fluence as in ns ablation. Even though the pulse energy was much smaller, there was a considerable ablation weight loss of lysozyme from each shot. This is the first time the ablation by fs-lasers of a protein has been recorded quantitatively. Films of lysozyme produced by fs-laser irradiation were analyzed by MALDI and a significant number of intact
Original languageEnglish
Publication date2012
Number of pages1
Publication statusPublished - 2012
EventDanish Physical Society Annual Meeting 2012 - Nyborg, Denmark
Duration: 19 Jun 201220 Jun 2012


ConferenceDanish Physical Society Annual Meeting 2012
Internet address


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