A combined low‐pressure hydrogen peroxide evaporation plus hydrogen plasma treatment method for sterilization − Part 2: An intercomparison study of different biological systems | Zendy

Lackmann JanWilm | Zendy; Fiebrandt Marcel | Zendy; Raguse Marina | Zendy; Kartaschew Konstantin | Zendy; Havenith Martina | Zendy; Bandow Julia E. | Zendy; Moeller Ralf | Zendy; Awakowicz Peter | Zendy; Stapelmann Katharina | Zendy

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A combined low‐pressure hydrogen peroxide evaporation plus hydrogen plasma treatment method for sterilization − Part 2: An intercomparison study of different biological systems

Author(s) -

Lackmann JanWilm,

Fiebrandt Marcel,

Raguse Marina,

Kartaschew Konstantin,

Havenith Martina,

Bandow Julia E.,

Moeller Ralf,

Awakowicz Peter,

Stapelmann Katharina

Publication year - 2017

Publication title -

plasma processes and polymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.644

H-Index - 74

eISSN - 1612-8869

pISSN - 1612-8850

DOI - 10.1002/ppap.201600199

Subject(s) - hydrogen peroxide , sterilization (economics) , hydrogen , plasma , chemistry , raman spectroscopy , spore , response surface methodology , materials science , chemical engineering , chromatography , biochemistry , organic chemistry , microbiology and biotechnology , biology , physics , optics , quantum mechanics , monetary economics , economics , foreign exchange market , engineering , foreign exchange

Low‐pressure plasmas are a promising alternative to modern sterilization processes. As plasma is a surface process, multilayered stacks of spores are a crucial challenge to overcome. Here, a combined process of condensed hydrogen peroxide and hydrogen plasma is analyzed for its efficacy against various spore concentrations showing a clear increase in efficacy using a combined process compared to the two steps used separately. Besides spores, protein contaminations are a major issue in clinics and the combined process is investigated for protein removal efficiency using the well‐established BSA model. Furthermore, RNase A serves as a difficult‐to‐inactivate protein model to investigate protein inactivation efficiency. Finally, inactivation mechanisms of RNase A with a special focus on sulfur‐based modifications are investigated using Raman spectroscopy.

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