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Sterilization mechanism of nitrogen gas plasma: induction of secondary structural change in protein
Author(s) -
Sakudo Akikazu,
Higa Masato,
Maeda Kojiro,
Shimizu Naohiro,
Imanishi Yuichiro,
Shintani Hideharu
Publication year - 2013
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/1348-0421.12061
Subject(s) - protein secondary structure , circular dichroism , plasma , sterilization (economics) , chemistry , analytical chemistry (journal) , fourier transform infrared spectroscopy , biophysics , infrared spectroscopy , chromatography , biology , crystallography , biochemistry , organic chemistry , physics , quantum mechanics , monetary economics , economics , foreign exchange market , foreign exchange
The mechanism of action on biomolecules of N 2 gas plasma, a novel sterilization technique, remains unclear. Here, the effect of N 2 gas plasma on protein structure was investigated. BSA, which was used as the model protein, was exposed to N 2 gas plasma generated by short‐time high voltage pulses from a static induction thyristor power supply. N 2 gas plasma‐treated BSA at 1.5 kilo pulses per second showed evidence of degradation and modification when assessed by Coomassie brilliant blue staining and ultraviolet spectroscopy at 280 nm. Fourier transform infrared spectroscopy analysis was used to determine the protein's secondary structure. When the amide I region was analyzed in the infrared spectra according to curve fitting and Fourier self‐deconvolution, N 2 gas plasma‐treated BSA showed increased α‐helix and decreased β‐turn content. Because heating decreased α‐helix and increased β‐sheet content, the structural changes induced by N 2 gas plasma‐treatment of BSA were not caused by high temperatures. Thus, the present results suggest that conformational changes induced by N 2 gas plasma are mediated by mechanisms distinct from heat denaturation.