Plasma-activated water (PAW) contains multiple active species that alter the structure of myofibrillar protein (MP) to enhance their gel properties. This work investigated the impact of PAW on the oxidation of cysteine in MP by label-free quantitative proteomics. PAW treatment caused the oxidation of 8241 cysteine sites on 2815 proteins, and structural proteins such as nebulin, myosin XVIIIB, myosin XVIIIA, and myosin heavy chain were susceptible to oxidation by PAW. Bioinformatics analysis, including Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, subcellular localization, and STRING analysis, indicated that these proteins with differential oxidation sites were mainly derived from the cytoplasm and membrane, and were involved in multiple GO terms and KEGG pathways. This is one of the first reports of the redox proteomic changes induced by PAW treatment, and the results are useful for understanding the possible mechanism of PAW-induced oxidation of MP.
This study investigated the effects of plasma-activated water (PAW) generated with argon at discharge times of 0, 4, 8, 12, and 16 min on the gel properties and structures of chicken myofibrillar protein (MP). Under treatments of 8, 12, and 16 min, both the gel strength and water retention capacity of MP significantly improved, with the gel strength (0.53 N) peaking at 16 min and the lowest cooking loss（30.38 %）. As the treatment time increased from 0 to 16 min, the storage modulus also gradually increased. Results from low-field nuclear magnetic resonance indicated a slowing of water proton mobility, with the proportion of bound water rising from 0.26 % (0 min) to 0.52 % at 16 min. Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy and scanning electron microscopy confirmed PAW's alteration of MP's secondary and tertiary structures and gel microstructure. Additionally, this study explored the influence of argon PAW's primary active species on MP from a molecular docking perspective·H2O2 could form hydrogen bonds with MP, while O3 and NO2‾could interact via both hydrogen bonds and electrostatic interactions. Thus, PAW can alter protein structure and enhance MP's functional properties, providing insights for applying cold plasma in processing chicken gel products.