Nonthermal plasma (NTP) is an advanced technology that has gained extensive attention because of its capacity for decontaminating food from both biological and chemical sources. Plasma‐activated water (PAW), a product of NTP's reaction with water containing a rich diversity of highly reactive oxygen species (ROS) and reactive nitrogen species (RNS), is now being considered as the primary reactive chemical component in food decontamination. Despite exciting developments in this field recently, at present there is no comprehensive review specifically focusing on the comprehensive effects of PAW on food safety and quality. Although PAW applications in biological decontamination have been extensively evaluated, a complete analysis of the most recent developments in PAW technology (e.g., PAW combined with other treatments, and PAW applications in chemical degradation and as curing agents) is nevertheless lacking. Therefore, this review focuses on PAW applications for enhanced food safety (both biological and chemical safeties) according to the latest studies. Further, the subsequent effects on food quality (chemical, physical, and sensory properties) are discussed in detail. In addition, several recent trends of PAW developments, such as curing agents, thawing media, preservation of aquatic products, and the synergistic effects of PAW in combination with other traditional treatments, are also presented. Finally, this review outlines several limitations presented by PAW treatment, suggesting several future research directions and challenges that may hinder the translation of these technologies into real‐life applications.
We used yeast proteome microarrays (∼5800 purified proteins) to conduct a high-throughput and systematic screening of PI5P-interacting proteins with PI5P-tagged fluorescent liposomal nanovesicles. Lissamine rhodamine B-dipalmitoyl phosphatidylethanol was incorporated into the liposome bilayer to provide the nanovesicles with fluorescence without any encapsulants, which not only made the liposome fabrication much easier without the need for purification but also improved the chipprobing quality. A special chip assay was washed very gently without the traditional spin-dry step. Forty-five PI5P-interacting proteins were identified in triplicate with this special chip assay. Subsequently, we used flow cytometry to validate these interactions, and a total of 41 PI5P-interacting proteins were confirmed. Enrichment analysis revealed that these proteins have significant functions associated with ribosome biogenesis, rRNA processing, ribosome binding, GTP binding, and hydrolase activity. Their component enrichment is located in the nucleolus. The InterPro domain analysis indicated that PI5P-interacting proteins are enriched in the P-loop containing nucleoside triphosphate hydrolases domain (P-loop). Additionally, using the MEME program, we identified a consensus motif (IVGPAGTGKSTLF) that contains the Walker A sequence, a well-known nucleotide-binding motif. Furthermore, using a quartz crystal microbalance, both the consensus motif and Walker A motif showed strong affinities to PI5P-containing liposomes but not to PI5P-deprived liposomes or PI-containing liposomes. Additionally, the glycine (G6) and lysine (K7) residues of the Walker A motif (-GPAGTG 6 K 7 S-) were found to be critical to the PI5P-binding ability. This study not only identified an additional set of PI5P-interacting proteins but also revealed the strong PI5P-binding affinity (K d = 1.81 × 10 −7 M) of the Walker A motif beyond the motif's nucleotide-binding characteristic.
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