Cold Plasma Applications in Protein Modification and Characterization

Cold plasma, a partially ionized gas generated under atmospheric or reduced pressure and maintained at near-ambient temperatures, has emerged as a versatile non-thermal technology for altering protein structure and function. Reactive oxygen and nitrogen species generated within the plasma interact with amino acid side chains, inducing oxidation, cross-linking and unfolding without extensive heat damage. These modifications can enhance emulsifying capacity, gelation, solubility and digestibility of food proteins, reduce allergenicity and modulate enzymatic activity. In parallel, plasma-induced structural changes are exploited in protein characterisation, where altered secondary and tertiary structures facilitate detection of conformational epitopes and mapping of reactive sites by techniques such as circular dichroism and mass spectrometry. The breadth of applications spans food processing—improving texture, shelf life and safety—to biotechnology and proteomics, where cold plasma serves both as a preparative tool for tailored protein modification and as an analytical probe of protein stability and interaction.

Research from Nature Portfolio

Recent studies have demonstrated the capacity of cold plasma to reduce allergenicity in major peanut proteins. Treatment of whole peanuts and defatted flour with an atmospheric air discharge reactor led to dose-dependent decreases in solubility of key allergens, accompanied by alterations in secondary structure as revealed by circular dichroism. Competitive immunoassays confirmed reductions in antigenic binding of up to two-thirds, indicating that plasma-generated reactive species can selectively modify epitope regions. These findings establish a mechanistic link between plasma-induced structural perturbations and functional reduction of food allergens, offering a promising route to hypoallergenic products without chemical additives.

Cold Plasma Applications in Protein Modification and Characterization publication trend

The graph below shows the total number of articles in cold plasma applications in protein modification and characterization across all publications each year (not limited to Nature Index journals).

Technical terms

Cold plasma: A partially ionized gas at near-ambient temperature containing electrons, ions and neutral species capable of inducing chemical modifications.

Dielectric barrier discharge (DBD): A method for generating cold plasma by applying high voltage across insulating barriers, producing uniform reactive species.

Reactive oxygen species (ROS): Highly reactive molecules derived from oxygen that can oxidise amino acid side chains and induce protein cross-linking.

Surface hydrophobicity: A measure of exposed non-polar regions on a protein’s surface, influencing interactions with lipids and other proteins.

SDS-PAGE: A gel electrophoresis technique that separates proteins by molecular weight under denaturing conditions, used to assess fragmentation and cross-linking.

References

1. Dielectric barrier discharge cold plasma treatment of pork loin: Effects on muscle physicochemical properties and emulsifying properties of pork myofibrillar protein. LWT (2022).
2. Impact of cold plasma processing on major peanut allergens. Scientific Reports (2020).
3. Effect of High Voltage Cold Plasma on Oxidation, Physiochemical, and Gelling Properties of Myofibrillar Protein Isolate from Asian Sea Bass (Lates calcarifer). Foods (2021).
4. Changes in Biochemical Properties and Activity of Trypsin-like Protease (Litopenaeus vannamei) Treated by Atmospheric Cold Plasma (ACP). Foods (2022).